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ORGANIZADOR GENERAL

Dra. Patricia Gorocica Rosete

Instituto Nacional de Enfermedades Respiratorias Ismael Cosio Villegas

gorocicap@gmail.com

Tel 54871705

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31 DE JULIOA L 2 DE AGOSTO 2013

PALACIO DE MEDICINA

CIUDAD DE MEXICO

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CONSEJO DIRECTIVO DE LA SOCIEDAD

LATINOAMERICANA DE GLICOBIOLOGIA

Dr. Ivn Martnez Duncker R PRESIDENTE

Facultad de Ciencias, Universidad Autnoma del Estado de Morelos, Mxico

Dra. Blanca Ortiz Quintero, SECRETARIO

Instituto Nacional de Enfermedades Respiratorias Ismael Cosio Villegas

,Mxico

Dra. Patricia Gorocica Rosete, TESORERO

Instituto Nacional de Enfermedades Respiratorias Ismael Cosio Villegas, Mxico

Dr. Hctor Mora Montes, VOCAL

Departamento de Biologa, Universidad de Guanajuato, Mxico

Dr. Julio Reyes Leyva , VOCAL

Centro de Investigacin Biomdica de Oriente (CIBIOR) , Puebla, Mxico

Dr. Jos Luis Montiel Hernndez, VOCAL

Facultad de Farmacia, Universidad Autnoma del Estado de Morelos, Mxico

Dr. Miguel ngel Mayoral Chvez VOCAL

Facultad de Medicina, Universidad Benito Jurez de Oaxaca, Mxico

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PROGRAMA DE INAGURACION

PRESENTACIN DE LA SOCIEDAD LATINOAMERICANA DE

GLICOBIOLOGA

Dr. Ivn Martnez Drunker

Presidente de la Sociedad

Mesa de Honor

Dr. Juan Jos Hicks Gmez

General de Polticas de Investigacin en Salud en la CCINSHAE

Dr. Jorge Salas Hernndez

Director del Instituto Nacional de Enfermedades Respiratorias Ismael Cosio

Villegas

Dr. Enrique Graue Weichers

Director de Facultad de Medicina de la UNAM.

Dr. Gabriel Cuevas Gonzlez Bravo.

Director del Instituto de Qumica de la UNAM

Dr. Octavio Tonahiu Ramrez Reivich

Director del Instituto de Biotecnologa de la UNAM

Dra. Patricia Gorocica Rosete

Coordinador general del Congreso

Dr. Edgar Zenteno Galindo

Miembro Honorario de la Sociedad

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PATRCINADORES

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PROGRAMA DETALLADO DEL CONGRESO

MIERCOLES 31 DE JULIO

Curso precongreso

TEMA EXPOSITOR

"Estructura de glicanos, nomeclatura y papel biolgico" Dra. Blanca ESPINOSA, INER

"Biosntesis de glicanos y las consecuencias por el deficit en su biosntesis"

Dr. Miguel Angel MAYORAL, UABJO

"Funcin de los glicanos en la invasin de microrganismos " Dr. Hctor MORA . U DE GTO.

"Papel de los glicanos en la respuesta inmune" Dr. Ricardo LASCURAIN. UNAM

"Estrategas generales para abordar el estudio de glicanos Dr. Antonio Serrato. INER

Herramientas qumicas en la Glicobiologa. Dra. Yobana PREZ. UABJO

"Lectinas como herramientas para el estudio de la Glicobiologia"

Dr. Pedro Hernandez Cruz. UABJO

"Determinacin de Carbohidratos por Cromatografa Inica mediante Deteccin Amperomtrica

Q.I Marco Antonio BUSTAMENTE ACEVEDO. METROHM

CEREMONIA INAGURAL

SESION GENERAL 1 CONFERENCIAS INAGURALES

AUDITORIO DR.

GUSTAVO BAZ PRADA

Coordinador: Dr. Ivn Martnez Druncker

"Biological Roles of Glycans: a Look Back Over the Decades"

Dr. Ajit VARKI. University of California, San Diego, EUA

Tools for identifying new human glycosylation disorders

Dr. Hudson FREEZE. Sanford Burnham Institute, EUA.

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COCKTAIL DE BIENVENIDA PATIO CENTRAL

JUEVES 1 DE AGOSTO

SYMPOSIUM "TECNICAS PARA EL ESTUDIO DE LA GLICOBIOLOGIA"

AUDITORIO DR. GUSTAVO

BAZ PRADA

Coordinador: Dr. Edgar Zenteno

"Bioingenieria aplicada (Nucleasas con dedos de Zinc y modificacione de genomas en sistemas eucarioticos)."

MsC David Pierre Pillon. Sigma Aldrich de Mxico

Uso de la espectrometra de masas para la identificacin de residuos de carbohidratos

Dra. Victoria PANDO. Instituto Nacional de Salud Publica , Mxico

Metabolic Glycoengineering; Implications in the Intake of Azide Non-Natural Sugar Analogs

Dr. Rubn ALMARAZ. University of Michigan , EUA

La interaccin CH/H, base del reconocimiento protena carbohidrato y su aplicacin a la sntesis de catalizadores.

Dr. Gabriel CUEVAS Instituto de Qumica de la UNAM.

La citometra de flujo como herramienta para el estudio de la glicobiologa

Dra. Lourdes A. ARRIAGA Pizano. Centro Mdico Nacional Siglo XXI,Mxico

Glicosilacin de protenas en sistemas de cultivo celular.

Dr. Antonio SERRATO . Departamento de Bioqumica, INER

COFFE BREAK

SESION GENERAL 2 GLICOBIOLOGIA MEDICA

Coordinador: Dr. Hector Mora AUDITORIO DR. GUSTAVO

BAZ PRADA

Defectos gneticos de glicosilacin

Dr. Ivn MARTNEZ DUNCKER. Fac, Ciencias,UAEM, Mxico

Glycobiology in skeletal dysplasias associated to Congenital Disorder of Glycosylation"

Dra. Carla ASSTEGIANO. Universidad Nacional de Crdoba,Argentina.

COMIDA

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SESION GENERAL 3 GLICOBIOLOGIA DE LA ENFERMEDADES INFECCIOSAS

AUDITORIO DR. GUSTAVO

BAZ PRADA

Coordinador: Dr. Jos Luis Montiel

"El zimozn como potente inductor de la respuesta inmunitaria en el mosquito Anopheles albimanus"

Dr. Humberto LANZ. Instituto Nacional de Salud Publica-CISEI

Glicobiologa de la pared celular de Candida albicans

Dr. Hctor MORA MONTES. Universidad de Guanajuato, Mxico

"Fungal cell wall glycococonjugates as virulence factors: true or false?"

Dra. Leila M. LOPES-BEZERRA. Universidade do Estado do Rio de Janeiro, Brasil

Glicobiologa de hongos y protozoarios patgenos de humanos: un recuento de historias no terminadas"

Dr. Everardo LPEZ ROMERO. Universidad de Guanajuato, Mxico.

COFFE BREAK

SESION DE CARTELES PATIO CENTRAL

Coordinador: Dr. Pedro Hernndez

SESION DE TRABAJOS LIBRES AUDITORIO PARANINFO

Coordinador. Dr. Ricardo Lascurain

VIERNES 2 DE AGOSTO

SESION GENERAL 4 GLICOBIOTECNOLOGIA

AUDITORIO DR. GUSTAVO

BAZ PRADA

Coordinador. Dr. Everardo Lpez Romero

Papel de la N-glicosilacin en la estabilidad e inmunogenicidad de una vacuna recombinante contra influenza.

Dra. Laura A. PALOMARES. IBT, UNAM, Mxico

Protein glycosylation systems in bacterial pathogens and their promising applications in glycoengineering

Dr. Mario FELDMAN. University of Alberta, Canada.

Development of Streptococcus pneumoniae conjugate vaccine with the most prevalent serotypes in Latin America.

Dr. Vicente VEREZ BENCOME. Centro de Qumica Biomolecular, La Habana, Cuba.

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"Carbohydrate engineering in Escherichia coli K-12.

Dr. Bernard PRIEM.CNRS-CERMAV, Grenoble Francia

COFFE BREAK

SESION GENERAL 5 BIOSINTESIS Y METABOLISMO DE GLICOCONJUGADOS

AUDITORIO DR. GUSTAVO

BAZ PRADA

Coordinador: Dr. Edgar Zenteno

"Glycobiologie des voies de signalisation et pathologies associes-Fonctions associes la O-GlcNAcylation"

Dr. Tony LEFEBVRE. Unit de Glycobiologie Structurale et Fonctionnelle, Lille France

Nueva Regulacion de Reacciones Posttraduccional en el Aparato de Golgi: desde Ciencia Basica a Patologias

Dr. Carlos HIRSCHBERG. Boston University, USA .

UDP-glucose transporters and their role in protein quality control in the endoplasmic reticulum

Dr. Ariel ORELLANA. Universidad Andrs Bello, en Santiago, Chile

"O-GlcNAcylation, diabetes and cancer Dr. Tarik ISSAD. INSERM, Francia.

COMIDA SESION GENERAL 6 MODULACION DE LA RESPUESTA INMUNE Y

GLICOBIOLOGIA DEL CANCER

Coordinador: Dr. Miguel Mayoral

"Galectins in host-pathogen interactions and cancer: Structural and functional aspects

Dr. Gerardo VASTA . University of Maryland,Baltimore, EUA.

Role for Galectin-Glycan interactions in tuning the immune responses

Dra. Martha TOSCANO. Inst. Biol. y Med. Exp, Argentina.

"O-GlcNAcylation : a novel regulator of cell signaling and cell cycle

Dra. Vannesa DEHENAUT . Institut de Biologie de Lille, Universit de Lille Nord de France

New clinical and preclinical observations on human milk oligosaccharides"

Dr. Pedro PRIETO. Abbot Nutrition, EUA, Columbia.

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" Regulacin de la respuesta inmune innata por el Siglec-9, mediante el empleo de un nuevo SAMP (self-associated molecular pattern): el cido hialurnico"

Dr. Ismael SECUNDINO. University of California, San Diego, EUA

CLAUSURA Y PREMIACION DE TRABAJOS

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CONFRERENCISTAS EXTRANJEROS

DR: AJIT VARKI

CORREO ELECTRONICO: a1varki@ucsd.edu POSICION ACTUAL: Profesor de medicina celular y molecular, y co-director del Centro de Investigacin y Enseanza en Glicobiologa , University of California, San Diego, EUA LINEA DE INVESTIGACION: El papel del cido silico en las enfermedades y en las funciones biolgicas FORMACIN PROFESIONAL: Formacin bsica en fisiologa, medicina y bioqumica en la Universidad de Nebraska y Universidad de Washington en St. Louis. Certificacin en medicina interna, hematologa y oncologa. DATOS RELEVANTES: Presidente de la American Society of Glicobiology. Editor del J. Clinical Investigation, Premio emrito de NIH ,Premio de Investigacin de la Sociedad Americana de Cncer , Premio Karl Meyer de la Sociedad de Glycobiologa y la Organizacin Internacional Glicoconjugados 2007

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DR. GERARDO VASTA

CORREO ELECTRONICO: GVasta@som.umaryland.edu POSICION ACTUAL: Profesor del Departamento de Microbiologa e Inmunologa de la Escuela de Medicina, Programa de Biologa de Sistemas de Imagen, Universidad de Merylan, EUA LINEA DE INVESTIGACION: Aspectos bioqumicos y moleculares de las galactinas en la respuesta inmune FORMACIN PROFESIONAL: Licenciatura y doctorado en Bioqumica en la Escuela de Ciencias Exactas , Universidad Nacional , La plata , Buenos Aires Argentina, posdoctorado en el departamento de medicina e inmunologa clnica en el Roswell Park Memorial Institute, Buffalo, NY DATOS RELEVANTES: Fue profesor en el Centro de Biotecnologa Marina de la Universidad de Maryland Biotechnology Institute (UMBI) y asesor de Investigacin en el Departamento de Ciencias Biolgicas de la Universidad George Washington

CORREO ELECTRONICO: hudson@sanfordburnham.org POSICION ACTUAL: Director del Programa de Enfermedades Genticas del Centro Infantil de Sanford, Sanford Burnham Institute, EUA, Presidente de la Sociedad de Glycobiologa. LINEA DE INVESTIGACION:

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DR. HUDSON FREEZE

Enfermedades congnitas por dficit en glicosilacin FORMACIN PROFESIONAL: Doctorado en la Universidad de San Diego California en Biologa, medicina y Neurociencias DATOS RELEVANTES: Se dedica a descubrir las causas moleculares de las enfermedades congnitas por dficit de glicosilacin as como en cncer, diabetes, enfermedades infecciosas, neurodegenerativas, inflamatorias e infecciosas en la niez.

DR. PEDRO PRIETO

CORREO ELECTRONICO: pedro.prieto@abbott.com POSICION ACTUAL: Director de Investigacin ABBOT laboratorios, Columbia, USA LINEA DE INVESTIGACION: Composicin de carbohidratos complejos en leche materna FORMACIN PROFESIONAL: Ingeniero Bioqumico por el Tecnolgico de Monterrey, Maestra en Administracin por la Universidad de Alabama, Maestra en Bioqumica y Nutricin y el Doctorado en Bioqumica y Nutricin, ambos por Virginia Tech, miembro de la Facultad de Bioqumica de la Universidad de Georgia. DATOS RELEVANTES: Miembro de la Sociedad honorfica de

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investigacin cientfica Sigma XI y la Sociedad Internacional de Glicobiologa, miembro del Consejo Asesor de la Fundacin Zambrano Helin del Tecnolgico de Monterrey y es titular de Ctedra en la Universidad Autnoma de Quertaro en Mxico.

DR. ISMAEL SECUNDINO

CORREO ELECTRONICO: isecundinovelazque@ucsd.edu POSICION ACTUAL: Postdoctorado en el Laboratorio. A. Varkin, University of California LINEA DE INVESTIGACION: El papel de los cidos silicos expresadas en la cpsula de Escherichia K1 y sus interacciones con los receptores Siglec en macrfagos y clulas microgliales en la patogenia de la meningitis neonatal. FORMACIN PROFESIONAL: Doctorado en Inmunologa en la UNAM Mxico. Investigacin postdoctoral en el Instituto de Biotecnologa, Cuernavaca, Mxico).

CORREO ELECTRONICO: rtalmaraz@ucdavis.edu POSICION ACTUAL: Posdoctorado de la University of Michigan LINEA DE INVESTIGACION: Aplicacin de tcnicas para el anlisis de glicanos de clulas de cncer pancretico. Aplicacin de tcnicas de glicoingeniera metablicos para

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DR. RUBN ALAMARAZ

modificar las estructuras de glicanos in vitro FORMACIN PROFESIONAL: Postdoctorado en la Universidad de Michigan, ttulo de su investigacin: "Anlisis de la glicobiologa de las clulas del cncer de pncreas por Espectrometra de Masas". Posdoctorado en Johns Hopkins University 2009-2012. Ttulo de investigacin: "Propiedades Glicobiolgicas y Biofsicas de la metstasis del cncer pancretico". DATOS RELEVANTES: Posdoctorado de la Jonhs Hopkins University

DR. CARLOS HIRSCHBERG

CORREO ELECTRONICO: chirschb@bu.edu POSICION ACTUAL: Profesor del Departamento de Biologa Molecular y Celular, Boston University LINEA DE INVESTIGACION: Biognesis, estructura y funcin de la superficie de las clulas eucariotas inferiores y superiores y de la matriz extracelular, (glicoprotenas, glicolpidos, y glicosaminoglicanos). FORMACIN PROFESIONAL: Doctorado obtenido en la Universidad de Illinois, Urbana, 1970 Universidad de Harvard, 1970-1972 Instituto Tecnolgico de Massachusetts, 1972-1974 DATOS RELEVANTES: "MERIT Award NIH grant GM 30365 ""Glycosylation of Cell Lipids and Proteins"" (19912001). Pertenece a

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multiples Sociedades Cientficas Americanas e Internacionales como American Association for the Advancement of Science, American Society for Biochemistry and Molecular Biology, American Society for Cell Biology.

DR. MARIO FELDMAN

CORREO ELECTRONICO: mfeldman@ualberta.ca POSICION ACTUAL: Profesor en el departamento de Ciencias Biolgicas de la Universidad de Alberta e Investigador Titular en Alberta Glycomics Centre, Canad LINEA DE INVESTIGACION: Glicoingeniera de vacunas contra microorganismos patgenos FORMACIN PROFESIONAL: Doctorado en la Universidad de Buenos Aires DATOS RELEVANTES: Autor de mltiples artculos sobre mecanismos de glicosilacin de la protena en bacterias , glicoingeniera para el diseo de vacunas y factores de virulencia de microorganismos

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DRA. MATHA TOSCANO

CORREO ELECTRONICO: martalitos@gmail.com POSICION ACTUAL: Investigador Adjunto - CONICET. Instituto de Biologa y Medicina Experimental (IByME). Consejo Nacional de Investigaciones Cientficas y Tcnicas (CONICET). LINEA DE INVESTIGACION: Interacciones entre galectinas y glicanos en la regulacin de la respuesta inmune adaptativa, en condiciones patolgicas como autoinmundad y cncer. FORMACIN PROFESIONAL: Dra. en Ciencias Biolgicas de la Universidad de Buenos Aires.

DRA. CARLA ASSTEGIANO

CORREO ELECTRONICO asteggianocarla@hotmail.com POSICION ACTUAL: Directora del laboratorio de Desrdenes Congnitos de la Glicosilacin en el Centro de Estudio de las Metabolopatas Congnitas (CEMECO), Profesora Adjunta de Qumica en la Facultad de Medicina de la Universidad Catlica de Crdoba. Argentina LINEA DE INVESTIGACION: Estudio de glicoprotenas de membrana plaquetaria humana, Bases moleculares de displasias esquelticas debidas a alteraciones de O-glicosilacin entre otras o-glicanopatas).

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FORMACIN PROFESIONAL: Doctorado en Ciencias Biolgicas con formacin especialista en gentica molecular humana y glicobiologa humana DATOS RELEVANTES: Capacitacin en el estudio de los Desrdenes Congnitos de la glicosilacin (CDG) en centros de investigacin europeos pertenecientes a la red Euroglycanet.

DRA. LEILA M. LOPES-BEZERRA

CORREO ELECTRONICO: lmlb23@globo.com POSICION ACTUAL: Profesora adjunta en la Universidad Estatal de Ro de Janeiro. LINEA DE INVESTIGACION: Estudio de Sporothrix schenckii causante de la esporotricosis, la adhesin de los antgenos en la matriz extracelular, pared celular, el endotelio, y serodiagnstico con glicoconjugados. FORMACIN PROFESIONAL: Doctorado en Bioqumica por la Universidad Federal de Ro de Janeiro en 1991. DATOS RELEVANTES: Creadora de la primera vacuna sinttica basada en carbohidratos

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DR. VICENTE VEREZ

CORREO ELECTRONICO: vicente.verez@cqb.cu vicente@fq.oc.uh.cu POSICION ACTUAL: Director General del Centro de Qumica Biomolecular. Laboratorio de Antgenos sintticos. Facultad de Qumica, Universidad de la Habana, Cuba. Centro de Qumica Biomolecular LINEA DE INVESTIGACION: Vacunas sintticas de carbohidratos antignicos para uso humano FORMACIN PROFESIONAL: Dr. En Qumica DATOS RELEVANTES: Premio en honor de William J Probst de la Universidad del Sur de Illinois en 2006. Es miembro emrito de la Academia de Ciencias de Cuba, miembro de la Academia de Ciencias del tercer mundo desde el 2007, miembro honorario de la Sociedad Latinoamericana de Glicobiologa

DR. TONY LEFEBVRE

CORREO ELECTRONICO tony.lefebvre@univ-lille1.fr POSICION ACTUAL: Investigador Unit of Structural and Functional Glycobiology (UGSF), University of Lille LINEA DE INVESTIGACION: Glicobiologa estructural y funcional FORMACIN PROFESIONAL: Se gradu de la Universidad de Minnesota, Twin Cities, de Minneapolis en medicina interna.

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DATOS RELEVANTES:

DRA. VANNESA DEHENAUT.

CORREO ELECTRONICO vanessa.dehennaut@ibl.fr POSICION ACTUAL: Investigador del Instituto de Biologa de Lille, Universit de Lille Nord de Francia LINEA DE INVESTIGACION: Modificaciones postraduccionales en Cncer, estudio de la regulacin en las funciones -catenina and ciclina D1 por O-GlcNAcylation FORMACIN PROFESIONAL: Licenciatura en biologa celular y Fisiologa en la Universidad de Lille 1, Francia . Doctorado en ciencias Biolgicas en la Universidad Lille 1, France , en el tema Study of the tumor suppressor HIC1 (Hypermethylated in Cancer 1 . Post- doctorado en el Institute of Biology of Lille Asistente de Profesor en la Universidad de Lille 1, Francia DATOS RELEVANTES: mltiples artculos sobre glicoconjugados y O-GlcNAcylation

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DR. TARIK ISSAD

CORREO ELECTRONICO tajik.issad@inserm.fr POSICION ACTUAL: Director de Investigacin del Instituto Cochin en Pars, INSRM LINEA DE INVESTIGACION: Regulacin de la insulina y el metabolismo de la energa, mecanismos celulares y moleculares. FORMACIN PROFESIONAL: Licenciatura y doctorado en Ciencias Biolgicas en la Universidad de Pars. Post-doctorado en la Universidad de Bristol (Reino Unido). DATOS RELEVANTES: Pioneros en el desarrollo de la tecnologa de BRET para el estudio de la interaccin protena-protena en clulas vivas. Se ha usado esta tcnica para el estudio de la insulina y la sealizacin de IGF-1

DR. BERNARD PRIEM

CORREO ELECTRONICO priem@cermav.cnrs.fr POSICION ACTUAL: Investigador del "Centre de Recherches sur les Macromolcules Vgtales. Universidad de Grenoble, Francia LINEA DE INVESTIGACION: Ingeniera de carbohidratos de microorganismos FORMACIN PROFESIONAL: Doctorado en Bioqumica en la Universidad de Lille. Post-doctorado en

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Beltsville, Maryland, donde trabaj en la maduracin del fruto de tomate DATOS RELEVANTES: Profesor en la Universidad de Grenoble, investigacin en CERMAV, un conocido centro CNRS en hidratos de carbono.

DR. ARIEL ORELLANA

CORREO ELECTRONICO: aorellana@unab.cl POSICION ACTUAL: "Profesor Titular en la Universidad de Concepcin, Chile, Doctor en Ciencias Biolgicas, Biologa Celular y Molecular, P. Universidad Catlica de Chile. Departamento de Biologa, Universidad de Chile" LINEA DE INVESTIGACION: Protemica, genmica y biosntesis de polisacridos de pared celular de plantas DATOS RELEVANTES: "Investigador principal durante el (2010-2014 ) en Centro FONDAP de Regulacin del Genoma Investigador Principal. (2010-2013) en Genmica de Plantas. "

CONFERENCISTAS

NACIONALES

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DR. EDGAR ZENTENO GALINDO

CORREO ELECTRONICO: ezenteno@servidor.unam.mx POSICION ACTUAL: Jefe del Depto. Bioqumica Fac. Medicina UNAM, Investigador Nacional Nivel 3 y Profesor Titular de Bioqumica y de Inmunologa LINEA DE INVESTIGACION: Papel biolgico de los glicoconjugados en diversas patologas y en respuesta inmune innata. FORMACIN PROFESIONAL: Mdico Cirujano de la Facultad de Medicina UNAM (1976), Doctor de Tercer Ciclo en Bioqumica Aplicada (1986) y Habilitacin para Dirigir la Investigacin en el rea de Ciencias Naturales (1994) de la Universidad de Ciencias de Lille Francia. DATOS RELEVANTES: Distincin Cecilio Robelo, del Gobierno de Morelos (1994). Mencin Honorfica en el Premio CANIFARMA 1997 Dr. Alfredo Tellez Girn, Premio CANIFARMA-INFARVET en 2004. Profesor Honorario por la Facultad de Medicina de la Universidad Ricardo Palma de Per (2007).

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DR. GABRIEL CUEVAS

CORREO ELECTRONICO: gecb@unam.mx POSICION ACTUAL: Director del Instituto de Qumica de la Universidad Nacional Autnoma de Mxico LINEA DE INVESTIGACION: Naturaleza de los efectos estereoelectrnicos y de las interacciones dbiles en la conformacin, la reactividad y el reconocimiento molecular DATOS RELEVANTES: "Premio Weizmann 1993 en Ciencias Exactas Beca de la Fundacin Alexander von Humboldt para efectuar estudios posdoctorales. Reconocimiento a los Autores Mexicanos cuyos artculos han sido frecuentemente citados a nivel Internacional. Institute for Scientific Information (ISI). Premio de Investigacin 2002 de la Academia Mexicana de Ciencias. Distincin Universidad Nacional para Jvenes Acadmicos en el 2003. Investigador Nacional nivel III desde 2003."

CORREO ELECTRONICO: everlope@ugto.mx POSICION ACTUAL: Investigador Titular Universidad de Guanajuato LINEA DE INVESTIGACION: Mecanismos de glicosilacin protenas de

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DR. EVERARDO LPEZ ROMERO microorganismos patgenos FORMACIN PROFESIONAL: Doctor en Ciencias (Microbiologa), por el Instituto Politcnico Nacional DATOS RELEVANTES: realiz una estancia sabtica en la UAMS (University of Arkansas Medical School) en Little Rock, AR Sntesis de glicoprotenas en tejidos animales. A su regreso a Guanajuato, inici una lnea de investigacin sobre los mecanismos de sntesis de estas macromolculas utilizando hongos (Cndida albicas) y protozoarios (Entamoeba histolytica y E. invadens) como modelos.

DR. IVAN MARTINEZ DUNCKER

CORREO ELECTRONICO: duncker@uaem.mx POSICION ACTUAL: Jefe del Laboratorio. De glicobiologa humana. Profesor-Investigador Universidad del Estado de Morelos LINEA DE INVESTIGACION: Glicosilacin de protenas y su relacin con la pato fisiologa molecular de diversas enfermedades humanas FORMACIN PROFESIONAL: Dr. en Ciencias, Universidad de Paris, Postdoctorado. Instituto Nacional de Ciencias y Tcnicas Nucleares de Francia.

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DATOS RELEVANTES: Presidente de la Sociedad Latinoamericana de Glicobiologa

DRA. LAURA PALOMARES

CORREO ELECTRONICO: laura@ibt.unam.mx POSICION ACTUAL: Investigadora Titular del Instituto de Biotecnologa de la UNAM LINEA DE INVESTIGACION: Ingeniera del cultivo de clulas animales para la produccin, caracterizacin y purificacin de glicoprotenas y protenas multimricas recombinantes. FORMACIN PROFESIONAL: Ingeniera Bioqumica por el Instituto Tecnolgico y de Estudios Superiores de Monterrey, Investigadora Asociada en 1999 postdoctorado en la Universidad de Cornell, EUA, doctora en Ciencias (1999) en la UNAM. DATOS RELEVANTES: Su trabajo doctoral fue distinguido con la Medalla Alfonso Caso 1999 al Mrito Universitario que otorga la UNAM, el Premio Alfredo Snchez Marroqun 2001 a la mejor tesis de doctorado (otorgado por la Sociedad Mexicana de Biotecnologa y Bioingeniera, SMBB) y el Premio Weizmann-Khan 2001 a la mejor tesis doctoral en investigacin tecnolgica (otorgado por la Academia Mexicana de Ciencias)

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DR HECTOR MORA

CORREO ELECTRONICO: hmora@ugto.mx POSICION ACTUAL: Profesor-Investigador Titular de la Universidad de Guanajuato LINEA DE INVESTIGACION: Estructura y funcin de la pared celular de hongos patgenos en reconocimiento inmune DATOS RELEVANTES: Editor asociado de la seccin de divulgacin cientfica de la pgina de web " The International Society for Human and Animal Mycology , miembro del comit editorial de la revista internacional Medical Mycology, Editor en Jefe de la revista internacional Journal of Glicobiology.

CORREO ELECTRONICO: humberto@insp.mx POSICION ACTUAL: Director del rea de Infeccin e inmunidad CISEI Presidente de la Sociedad Mexicana de Inmunologa LINEA DE INVESTIGACION: Evolucin y Filogenia de la Respuesta Inmune, inmunidad innata, especies reactivas de oxgeno e investigacin en protemica. FORMACIN PROFESIONAL: Licenciado en Biologa. ENEP-Iztacala UNAM. Doctor en Inmunologa, Escuela Nacional de Ciencias Biolgicas, IPN.

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DR. HUMBERTO LANZ Posdoctorado en Inmunologa de Insectos (Universidad de Estocolmo). Posdoctorado en Entomologa Aplicada (Escuela Politcnica de Zrich). Posdoctorado en Inmunologa celular de insectos (Universidad de Arizona). DATOS RELEVANTES: Investigador Nacional II Presidente de la Sociedad Mexicana de Protemica 2010-2011.

DRA. VICTORIA PANDO

CORREO ELECTRONICO: victoria.pando@insp.mx POSICION ACTUAL: Investigador en Ciencias Mdicas "C. Unidad de Protemica, Instituto Nacional de Salud Publica LINEA DE INVESTIGACION: interaccin patgeno hospedero, principalmente en el modelo del virus dengue-monocitos/macrfagos FORMACIN PROFESIONAL: Licenciatura en Qumica, en la Universidad Peruana Cayetano Heredia. En el 2002, termin el Doctorado en Ciencias en el Instituto de Biotecnologa de la Universidad Nacional Autnoma de Mxico. DATOS RELEVANTES: Miembro fundador y actual presidente de la Sociedad Mexicana de Protemica

CORREO ELECTRONICO: landapi@hotmail.com

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DRA. LOURDES ARRIAGA

POSICION ACTUAL: "Investigador Asociado D, Unidad de Investigacin Mdica en Inmunoqumica, Hospital de Especialidades, Centro Mdico Nacional Siglo XXI, Instituto mexicano del Seguro Social. Miembro del sistema Nacional de Investigadores Nivel I. LINEA DE INVESTIGACION: Marcadores inmunolgicos en enfermedades inflamatorias sistmicas FORMACIN PROFESIONAL: Dra. En Ciencias Qumico-Biolgicas por la ENCB. DATOS RELEVANTES: Miembro del sistema Nacional de Investigadores Nivel I. Especialista en citometra de flujo que utiliza la tcnica para la bsqueda de inmunofenotipos con potencial valor diagnstico/pronstico en enfermedades inflamatorias sistmicas. Encargada del Captulo de Citometris de Flujo de la SMI

CORREO ELECTRONICO: yobanper@gmail.com POSICION ACTUAL: Profesor-Investigador de la Universidad Autnoma de Benito Jurez de Oaxaca LINEA DE INVESTIGACION: Glicosilacin de dominios lipdicos

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DRA. YOBANA PEREZ

FORMACIN PROFESIONAL: Doctora en Bioqumica de la Universit des Sciences et Technologies de Lille, FRANCE

DR. PEDRO HERNANDEZ CRUZ

CORREO ELECTRONICO: fuegoblanco68@yahoo.com.mx POSICION ACTUAL: Profesor-Investigador de la Universidad Autnoma de Benito Jurez de Oaxaca FORMACIN PROFESIONAL: Dr. Ciencias Biomdicas UNAM DATOS RELEVANTES: Investigador Nivel I del Sistema Nacional de Investigadores.

CONFERENCISTAS CURSO

PRECONGRESO

DRA. BLANCA ESPINOSA CORREO ELECTRONICO: bespinosa1118@yahoo.com.mx POSICION ACTUAL: Profesor-Investigador Depto. de Bioqumica INER LINEA DE INVESTIGACION: Glicosilacin en Alzheimer FORMACIN PROFESIONAL: Dra. Ciencias Biomdicas UNAM

31

DATOS RELEVANTES: Investigador Nivel I del Sistema Nacional de Investigadores Investigador en Ciencias Mdicas, CCINSHAE

DR. MIGUEL ANGEL MAYORAL

CORREO ELECTRONICO: mianmayo@yahoo.com POSICION ACTUAL: Profesor-Investigador de la Universidad Autnoma de Benito Jurez de Oaxaca LINEA DE INVESTIGACION: Glicobiologa del Cncer FORMACIN PROFESIONAL: Dr. Ciencias Biomdicas UNAM DATOS RELEVANTES: Investigador Nivel I del Sistema Nacional de Investigadores.

CORREO ELECTRONICO: rlascurainl@yahoo.com.mx POSICION ACTUAL: Profesor Titular -Investigador Facultad de Medicina, UNAM LINEA DE INVESTIGACION: Inmunologa del asma alrgico FORMACIN PROFESIONAL: Dr. Ciencias Biomdicas UNAM

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DR. RICARDO LASCURAIN

DATOS RELEVANTES: Investigador Nivel II del Sistema Nacional de Investigadores. PDRIDE D

DR. ANTONIO SERRATO

CORREO ELECTRONICO: serratoiner@gmail.com POSICION ACTUAL: Profesor-Investigador Depto. de Bioqumica INER LINEA DE INVESTIGACION: Glicobiologa de anticuerpos FORMACIN PROFESIONAL: Doctor en Biotecnologa, UNAM DATOS RELEVANTES: Investigador Nivel I del Sistema Nacional de Investigadores Investigador en Ciencias Mdicas, CCINSHAE

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RESUMEN DE CONFERENCIAS

MAGISTRALES

SESION GENERAL 1 CONFERENCIAS INAGURALES

AUDITORIO DR. GUSTAVO BAZ PRADA

Coordinador: Dr. Ivn Martnez Druncker

BIOLOGICAL ROLES OF GLYCANS - A LOOK BACK OVER THE DECADES

Ajit Varki

Glycobiology Research and Training Center, Departments of Medicine, and Cellular & Molecular

Medicine, University of California at San Diego, La Jolla, CA, USA

Both simple and complex glycans have long been known to play major metabolic,

structural and biophysical roles in various biological systems. Pathogen and commensal

recognition of host glycans has also been the subject of intense study for many

decades. However such biological roles cannot fully explain the remarkable complexity

and organismal diversity of glycan structures found in nature. Indeed, in systematically

reviewing the subject just twenty years ago (Glycobiology 3:97-130, 1993), one had to

search hard to find a few clear-cut instances of more specific biological roles of glycans

that are of intrinsic value to the organism that synthesizes the glycans. In striking

contrast there is now a wealth of examples to choose from. Thus, any current review of

the biological roles of glycans cannot possibly be comprehensive. Instead, a historical

overview will be presented, broad principles outlined and a few specific examples cited,

representing biological roles of different kinds mediated by various classes of glycans,

in different evolutionary taxa. What has remained unchanged since 1993 is the fact that

while all of the theories regarding biological roles of glycans are supported by

34

compelling evidence, exceptions to every single one can also be found. In retrospect

this is not too surprising. Complex and diverse glycans are now known to be ubiquitous

to all living cells in nature, and essential to all life forms. Thus, it was inevitable that >3

billion years of evolution selected these molecules for several key biological roles even

while using them in other circumstances for relatively unimportant roles, or sometimes

even expressing them for no obvious roles at all. In this respect glycans are no different

from other classes of biological macromolecules such as DNA, RNA, proteins and lipids.

The question now to be addressed is, what biological roles do glycans not mediate?

TOOLS FOR IDENTIFYING NEW HUMAN GLYCOSYLATION DISORDERS Hudson Freeze, Sanford-Burnham. Medical Research Institute, La Jolla CA

Today there are nearly 100 human glycosylation disorders caused by mutations in

genes serving one or more biosynthetic pathways. In 2013 alone, a new glycosylation

disorder was reported on average every 11.7 days. That trend is likely to continue in the

near future since at least 2% of the human genome encodes genes used for glycan

biosynthesis and recognition. Additional unanticipated genes will certainly be identified

that affect glycosylation pathways or alter glycan structure. Evidence of their importance

will come from the discovery of patients who carry function-compromising mutations in

these genes.

This bonanza of discovery was fueled and enabled by a coalescence of genomic,

biochemical and social media technologies that include all stakeholders: scientists,

physicians, patients themselves, and their families.

The falling costs and greater availability of exome and genome sequencing will soon

make it an accessible diagnostic clinical test. Sophisticated data analysis programs filter

and distill terabytes of sequencing data to a few candidate genes. The key word is

candidate. Functional validation of putative mutations is needed to confirm the

predictions of a mutations deleterious impact. The well-considered and sophisticated

filters may sometimes inadvertently dismiss critical candidates. An example of such an

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oversight is the identification of glycosylation disorder due to spontaneous mutations in

4 patients resulting in somatic mosaicism. Standard exome analysis overlooked the

defective gene, but routine analysis of a glycan-based biomarker, transferrin, provided

the critical biochemical evidence early on that identified the gene. A combination of

reliable biochemical tests and exome/genome sequencing is indispensible. It enabled

us to identify 8 new glycosylation disorders from 50 patients who showed abnormal

glycosylation. Moreover, incoming results of exome sequencing in patients for whom

glycosylation markers were not analyzed deliver new glyco-candidates that can be

validated by glycosylation analysis of serum, fibroblasts or lymphoblasts.

Today, the highly motivated parents of children with unknown metabolic disorders scour

the web and social networks on a daily search for leads and answers for their families.

Our laboratories are but a click away from their questions and their cooperation. As new

genes are discovered that reveal causes of the estimated 3500 unsolved genetic

disorders, the basic scientist will lead the assault on functional analysis of these genes

with support from an increasingly savvy group of web-wise families who are fully

committed to solutions. This creates an opportunity to educate and strengthen the vital

and expanding links between basic scientists, physicians and the voter/tax payer

families. Solving glycosylation disorders provides a model of how to integrate and

advance both medical and fundamental science to benefit afflicted families.

Supported by R01DK55615 and The Rocket Fund.

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SYMPOSIUM

TECNICAS PARA EL ESTUDIO DE LA GLICOBIOLOGIA

AUDITORIO DR. GUSTAVO BAZ PRADA

Coordinador: Dr. Edgar Zenteno

BIOINGENIERIA APLICADA (NUCLEASAS CON DEDOS DE ZINC Y MODIFICACIONES DE GENOMAS EN SISTEMAS EUCARIOTICOS. MsC David Pierre Pillon. Sigma Aldrich de Mxico. David.Pillon@sial.com

Las nucleasas con dedos de zinc (ZFN) son una clase de protenas de unin a ADN, derivadas de la bioingeniera, que facilitan la edicin especfica del genoma mediante la creacin de rupturas de la doble cadena del ADN en los lugares especificados por el usuario. Las rupturas de la doble cadena son importantes para la mutagnesis sitio-especfica que estimula los procesos naturales de reparacin del ADN de las clulas, es decir la recombinacin homloga y la unin de extremidades no homologas (NHEJ). La ingeniera genmica en clulas de mamfero presenta un enorme potencial para investigacin bsica, descubrimiento de medicamentos, as como para la produccin de medicamentos basados en tcnicas de cultivo celular. Para este fin, Sangamo Biosciences y Sigma-Aldrich se han asociado recientemente para desarrollar y proveer una nueva tecnologa que permite la edicin del genoma a travs del diseo de nucleasas con dedos de zinc (ZFN). Dentro de estas protenas quimricas, la especificidad de unin al ADN es determinada por la protena con dedos de zinc permitiendo definir el sitio de accin de la nucleasa. Tales Nucleasas (ZFN) son capaces de reconocer y unirse a un lugar especfico del genoma y provocar un corte preciso de la doble cadena del ADN con alta eficiencia y precisin. La clula entonces emplea los procesos naturales de reparacin del ADN, como son la "reparacin homologa dirigida (HDR)" o "unin de extremidades no homlogas (NHEJ)" para reparar de manera especfica el punto de ruptura. Estas dos vas proporcionan al investigador la capacidad de provocar tres opciones claras para editar genomas: correccin de genes, supresion de genes y la adicin dirigida de genes o secuencias de inters. Por otra parte, la velocidad y la eficiencia de este proceso nos permiten realizar knock-out (KO) en mltiples genes en la misma clula. El tener acceso a la ingeniera gentica facilita la creacin de lneas celulares y animales transgnicos para aplicaciones en investigacin biomdica, generando un nuevo campo de oportunidades para el desarrollo de nuevos frmacos, pero sobre todo la posibilidad de seguir el camino de la medicina personalizada.

37

La tecnologa de las ZFN pone al alcance de los investigadores una herramienta mucho ms precisa, acelerando la investigacin cientfica y brindando as mayores oportunidades de desarrollo de terapias an ms eficaces y personalizadas

USO DE LA ESPECTROMETRA DE MASAS PARA LA IDENTIFICACIN DE

RESIDUOS DE CARBOHIDRATOS

Dra. Victoria Pando-Robles

Centro de Investigacin en Enfermedades Infecciosas, Instituto Nacional de Salud Pblica.

La espectrometra de masas (EM) es una tcnica analtica que se ha convertido en el eje central de la investigacin a nivel de protenas y biomolculas. La capacidad de identificar protenas y determinar su estructura primaria es fundamental para el estudio de los seres vivos, donde la secuencia de aminocidos comprueba la conexin entre protena y su gen codificante, va el cdigo gentico; mientras que el descubrimiento de sus modificaciones post-traduccionales hace evidente la relacin entre fisiologa celular y gentica. Los espectrmetros de masas existen desde 1900, miden la relacin masa/carga de las molculas. Sus componentes principales son: la fuente de ionizacin, el analizador de masas y el detector, que existen en varias versiones, la combinacin de estas partes es muy importante ya que repercute en la sensibilidad y exactitud de la medicin. A fines de los 80s se desarrollaron fuentes de ionizacin suave, que permitieron el anlisis de polmeros como las protenas, los cidos nucleicos y los carbohidratos. Los proteoglicanos (PG) son una clase especial de glicoprotenas altamente glicosiladas, formados por varios ncleos proteicos que se modifican post-traduccionalmente con polisacridos denominados glicosaminoglicanos (GAG), que a su vez son polmeros de carbohidratos lineares cargados negativamente. Dada su diversidad estructural los proteoglicanos realizan diferentes funciones tanto en la matriz extracelular como en la clula, y han sido involucrados en diferentes procesos celulares: interacciones clula-clula, clula-matriz, activacin de quimiocinas y citocinas, morfognesis de tejidos durante el desarrollo embrionario, migracin, proliferacin celular y en el reconocimiento de patgenos. Proteoglycomics se refiere al estudio de los proteoglicanos usando las herramientas del anlisis protemico. Las funciones individuales de los PG pueden ser atribuidas tanto al centro proteico como a las cadenas GAG, donde la determinacin de la estructura GAG es un reto analtico formidable debido a su complejidad estructural, su carga negativa, polidispersidad y microheterogeneidad.

THE INTERACTION CH / PI, PROTEIN CARBOHYDRATE RECOGNITION BASE AND ITS APPLICATION TO THE SYNTHESIS OF CATALYSTS. Fabin Cutara Guadarrama and Gabriel Cuevas

38

Instituto de Qumica. Un iversidad Nacional Autnoma de Mxico. Apdo. Postal 70213, 04510, Coyoacn, Circuito Exterior, Mxico D.F. Mxico. Specific interactions between molecules, including those produced by a given solute, and the surrounding solvent are essential to drive molecular recognition processes. A simple molecule such as benzene is capable of recognizing and differentiating among very similar entities, such as methyl 2,3,4,6- tetra-O-methyl--D-galactopyranoside ( -Me5Gal), methyl 2,3,4,6-tetra-O-methy--D-galactopyranoside (-Me5Gal), 1,2,3,4,6-penta-O-acetyl- -D-galactopyranose (-Ac5Gal), and methyl 2,3,4,6-tetra-O-methyl- -D- mannopyranoside (-Me5Man). In order to determine if these complexes are formed, the interaction energy between benzene and the different carbohydrates was determined, using Calvet microcalorimetry, as the enthalpy of solvation. These enthalpy values were -89.0 ( 2.0, -88.7 ( 5.5, -132.5 ( 6.2, and -78.8 (3.9 kJ mol-1 for the four complexes, respectively. Characterization of the different complexes was completed by establishing the molecular region where the interaction takes place using NMR. It was determined that -Me5Gal is stabilized by the CH/ interaction produced by the nonpolar region of the carbohydrate on the face. In contrast, -Me5Man is not specifically solvated by benzene and does not present any stacking interaction. Although -Me5Gal has a geometry similar to that of its epimer, the obtained NMR data seem to indicate that the axial methoxy group at the anomeric position increases the distance of the benzene molecules from the pyranose ring. Substitution of the methoxy groups by acetate moieties, as in -Ac5Gal, precludes the approach of benzene to produce the CH/ interaction. In fact, the elevated stabilization energy of -Ac5Gal is probably due to the interaction between benzene and the methyl groups of the acetyls. Therefore, methoxy and acetyl substituents have different effects on the protons of the pyranose ring. With these data on hand it is possible to establish that benzene can recognize galactose and this property can be combined with the catalytical properties of phenylpyridone to promote esther aminolysis reactions. Both effects can be used to generate a molecule that recognizes a region of galactose and transforms an acetyl group. The substrate requires the incorporation of an acetyl group in the anomeric position and introduces methyl groups to eliminate the formation of hydrogen bonds which are dominant when compared with the CH/ interaction. The molecule was modeled using computational methods at the M05-2x/6-31+G(d,p) level; and was synthesized using a procedure that needs 3 steps and renders an 83% yield. The substitution of the phenyl group with a cyclohexane slows down the hydrolysis from 0.039 0.005 l2mol-2hr-1 to 0.028 0.003. The homologation of the chain gives a rate of hydrolysis of 0.028 0.003. NMR was used to demonstrate the interaction between the catalyzers phenyl group and galactose protons at positions 3, 4 and 5. The results show that CH/ interactions participate in the recognition processes between carbohydrates and aromatic groups of certain amino acids. This contribution adds to the existing evidence of the usefulness of such interactions. This can be used to develop organocatalyzers that can contribute to streamline diverse chemical processes.

39

SESION GENERAL 2 GLICOBIOLOGIA MEDICA

AUDITORIO DR. GUSTAVO BAZ PRADA

Coordinador: Dr. Hctor Mora

GLYCOBIOLOGY IN SKELETAL DYSPLASIA DUE TO CONGENITAL DISORDERS OF GLYCOSYLATION (CDG) Carla G Asteggiano (PhD) Investigadora Adjunta CONICET (Consejo Nacional de Investigaciones Cientficas y Tcnicas), Argentina. Directora Laboratorio Desrdenes Congnitos de las Glicosilacin, Centro de Estudio de las Metabolopatas Congnitas (CEMECO), Facultad de Ciencias Mdicas, Universidad Nacional de Crdoba, Crdoba, Argentina. Profesora Adjunta, Facultad de Medicina, Universidad Catlica de Crdoba, Crdoba, Argentina. E-mail: asteggianocarla@hotmail.com Web page: www.cdgargentina.com.ar

Glycosylation diseases are due to defects in different pathways, in protein glycosylation

and, recently defects in glycolipid have been identified as well. Congenital Disorders of

Glycosylation (CDG) are rapidly growing genetic pathologies with more than 50 genes

reported since 1980, the first clinical description by Prof. Jaak Jaeken. Defects have

been identified in N-glycosylation and O-glycosylation pathways and combined N- and

O-glycosylation types of CDG. The clinical manifestations can affect nearly all organs

and systems or could be restricted to a specific tissue such as the cartilage in multiple

osteochondromatosis (MO or EXT1/EXT2-CDG). An important neurological component

is often reported but a peculiar skeletal phenotype has been described in CDG patients,

gaining special relevance over the past few years. In patients exposed to the cell

hypoglycosylation due to altered glycosylation pathway, numerous extracellular matrix

proteins undergo glycosylation defects that lead to skeletal manifestations.

During the last eight years, we have focused on CDG and we detected altered N-

glycosylation (2 PMM2-CDG and 4 CDG-IIx patients) and O-glycosylation (33

EXT1/EXT2-CDG patients) subtypes. Most of CDG are autosomal recessive, but

EXT1/EXT2-CDG was described as a dominant disease. It is characterized by short

stature and development of benign bone tumors during childhood and adolescence. It is

based on heterozygous mutations in EXT1 or EXT2, two genes that codified

glycosyltransferases required for the synthesis of heparin sulfate proteoglycans

40

(HSPGs). This special pathology and other with a severe skeletal phenotype have

called our interest: O-glycosylation defects as GALNT3-CDG (Hyperfosfatemic Tumoral

Calcinosis); LFNG-CDG (Spondylocostal Dysostosis); SLC35D1-CDG

(Schneckenbecken Dysplasia); B4GALT7-CDG (Progeroid Variant of Ehlers Danlos)

and B3GALTL-CDG (Peter-Plus Syndrome). In these pathologies skeletal

manifestations as osteopaenia, rib cage abnormalities, short stature, kyphosis and

scoliosis are the most common manifestations. Molecules dependent on post-

translational modification processes such as glycosylation may play specific functions in

bone mineralization and in the endochondral growth plate. The glycosaminoglycans

heparan sulfate (HS), are usually found in the cell surface and extracellular matrix as

HSPG. They play an integral role in the structural integrity of various tissues, in ligand

binding, cell adhesion and cell signaling during endochondral ossification, process

regulated by growth factors that bind to HS chains.

Different reports postulated that it is very probable that not only hypoglycosylation but

also gain-of-glycosylation may cause skeletal phenotypes. Our results highlight the

hypoglycosylation effect on the genesis of skeletal manifestation in CDG patients,

suggesting that the process of glycosylation is also important in proteins implicated in

the development of cartilage and bone. In conclusion, it is strongly recommended to

search CDG diseases in any unexplained skeletal dysplasia. PICT2010/2824-UCC

2011-2013, CONICET.

SESION GENERAL 3

GLYCOBIOLOGY OF INFECTIOUS DISEASES AUDITORIO DR. GUSTAVO BAZ PRADA

Coordinador: Dr. Jos Luis Montiel

Candida albicans CELL WALL GLYCOBIOLOGY. Mora-Montes Hctor M.*, Flores-Carren Arturo, Daz-Jimnez Diana F., Gonzlez-Hernndez Roberto de J., Tamez-Castrelln Alma K. Departamento de Biologa, Universidad de Guanajuato, Noria Alta s/n,

41

Col. Noria Alta, C.P. 36050, Guanajuato, Gto., Mxico. Tel. 473 732 0006, ext. 8154. *e-mail: hmora@ugto.mx

The cell wall of the opportunistic pathogen Candida albicans -

glucans and glycoproteins, which are enriched with N-linked and O-linked mannans.

Protein mannosylation starts in the endoplasmic reticulum and finalizes in the Golgi

complex, where mannosyltransferases further modify the mannans. The study of

glycosylation pathways in C. albicans has allowed assessing the importance of these

protein modifications for fungal virulence and interaction with the host immune system.

We have generated a collection of mutant cells lacking key steps in N-linked

mannosylation processes and have found that disruption of both N-linked mannan core

trimming and outer chain extension, are required for virulence, proper cell wall

composition, dimorphism, and interaction with components of the immune system;

though the disruption of N-linked mannosylation pathway led to increased virulence in

C. glabrata. Over the last years, we have focused to the study of two

mannosyltransferase gene families: MNT1 and MNN4. Using genetic and biochemical

approaches we have found that the members of the MNT1 gene family have redundant

roles in the biosynthesis of phosphomannan, N-linked and O-linked mannans. In

addition, the encoded enzyme activities are required for a proper cell wall structure,

virulence and immune sensing. Members of the MNN4 gene family encode both

phosphomannosyltransferases and positive regulators of such enzyme activity, and

together with members of the MNT1 gene family participate in elaboration of

phosphomannan, a cell wall component required for phagocytosis and the effect of

antimicrobial peptides.

This work is supported by CONACyT (CB2011-166860) and Universidad de Guanajuato.

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SESION GENERAL 4 GLICOBIOTECNOLOGIA

AUDITORIO DR. GUSTAVO BAZ PRADA

Coordinador. Dr. Everardo Lpez Romero

N-GLYCOSYLATION DETERMINES THE STABILITY AND IMMUNOGENICITY OF RECOMBINANT INFLUENZA HEMAGGLUTININ. Laura A. Palomares, Lus ngel Cueto, Vanessa Hernndez, Ana Ruth Pastor and Octavio T. Ramrez Instituto de Biotecnologa, Universidad Nacional Autnoma de Mxico. Av. Universidad 2001 Col. Chamilpa, Cuernavaca Morelos. C.P. 62210, Mxico. Tel. (777) 3291646, laura@ibt.unam.mx

Hemagglutinin (HA) is the main antigen of influenza virus. Antibodies against HA block viral infection. Recombinant HA is an efficient vaccine against influenza virus infection. In this work, we investigated the role of N-glycosylation of HA in its susceptibility to aggregation. HA was produced in the insect cell-baculovirus system, purified and deglycosylated with Endo-H. Deglycosylated HA aggregated when exposed for 10 min to temperatures above 45C. In contrast, glycosylated HA only aggregated at temperatures above 55C. Glycosylated and deglycosylated HA were more stable at pH 6.8, but while few aggregates were observed in glycosylated HA, 20 % of deglycosylated HA was aggregated. Changing the pH between 3 and 8 resulted in different extents of aggregation, ranging from 2 to 18% in glycosylated HA and from 18 to 50% in deglycosylated HA. The kinetics of aggregation caused by temperature or pH were different. Aggregation caused by temperature followed an exponential increase with time, indicating a cooperative aggregation. No difference in the aggregation rates at the temperatures tested was observed. Aggregation caused by pH followed kinetics independent of the aggregate concentration, and higher aggregation rates were observed as pH decreased. Finally, the immunogenicity of glycosylated and deglycosylated HA was measured in mice. It was found that immunizing with deglycosylated HA resulted in IgG titers 20 times higher than those obtained when glycosylated HA was used. It was demonstrated that N-glycosylation of HA determines protein stability and immunogenicity. DEVELOPMENT OF Streptococcus pneumoniae CONJUGATE VACCINE WITH

THE MOST PREVALENT SEROTYPES IN LATIN AMERICA.

Y. Valds Balbin1, D. Santana Medero1, D. Garca Rivera1, A. Villar Aneiros1, D. Gonzlez Daz

2, B. Paredes Moreno1, L. Rodrguez Noda1, U. Ramrez Gonzlez2, J. Chang Caldern1 , J.

Lora Garca1, V Verez Bencomo1.

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1 Center for Biomolecular Chemistry, calle 21 y 200, Playa and 2 Finlay Institute Ciudad

Habana, Cuba

The development of a conjugate vaccine against multiple serotypes of S. pneumonia is

a complex task with numerous challenges. Several years ago, the Center for

Biomolecular Chemistry launched a research project for developing a heptavalent

vaccine containing the seven serotypes of S. pneumoniae more frequently associated

with infection in Cuba and Latin America. As a result we were able to design a

candidate vaccine containing 2g of each capsular polysaccharide 1, 5, 14, 18C, 19F

and 23F as well 4g for 6B - all of them conjugated to tetanus toxoid- and aluminum

phosphate as adjuvant. After several years of research and development, the

technology was established for the production of the seven active pharmaceutical

ingredients and of the combined vaccine. Several batches have been produced with the

aim to assess their physico-chemical properties and to perform the preclinical and

toxicological studies, guaranteed by a Quality Assurance System1. Last year, the first

clinical trial was conducted, demonstrating the safety and immunogenicity of vaccine in

healthy young. Presently, we are beginning the clinical trials in infants, with focus on

Phase I and Phase II no inferiority; thus paving the way toward first Latin-American

custom-designed conjugate vaccine against S. pneumoniae.

* Dedicated to Violeta Fernndez Santana memory. Deceased on 20th November, 2011

1 D. Garca-Rivera, L. Rodrguez, G. Hernndez, et al,8TH International Symposium

Pneumococci and Pneumococcal diseases ISPPD-8, 104, 2012

CARBOHYDRATE ENGINEERING IN Escherichia coli K-12.

Priem Bernard. CNRS-CERMAV, UPR 5301, BP53X, 38041 Grenoble cedex 9, France Tel +33

476037648. priem@cermav.cnrs.fr.

44

Bacterial metabolic engineering has emerged as a powerful method for large scale

synthesis of oligosaccharides. Glycosylation reactions are performed by whole cells

overexpressing the genes encoding the appropriate glycosyltransferases and sugar-

nucleotide biosynthesis. Combinations of engineered strains carrying several plasmids

allow producing a great variety of mammal carbohydrate structures. Furthermore,

chemical modifications can be carried out before or after the bacterial cultures, thus

allowing obtaining chemically modified oligosaccharides. Those chemical modifications

can be used either to ease chemical couplings or to modify the biological properties of

carbohydrates. An overview of the technology and suitable examples will be presented

in the talk.

SESION GENERAL 5

BIOSINTESIS Y METABOLISMO DE GLICOCONJUGADOS

AUDITORIO DR. GUSTAVO BAZ PRADA Coordinador: Dr. Edgar Zenteno

FUNCTIONS PLAYED BY O-GlcNACYLATION

Tony Lefebvre, Professor, Lille 1 University, CNRS/UMR 8576, Unit of Structural and Functional

Glycobiology, Villeneuve d'Ascq, FRANCE

Post-translational modifications (PTM) regulate protein functions by promoting or

preventing protein-protein interactions (theory of "one partner-one function"). The

modification therefore re-localizes the protein, impacts on its expression or regulates

enzyme activity as shown recently for PFK1. Glycosylations is a large family of PTM

that includes O-GlcNAcylation maybe the simplest one at the structural point of view.

O-GlcNAcylation consists in the reversible addition of a single N-acetylglucosamine to

the hydroxyl groups of serine and threonine of cytosolic and nuclear proteins. O-

GlcNAcylation processes are managed by a unique couple of enzymes namely O-

GlcNAc transferase (OGT) responsible for the transfer of the GlcNAc moiety and O-

GlcNAcase (OGA) that reverses the reaction. Despite appearances, O-GlcNAcylation

hides a very complex regulation mode such as phosphorylation with which besides O-

45

GlcNAcylation could either competes or acts in concert. In this way, O-GlcNAcylation is

part of signaling pathways which control the level of the glycosylation and in turn O-

GlcNAcylation interferes with the regulation of the PI3K and MAPK pathways. More

especially, in response to insulin OGT is targeted to lipid microdomains in a PI3K-

dependent manner. O-GlcNAcylation levels intimately correlate with the nutritional

status of the cell due to the nature of the nucleotide-sugar, UDP-GlcNAc, from which it

comes from. Therefore O-GlcNAcylation relays nutrient and energy status to cell

homeostasis. A -catenin O-GlcNAcylation, which

reduces its proteasomal susceptibility, is responsible for epithelial tumorigenesis. This

explains partly why patients suffering diabetes and obesity are more inclined to develop

colorectal cancers. In another set of studies, we showed that O-GlcNAcylation is crucial

for cell cycle progression. OGT is required for quiescent cells to reach the G0/G1

transition and for Xenopus laevis oocytes to mature in a process similar to G2/M

transition. On the contrary, OGA activity correlates with G1/S transition. On a

transcriptional point of view, it has been recently show by several groups that OGT

cooperates with TET proteins to remodel chromatin, a process needed for gene

expression. The focus of this talk is to give precise examples in which OGT and O-

GlcNAcylation are pivotal elements for cell fundamental processes.

NOVEL REGULATION OF POSTTRANSLATIONAL MODIFICATIONS IN THE GOLGI APPARATUS: FROM BASIC SCIENCE TO DESEASES. Carlos B. Hirschberg, Boston University, Boston, MA, USA.

Nucleotide sugars are transported by specific transporters from the cytosol, their site of

synthesis, into the lumen of the Golgi apparatus and endoplasmic reticulum, where they

serve as substrates for glycosylation reactions. These transporters play critical roles in

glycosylation of proteins, lipids and proteoglycans, which are essential for

organogenesis, development, mammalian cellular immunity and pathogenicity of human

pathogenic agents. Given their essential roles it is not surprising that these transporters

have been identified in all eukaryotes examined so far. The biochemical characteristics

and biological significance of these transporters have been demonstrated in mammals,

46

Caenorhabditis elegans, Drosophila melanogaster, yeast fungi, Leishmania, Entamoeba

and recently Trypanosoma brucei and Toxoplasma gondii .Importantly, mutations in

these transporters, result in human diseases such as Leukocyte Adhesion Deficiency II

and Schneckenbecken dysplasia and well as Complex Vertebral Malformation in

bovines.

Over the past years, numerous biochemical studies have demonstrated that

glycoconjugates were deficient in the particular sugar for which the corresponding

nucleotide sugar transport was defective. However, our recent studies of silencing

nucleotide sugar transporter genes of mammalian cells showed a more global defect in

the synthesis and secretion of not only glycoproteins but also in non glycoproteins. The

latter is probably the result of endoplasmic reticulum stress induction and protein

translation inhibition and may explain some of the diversity of symptoms in mammalian

diseases caused by transporter mutations. Further in depth studies of transporter

structures, functions and their regulation of glycosylation in mammals should lead to a

better understanding of the molecular mechanisms underlying the above diseases and

facilitate the discovery of appropriate therapies.

UDP-GLUCOSE TRANSPORTERS AND THEIR ROLE IN PROTEIN QUALITY

CONTROL IN THE ENDOPLASMIC RETICULUM

Dr. Ariel Orellana

FONDAP Center for Genome Regulation, Centro de Biotecnologa Vegetal, Universidad Andrs Bello,

Santiago, Chile

Nucleotide sugars are the substrates for glycosyltransferases located in the ER and the

Golgi apparatus. Most of them are synthesized in the cytosol, therefore they are

incorporated into the lumen of these organelles by nucleotide sugar transporters

(NSTs). The NSTs are a large gene family composed by around 50 members in

Arabidopsis thaliana. We have found two UDP-glucose transporters (UTr1 and Utr3),

located in the ER. Both genes are targets of the unfolded protein response (UPR) and

mutants on each of them trigger UPR. Double mutants are not viable. Our data suggest

47

that these NSTs are supplying the substrate for UGGT, the glucosyltransferase that

recognize unfolded proteins in the ER. This is an enzyme we have detected in

Arabidopsis and the analysis of different mutant alleles shows that these plants are

smaller and sensitive to different stress.

The human ortholog of Utr1 and Utr3 is HuGTRel1. We have tested the activity of this

protein and found that transport UDP-glucose. This gene also responds to UPR. All

these results support the hypothesis that transport of UDP-glucose is an important

process in the folding of glycoproteins in the ER.

Supported by Fondap-CRG 15090007, ICM P10-062-F, PB-16 and DI-365-13/R

O-GlcNACYLATION, DIABETES AND CANCER

Dr. Tarik Issad. INSERM U1016, CNRS UR 8104, Institut Cochin, Paris, France. E-mail:

tarik.issad@inserm.fr

O-GlcNAc glycosylation (O-GlcNAcylation) corresponds to the addition of N-

acetylglucosamine on serine and threonine residues of cytosolic and nuclear proteins.

O-GlcNAcylation is a dynamic post-translational modification, analogous to

phosphorylation, that regulates the stability, activity or subcellular localisation of target

proteins. This reversible modification depends on the availability of glucose and

therefore constitutes a powerful mechanism by which cellular activities are regulated

according to the nutritional environment of the cell. O-GlcNAcylation has been

implicated in important human pathologies including Alzheimer disease, type-2 diabetes

and cancer. Only two enzymes, OGT and O-GlcNAcase, control the O-GlcNAc level on

proteins. Therefore, O-GlcNAcylation cannot organize in signalling cascades as

observed for phosphorylation. O-GlcNAcylation should rather be considered as a

rheostat that controls the intensity of the signals travelling through different pathways

according to the nutritional status of the cell.

48

Several lines of evidence indicate that O-GlcNAcylation could contribute to the

glucotoxicity phenomenon in diabetic patients, in which hyperglycemia induces

alterations that result in worsening of the glycemia.

Excessive production of glucose by the liver is a major cause of fasting hyperglycemia

in type 2 diabetes. We previously showed that O-GlcNAcylation of FoxO1 in liver cells

stimulated its transcriptional activity and increased the expression of genes involved in

hepatic glucose production, suggesting a potential role of FoxO1 O-GlcNAcylation in

glucotoxicity.

FoxO1 also plays a major role in the regulation of pancreatic -cell physiology. We

observed that increased O-GlcNAcylation of FoxO1 in pancreatic -cells stimulated its

transcriptional activity towards Insulin-like growth factor-binding protein-1 gene (Igfbp1),

resulting in increased expression and secretion of IGFBP1. Increased IGFBP1 secretion

inhibited IGF1/IGF1R signalling pathway, and reduced the activity of the Phosphatidyl-

Inositol-3-Phosphate Kinase/Akt (PI3K/Akt) pathway. We therefore propose a novel

glucotoxicity mechanism in which O-GlcNAcylation of FoxO1, through increased

IGFBP1 production, negatively regulates the PI3K/Akt signalling in -cells.

Numerous epidemiological studies indicate that obesity or diabetic conditions increase

the risk of cancer. Recent evidences suggested that O-GlcNAcylation may affect the

growth of cancer cells. However, the consequences of O-GlcNAcylation on anti-cancer

therapy had not been evaluated. Breast cancer is the most common cancer in women.

Anti-estrogen therapies (e.g., tamoxifen) have permitted important progress for the

treatment of hormone-sensitive breast cancers. However, the development of treatment

resistance constitutes an important limitation to these therapies. We recently studied the

effect of O-GlcNAcyaltion on tamoxifen-induced MCF-7 breast cancer derived cells. We

observed that treatments that increase O-GlcNAcyaltion markedly inhibit tamoxifen-

induced MCF-7 cell death, suggesting that targeting this pathway could constitute an

interesting strategy for the treatment of tamoxifen-resistant tumours.

49

SESION GENERAL 6

MODULACION DE LA RESPUESTA INMUNE Y GLICOBIOLOGIA DEL CANCER

AUDITORIO DR. GUSTAVO BAZ PRADA

Coordinador: Dr. Miguel Mayoral

GALECTINS IN HOST-PATHOGEN INTERACTIONS AND CANCER: STRUCTURAL

AND FUNCTIONAL ASPECTS

Dr. Gerardo VASTA . University of Maryland,Baltimore, EUA.

Department of Microbiology and Immunology, University of Maryland School of

Medicine, Institute of Marine and Environmental Technology, Baltimore, Maryland, USA

Galectins are characterized by their binding affinity for -galactosides, a unique binding

site sequence motif, and wide taxonomic distribution and structural conservation in

vertebrates, invertebrates, protista, and fungi. Since their initial description, galectins

were considered to bind endogenous (self) glycans and mediate developmental

processes, including cell differentiation and tissue organization or regeneration. In the

past few years, however, numerous studies have described the diverse regulatory

effects of galectins on immune homeostasis and cancer. More recently, however,

evidence has accumulated to support the notion that galectins also bind exogenous

(non-self) glycans on the surface of potentially pathogenic microbes, parasites, and

fungi, suggesting that galectins could function as pattern recognition receptors (PRRs).

According to the currently accepted model for non-self recognition, PRRs recognize

pathogens via highly conserved microbial surface molecules of wide distribution such as

LPS or peptidoglycan (microbe-associated molecular patterns; MAMPs), which are

absent in the host. Galectins, however, can bind similar self/non-self molecular patterns

on host and microbial cells. Furthermore, although some galectins can bind and kill

bacteria, thereby displaying activity as innate immune recognition and effector factors, it

appears that in most cases galectin-mediated recognition favors the potential pathogen

50

rather than the host. Therefore, some galectins do not fit the definition of PRRs,

underscoring the significant gaps in our knowledge about the structural and functional

diversity, subcellular targeting, localization, and secretion of the galectin repertoire

components in any given species, and the host-parasite co-evolutionary processes that

have resulted in such interactions (Supported by Grant 5R01GM070589 from NIH, and

IOS 1050518, IOB- 0618409 and IOS0822257 from NSF).

A ROLE FOR GALECTIN-GLYCAN INTERACTIONS: LINKING TUMOR

NEOVASCULARIZATION AND IMMUNITY

Marta A Toscano, PhD. Laboratorio de Inmunopatologa, Instituto de Biologa y Medicina Experimental

(IBYME/ CONICET). E-mail: martalitos@yahoo.com.ar

Recent efforts towards decoding the glycan signature of immune cells have revealed

dramatic changes in N- and O-glycan structures during immune cell maturation,

activation and differentiation. The responsibility of deciphering these glycosylation

changes is assigned in part to endogenous lectins which expression is dynamically

regulated during chronic inflammatory responses. We will discuss recent findings from

our laboratory demonstrating the contribution of glycosylation-dependent mechanisms

and galectin-glycan interactions to the regulation of a broad range of immunological and

vascular programs, including: T and B cell survival, dendritic cell fate, microglia

activation and endothelial cell signaling. These mechanisms, which could be usurped by

tumors to evade and thwart immune responses, have been proposed to shift the

balance of immune responses and control immune cell tolerance, inflammation and

angiogenesis.

"O-GlcNACYLATION : A NOVEL REGULATOR OF CELL SIGNALING AND CELL

CYCLE.

Dra. Vannesa Dehenaut. Institut de Biologie de Lille, Universit de Lille Nord de France

51

In response to mitogenic signals, quiescent cells (G0 arrested) enter and progress

through the four phases of the cell cycle: G1, S (DNA replication), G2 and M (Mitosis)

to produce two daughter cells genetically identical. Cell cycle is highly controlled by

numerous factors especially at the G1/S and G2/M boundaries to ensure that DNA is

not damaged and correctly replicated: loss of control is one of the major causes of

cancer.

For a few years, beside phosphorylation, O-GlcNAcylation has emerged as a new key

regulator of cell cycle. O-GlcNAcylation, standing for O-linked N-

acetylglucosaminylation is an abundant and reversible post-translational modification

confined within the nucleus and the cytosol of eukaryotes. This glycosylation, often

compared to phosphorylation with which it can compete, is regulated by a unique

couple of enzymes, the O-GlcNAc transferase (OGT) and the O-GlcNAcase (OGA)

which catalyse respectively the transfer and the hydrolysis of the sugar moiety.

First, our works have focused on the study of O-GlcNAcylation implication in the

control of Xenopus laevis oocyte meiotic resumption, a process analogous to the G2/M

transition of the cell cycle of somatic cells. This G2/M transition is characterized by the

simultaneous activation of the MPF (M-phase Promoting Factor), the universal

regulator of the M-Phase entry and of the MAPK Erk2 pathway. We demonstrated the

existence of a rise in oocyte O-GlcNAcylation at the G2/M transition [1] that was

essential to this process since inhibition of OGT prevented the activation of the MPF

and of the MAPK pathway [2]. Then we studied the variations of O-GlcNAcylation

occurring during the cell cycle of synchronised somatic cells and again we observed an

increase in O-GlcNAcylation at the G2/M transition whereas we demonstrated a

decrease of these glycosylation at the G1/S boundary correlated with an increased

OGA activity [3]. Moreover, we recently proved that serum stimulated cell cycle entry

promoted the synthesis of OGT and that the enzyme was necessary to the G0/G1

transition since its down-regulation by RNA interference prevented the activation of the

52

PI3K/Akt and of the MAP kinase pathways and led to a decrease in cyclin D1

expression [4].

By a combination of several approaches (proteomics, immunoprecipitation and Click-

chemistry), we were able to identify 24 functionally different O-GlcNAcylated proteins in

matured (M-phase) oocytes among which the proliferating cell nuclear antigen (PCNA)

and the MAPK Erk2 [5]. We also identified 58 proteins differentially O-GlcNAcylated at

the G1/S boundary including several components of the MCM 2-7 complex that take

parts in the regulation of DNA replication [3]. Finally, preliminary results showed that

cyclin D1, a central regulator of the G1 phase is O-GlcNACylated. Taken together our

results demonstrate that O-GlcNAcylation dynamic is essential for the good progress of

the cell cycle at all steps since it modifies master regulators of this process.

HUMAN SIGLEC-9 BINDING TO HYALURONIC ACID DAMPENS NEUTROPHIL ACTIVATION AND IS SUBVERTED BY THE INVASIVE BACTERIAL PATHOGEN GROUP A Streptococcus Dr. Ismael SECUNDINO. University of California, San Diego, EUA Sialic acid-binding Ig-Like Lectins (Siglecs) are immunoregulatory receptors on

leukocytes. A number of CD33-related human Siglecs (CD33rSiglecs) possess

intracellular inhibitory domains (ITIMs) that act to blunt activatory signaling

cascades. Siglec-9, abundantly expressed on human neutrophils, is known to engage

terminal sialic acid residues on cell surface glycoconjugates, to limit baseline neutrophil

activation. We previously described how the neonatal pathogen group B Streptococcus

(GBS) expresses a sialylated exopolysaccharide capsule that can engage Siglec-9 to

blunt neutron phil bactericidal responses and promote its own survival. Recently, in

screening the lectin repertoire of human Siglec-9, we made the unexpected discovery

that Siglec-9 strongly and specifically binds to high molecular weigh hyaluronic acid

(HMW-HA), through a region of its V-set domain distinct from the sialic acid-binding

domain. HA engagement by Siglec-9 limits neutrophil activation phenomenon including

oxidative burst, proinflammatory cytokine release and elaboration of DNA-based

53

extracellular traps (NETs), suggesting HA represents an important "self-associated

molecular pattern". The leading human pathogen group A Streptococcus (GAS)

possesses a capsule composed of HA indistinguishable from the host

polysaccharide. GAS HA is strongly upregulated in the shift of GAS from localized to

invasive bloodstream infection, and is known to promote bacterial resistance to

neutrophil and antimicrobial peptide killing. Using WT and isogenic GAS capsule-

deficient mutants, we show the pathogen can engage neutrophils and inhibit oxidative

burst and NET formation in a Siglec-9- and HA-dependent manner, promoting its own

survival. Thus, a single immunoregulatory lectin receptor on human neutrophils binds to

two different ubiquitous glycans and is subverted through molecular mimicry by two

different leading human pathogens.

54

NDICE DE AUTORES DE TRABAJOS

LIBRES POR TEMA

Biosntesis y metabolismo de glicoconjugados

[BM]

1. Acua Avila Pedro Estanislao BM-11

2. Alvarado-Vsquez Noe BM-05

3. Aquino Gil M. BM-17

4. Aquino Gil M. O. BM-09

5. Aragn Cuervas F. BM-18

6. Arenas-Del ngel MC. BM-15

7. Arenas-Ros Edith BM-04

8. Balderas-Anaya Madeline BM-16

9. Blanco-Labra A. BM-07

10. Calvillo Minerva BM-12

11. Campos-Guilln J. BM-07

12. Campos-Pea V. BM-02

13. Carbajal Aguilera K. BM-03

14. Castaeda Saucedo Eduardo BM-14

55

15. Castro Guilln JL. BM-07

16. Chavelas-Adame Eneas Alejandro BM-14

17. Chvez R. BM-15

18. Cisneros Solano A. BM-18

19. Corts Barberena Edith BM-04

20. Cruz Santiago J. BM-09

21. Cruz-Hernndez A. BM-07

22. Dehennaut V. BM-17

23. Della-Valle Daniela BM-12

24. Daz-Garca E.J. BM-10

25. Daz-Jimnez Diana Fabiola BM-01

26. Domnguez-Salazar E. BM-02

27. Espinosa Blanca BM-12

28. Ferriz-Martnez R. BM-07

29. Fierro Reyna BM-04

30. Flores-Carren Arturo BM-01

31. Foulquier F. BM-17

32. Garca-Gasca T. BM-07

33. Garca-Surez MD. BM-02

34. Garca-Surez MD. BM-03

35. Geiser-Dawn BM-08

36. Gmez-Olivares JL. BM-02

56

37. Gmez-Olivares JL. BM-03

38. Gonzlez-Hernndez Roberto de Jess BM-01

39. Guedri K. BM-17

40. Guevara Jorge BM-05

41. Guevara Jorge BM-12

42. Gutirrez-Ruiz MC. BM-03

43. Guzmn-Partida Ana BM-08

44. Hernndez Cruz P. BM-18

45. Hernndez-Chvez Marco Josu BM-01

46. Hernndez-Snchez Fernando BM-16

47. Illescas Barbosa D. BM-09

48. Isidro-Lzaro J. BM-10

49. Lagarda-Daz Irlanda BM-08

50. Lascurain R. BM-15

51. Lefebvre T. BM-17

52. Lefebvre Tony BM-05

53. Len-Galvn Miguel A. BM-04

54. Limon Daniel BM-05

55. Lpez Cortz Mara del Socorro BM-11

56. Lpez Durn RM. BM-02

57. Lpez-Durn RM. BM-03

58. Lpez-Prez Mercedes Guadalupe BM-06

57

59. Lozano Liliana BM-05

60. Martnez Cruz M. BM-18

61. Martnez-Alarcn D. BM-07

62. Martnez-Duncker Ivan BM-13

63. Martnez-Quezada R. BM-02

64. Matias Cervantes Carlos BM-18

65. Michalski J.C. BM-17

66. Mollicone Rosella BM-13

67. Morales Arroyo Ivis Ibrahum BM-03

68. Morales-Arroyo I. BM-02

69. Mora-Montes Hctor Manuel BM-01

70. Mora-Montes Hctor Manuel BM-06

71. Navarro-Arias Mara de Jess BM-06

72. Olivier-Van Stichelen S. BM-17

73. Patio Morales Carlos Csar BM-14

74. Prez-Campos E. BM-18

75. Prez-Cervera Y. BM-09

76. Perez-Cervera Y. BM-17

77. Prez-Santiago A.D. BM-10

78. Pina Canseco MS. BM-18

79. Pina-Canseco M.S. BM-10

80. Quezada-Martnez R. BM-03

58

81. Robles-Burgueo M. Refugio BM-08

82. Rodriguez Tobn Ahizer BM-04

83. Salinas Arreortua N. BM-02

84. Salinas Marin Roberta BM-13

85. Salinas-Arreortua N. BM-03

86. Snchez-Medina M.A. BM-10

87. Serrano H. BM-02

88. Serrano H. BM-03

89. Serrano Luna Armando Levith BM-14

90. Solrzano Mata C. J. BM-17

91. Solrzano-Mata C.J. BM-09

92. Tamez-Castrelln Alma Karina BM-01

93. Torres Martha BM-16

94. Trujillo-Esquivel Jos Elas BM-01

95. Vasquez Murrieta Mara Soledad BM-11

96. Vzquez-Moreno Luz BM-08

97. Vega-Hernndez Ricardo BM-16

98. Winzerling Joy BM-08

99. Zenteno E. BM-15

100. Zenteno Edgar BM-05

101. Zenteno Galindo E. BM-09

102. Zomosa Viviana BM-05

59

Desrdenes de la glicosilacin y

enfermedades raras [D]

103. Asteggiano CG. D-05

104. Asteggiano CG. D-06

105. Bistu Milln MB. D-05

106. Bolado Martnez Enrique D-04

107. Candia Plata Mara del Carmen D-04

108. Chacn S. D-05

109. D Grinberg D-06

110. De la Cruz Castillo Doris Yared D-01

111. Dodelson de Kremer R. D-05

112. EG Martnez Domenech D-06

113. Elso de Berberian G. D-05

114. G Matthijs D-06

115. Gallegos Velasco B. D-02

116. Gutirrez Candia Sergio D-04

117. Hernndez Cruz P. D-01

118. Hernndez Cruz P. D-02

119. Hernndez Cruz Pedro D-03

120. Hernndez Huerta Mara Teresa D-03

121. Lpez Soto Luis Fernando D-04

60

122. Lujn Camarillo Christian I. D-04

123. MA Delgado D-06

124. Martnez Cruz Margarito D-03

125. Martnez Cruz Ruth D-03

126. Mayoral Prez-Campos Laura D-03

127. N Guelbert D-06

128. P Sarrin D-06

129. Prez Campos E. D-01

130. Prez-Campos E. D-02

131. Prez-Campos Eduardo D-03

132. Pina-Canseco Socorro D-03

133. Pineda Orozco Dmaris D-04

134. R Dodelson de Kremer D-06

135. Rios Lpez Karen I. D-02

136. S Balcells D-06

137. Soto Guzmn Jess Adriana D-04

138. Spcola N. D-05

139. Syravegna M. D-05

140. Velasco Belm D-01

Glicobiologa de las enfermedades

infecciosas [EI]

61

141. Acosta-Blanco EI-05

142. Agis- Jurez Ral A. EI-03

143. Amyris Sandra EI-04

144. Barbosa Sabanero EI-06

145. Carmona Baca Karla EI-07

146. Cervantes-Landn A.Y. EI-01

147. Espinoza B. EI-01

148. Fernndez Gonzlez C.D. EI-09

149. Flores Moreno Karen EI-02

150. Flores Villavicencio L. EI-06

151. Fuentes-Romero EI-05

152. Garca-Ruz Viridiana EI-03

153. Gonzlez Canto A. EI-09

154. Gonzlez Garca C. Ramn EI-08

155. Gutirrez Huante Kathya EI-08

156. Huebner J. EI-02

62

157. Lpez Vancell R. EI-09

158. Lpez Vidal Y. EI-02

159. Lpez-Ramrez Luz A. EI-07

160. Lpez-Vidal Yolanda EI-03

161. Lozoya-Prez Nancy E. EI-07

162. Martnez Duncker R. Ivn EI-08

163. Martnez I. EI-01

164. Mndez Capdeville Teresita Mildred EI-10

165. Mora-Montes Hctor M. EI-07

166. Nequiz Avendao M. EI-09

167. Newburg EI-05

168. Ordua Patricia EI-03

169. Ortega Francisco EI-04

170. Ortega-Francisco EI-05

171. Perez Tamayo R. EI-09

172. Ramos Martnez E. EI-09

63

173. Rosas Alquicira Graciela EI-05

174. Ruiz-Palacios Y.J. EI-05

175. Sabanero Lpez Myrna EI-06

176. Servn-Gonzlez Luis EI-03

177. Solano Rodrguez Luciana EI-10

178. Soto Arredondo K. EI-06

179. Soto-Ramrez EI-05

180. Viveros-Rogel M. EI-05

Cncer [C]

181. Acevedo Prez Miguel ngel C-04

182. Aguilar-Lemarroy A. C-07

183. Almazo-Domnguez Roco C-06

184. Apresa-Garca T. C-07

185. Cant de Len D. C-05

186. Ceballos-Reyes Guillermo C-03

187. Ceja-Utrera F.J. C-07

64

188. Daz y Orea A. C-07

189. Encarnacin-Guevara S. C-05

190. Escobar-Snchez Ma. Luisa C-01

191. Fernndez-Herrera Mara Antonieta C-01

192. Flores-Mendoza Lilian C-06

193. Galicia-Morales Isaas C-01

194. Galindo Hernandez O. C-02

195. Gallardo-Rincn D. C-05

196. Gallegos Velasco B. C-04

197. Garca-Lpez Roco Berenice C-06

198. Garibay-Cerdenares OL. C-05

199. Gonzlez-Ballesteros Mauricio M. C-01

200. Gutirrez Iglesias Gisela C-03

201. Hernndez Cruz P. C-04

202. Hernndez-Ortz M. C-05

203. Hernndez-Pacheco R.E. C-07

65

204. Hernndez-Pacheco Raquel Esneidy C-06

205. Hernndez-Ramrez VI. C-05

206. Jave-Suarez L.F. C-07

207. Lpez-Muoz Hugo C-01

208. Mendieta-Carmona V. C-07

209. Njera Garca Nayelli C-03

210. Navarro Tito N. C-02

211. Osorio-Trujillo JC. C-05

212. Palma Lara Icela C-03

213. Prez Campos E. C-04

214. Prez Salazar E. C-02

215. Pina Canseco MS. C-04

216. Ramrez-Gutirrez Ramss Elas C-01

217. Reyes-Leyva J.R. C-07

218. Reyes-Leyva Julio C-06

219. Reyes-Salinas J.S. C-07

66

220. Rivera-Jurez M.A. C-07

221. Rodea-vila C. C-07

222. Rosas-Murrieta N.H. C-07

223. Rubio-Gayosso Ivan C-03

224. Snchez-Snchez Luis C-01

225. Sandoval-Ramrez Jess C-01

226. Santos-Lpez G. C-07

227. Santos-Lpez Gerardo C-06

228. Serna Marquez N. C-02

229. Sosa-Jurado F. C-07

230. Talams-Rohana P. C-05

231. Vallejo-Ruiz V. C-07

232. Vallejo-Ruiz Vernica C-06

233. Varela Castillo Omar C-03

234. Vargas-Maldonado M.T. C-07

235. Vsquez Aquino Marisol C-04

67

236. Vzquez-Zamora V.J. C-07

237. Villegas Comonfort S. C-02

238. Zamora-Guinez I. C-07

Glycobiotechnology [T]

239. Aguilera P. T-15

240. Aragn-Cuevas F. T-11

241. Arellano Crdenas S. T-06

242. Arellano Crdenas Sofa T-03

243. Bedoya-Lpez Andrea T-12

244. Bchs Jochen T-07

245. Cardos San Jorge F. T-01

246. Carranza-Rosales, P. T-10

247. Casabuono A. T-10

248. Chang Caldern J. T-01

249. Contreras-Esquivel J.C. T-08

250. Contreras-Esquivel J.C. T-10

251. Cornejo Mazn Maribel T-03

252. Cornejo Mazn Maribel T-05

253. Couto S.A. T-10

254. Cruz-Guerrero Alma T-04

68

255. Escamilla-Lozano Yolanda T-04

256. Espita C. T-14

257. Espitia Clara T-07

258. Estrada de los Santos P. T-08

259. Estrada Karel T-12

260. Farres A. T-15

261. Fernndez Santana V. T-01

262. Fragoso Castro Inari Idalith T-05

263. Galindo-Msico J.H. T-08

264. Gamboa-Suasnavart T-07

265. Garca Garibay Mariano T-04

266. Garca Rivero D. T-01

267. Garrido Arteaga R. T-01

268. Gavilondo Cowley J.V. T-13

269. Gomez-Ruiz Lorena T-04

270. Guilln D. T-14

271. Guilln D. T-15

272. Hernndez A. Vanessa T-09

273. Hernndez Fernndez M. A. T-06

274. Isidro-Lzaro J. T-02

275. Kloeckner Wolf T-07

276. Lpez Cortz M.S. T-06

69

277. Lpez Cortz Mara del Socorro T-05

278. Luna Ramrez Karem Yazmin T-03

279. Manzo Sandoval A. T-13

280. Marn-Palacio Luz D. T-07

281. Martnez Sotelo Jos A. T-07

282. Martnez-Cruz M. T-11

283. Medina Escutia M.E. T-13

284. Medina Flores Y. T-13

285. Moreno-Mendieta S. T-14

286. Moreno-Mendieta S. T-15

287. Morlett-Chvez J.A. T-10

288. Palomares Laura T-09

289. Pedroso Fernndez J. T-01

290. Prez-Santiago A.D. T-02

291. Pina-Canseco M.S. T-02

292. Ramrez Octavio T. T-09

293. Ramirez Octavio T. T-12

294. Ramn Gallegos E. T-13

295. Ramn-Delgado M.J. T-10

296. Rodrguez Noda L. M. T-01

297. Rodrguez-Sanoja, R. T-14

298. Rodrguez-Sanoja, R. T-15

70

299. Rodrguez-Serrano Gabriela T-04

300. Snchez S. T-15

301. Snchez-Esperanza F. T-11

302. Sanchez-Flores Alejandro T-12

303. Snchez-Medina M.A. T-02

304. Serrano-Rodrguez Y. T-01

305. Serratob Jos A. T-09

306. Servn-Gonzlez Luis T-07

307. Sosa-Ancona Erik T-04

308. Trujillo-Roldn Mauicio A. T-12

309. Trujillo-Roldn Mauricio A. T-07

310. Valds Balbn Y. T-01

311. Valdez-Cruz Norma A. T-07

312. Valdez-Cruz Norma A. T-12

313. Vrez Bencomo V. T-01

Inmunoglicobiologa [I]

314. Acevedo Prez Miguel ngel I-08

315. Agundias Mata C. I-03

316. Agundis Concepcin I-04

317. Alpuche Osorno J.J. I-03

318. Campa Angel I-04

71

319. Cancino Daz J. C. I-12

320. Cancino Daz M. E. I-12

321. Candia Plata Ma. Del Carmen I-07

322. Carvajal Dosamantes Armando I-07

323. Castro Leyva V. I-12

324. Cervantes Alfaro M. I-01

325. Eslava C. I-02

326. Espinosa Cueto P. I-09

327. Estrada Gutierrez G. I-12

328. Fenton Navarro B. I-01

329. Gallegos Velasco B. I-08

330. Galvn Moroyoqui Jos I-07

331. Garca Aguilar T.C. I-09

332. Garca Villa Denisse I-07

3