Publication:
H-2Ld class I molecule protects an HIV N-extended epitope from in vitro trimming by endoplasmic reticulum aminopeptidase associated with antigen processing

dc.contributor.authorSamino, Yolanda
dc.contributor.authorLorente, Elena
dc.contributor.authorJimenez, Mercedes
dc.contributor.authorGarcia, Ruth
dc.contributor.authorVal, Margarita del
dc.contributor.authorLopez, Daniel
dc.contributor.authorInfantes, Susana
dc.contributor.funderComunidad de Madrid (España)
dc.contributor.funderMinisterio de Educación y Ciencia (España)
dc.contributor.funderInstituto de Salud Carlos III
dc.date.accessioned2020-07-06T05:53:54Z
dc.date.available2020-07-06T05:53:54Z
dc.date.issued2010-04-01
dc.description.abstractIn the classical MHC class I Ag presentation pathway, antigenic peptides derived from viral proteins by multiple proteolytic cleavages are transported to the endoplasmic reticulum lumen and are then exposed to ami-nopeptidase activity. In the current study, a long MHC class I natural ligand recognized by cytotoxic T lymphocytes was used to study the kinetics of degradation by aminopeptidase. The in vitro data indicate that this N-extended peptide is efficiently trimmed to a 9-mer, unless its binding to the MHC molecules protects the full-length peptide.es_ES
dc.description.peerreviewedes_ES
dc.description.sponsorshipWe thank Dr. A. K. Stout of the NIH Tetramer Facility for providing the peptide/MHC complex reagent. This work was suppor ted by grants provi ded by Programa Ramón y Cajal, and Fundación FIPSE to D. L.; by grants provided by Comunidad de Madrid and Ministerio de Educación y Ciencia to M. D. V.; and by a joint grant provided by Instituto de Salud Carlos III to D. L., and M. D. V.es_ES
dc.format.number7es_ES
dc.format.page3351-5es_ES
dc.format.volume184es_ES
dc.identifier.citationJ Immunol . 2010 Apr 1;184(7):3351-5.es_ES
dc.identifier.doi10.4049/jimmunol.0901560es_ES
dc.identifier.e-issn1550-6606es_ES
dc.identifier.issn0022-1767es_ES
dc.identifier.journalJournal of immunology (Baltimore, Md. : 1950)es_ES
dc.identifier.pubmedID20200278es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/10655
dc.language.isoenges_ES
dc.publisherAmerican Association of Immunologists (AAI)
dc.relation.publisherversionhttps://doi.org/10.4049/jimmunol.0901560es_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.rights.accessRightsopen accesses_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAnimalses_ES
dc.subject.meshAntigen Presentationes_ES
dc.subject.meshCells, Culturedes_ES
dc.subject.meshEndoplasmic Reticulumes_ES
dc.subject.meshEpitopes, T-Lymphocytees_ES
dc.subject.meshH-2 Antigenses_ES
dc.subject.meshHIV Envelope Protein gp120es_ES
dc.subject.meshHistocompatibility Antigen H-2Des_ES
dc.subject.meshHumanses_ES
dc.subject.meshLeucyl Aminopeptidasees_ES
dc.subject.meshMicees_ES
dc.subject.meshRecombinant Proteinses_ES
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationes_ES
dc.titleH-2Ld class I molecule protects an HIV N-extended epitope from in vitro trimming by endoplasmic reticulum aminopeptidase associated with antigen processinges_ES
dc.typeresearch articlees_ES
dc.type.hasVersionAMes_ES
dspace.entity.typePublication
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