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dc.creatorGarcia, Javier E. 
dc.creatorFierro, Ricardo 
dc.creatorPuentes, Alvaro 
dc.creatorCortés, Jimena 
dc.creatorBermudez, Adriana 
dc.creatorCifuentes, Gladys 
dc.creatorVanegas, Magnolia 
dc.creatorPatarroyo, Manuel E. 
dc.date.accessioned2020-08-06T16:20:20Z
dc.date.available2020-08-06T16:20:20Z
dc.date.created2007-04-06
dc.identifier.issnISSN: 0006-291X
dc.identifier.issnEISSN: 1090-2104
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/25963
dc.description.abstractA hepatitis C virus E2 protein-derived sequence was selected for studying the effect of N-glycosylation on the peptide chain’s conformational structure. The results suggested that the 534TDVF537 motif contained in peptide 33402 (529WGENDTDVFVLNNTRY544) had a type III ?-turn, relevant in antigen recognition of polyclonal antibodies, binding to human cells, and binding to HLA DRB1?0401 molecules. N-Glycopeptides derived from this sequence contained monosaccharides in Asn532. N-Glycopeptides presented differences in peptide chain structure compared to non-glycosylated peptides. Peptide 33402 specifically bound to human cells, specificity becoming lost when it was N-glycosylated. N-Glycosylation decreased antigen recognition of mouse polyclonal sera against this sequence. N-Glycopeptide binding to HLA DRB1?0401 molecules was similar to that presented by non-glycosylated peptide, indicating that N-glycosylation did not affect binding to HLA DRB1?0401 molecules. N-Glycosylation induced changes at structural and functional level which could be relevant for modulating human cell binding properties and antibody recognition.
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.relation.ispartofBiochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.355, No.2 (2007); pp.409-418
dc.relation.urihttps://www.sciencedirect.com/science/article/abs/pii/S0006291X07002422
dc.sourceBiochemical and Biophysical Research Communications
dc.titleMonosaccharides modulate HCV E2 protein-derived peptide biological properties
dc.typearticle
dc.publisherElsevier
dc.subject.keywordN-Glycopeptide
dc.subject.keywordN-Glycosylation
dc.subject.keywordHCV
dc.subject.keywordHLA-DR molecules
dc.rights.accesRightsinfo:eu-repo/semantics/restrictedAccess
dc.type.spaArtículo
dc.rights.accesoRestringido (Acceso a grupos específicos)
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.identifier.doihttps://doi.org/10.1016/j.bbrc.2007.01.167
dc.title.TranslatedTitleLos monosacáridos modulan las propiedades biológicas del péptido derivado de la proteína E2 del VHC
dc.relation.citationEndPage418
dc.relation.citationIssueNo. 2
dc.relation.citationStartPage409
dc.relation.citationTitleBiochemical and Biophysical Research Communications
dc.relation.citationVolumeVol. 355


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