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Monosaccharides modulate HCV E2 protein-derived peptide biological properties
dc.creator | Garcia, Javier E. | spa |
dc.creator | Fierro, Ricardo | spa |
dc.creator | Puentes, Alvaro | spa |
dc.creator | Cortés, Jimena | spa |
dc.creator | Bermudez, Adriana | |
dc.creator | Cifuentes, Gladys | spa |
dc.creator | Vanegas, Magnolia | spa |
dc.creator | Patarroyo, Manuel E. | spa |
dc.date.accessioned | 2020-08-06T16:20:20Z | |
dc.date.available | 2020-08-06T16:20:20Z | |
dc.date.created | 2007-04-06 | spa |
dc.description.abstract | A 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. | eng |
dc.format.mimetype | application/pdf | |
dc.identifier.doi | https://doi.org/10.1016/j.bbrc.2007.01.167 | |
dc.identifier.issn | ISSN: 0006-291X | |
dc.identifier.issn | EISSN: 1090-2104 | |
dc.identifier.uri | https://repository.urosario.edu.co/handle/10336/25963 | |
dc.language.iso | eng | spa |
dc.publisher | Elsevier | spa |
dc.relation.citationEndPage | 418 | |
dc.relation.citationIssue | No. 2 | |
dc.relation.citationStartPage | 409 | |
dc.relation.citationTitle | Biochemical and Biophysical Research Communications | |
dc.relation.citationVolume | Vol. 355 | |
dc.relation.ispartof | Biochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.355, No.2 (2007); pp.409-418 | spa |
dc.relation.uri | https://www.sciencedirect.com/science/article/abs/pii/S0006291X07002422 | spa |
dc.rights.accesRights | info:eu-repo/semantics/restrictedAccess | |
dc.rights.acceso | Restringido (Acceso a grupos específicos) | spa |
dc.source | Biochemical and Biophysical Research Communications | spa |
dc.source.instname | instname:Universidad del Rosario | |
dc.source.reponame | reponame:Repositorio Institucional EdocUR | |
dc.subject.keyword | N-Glycopeptide | spa |
dc.subject.keyword | N-Glycosylation | spa |
dc.subject.keyword | HCV | spa |
dc.subject.keyword | HLA-DR molecules | spa |
dc.title | Monosaccharides modulate HCV E2 protein-derived peptide biological properties | spa |
dc.title.TranslatedTitle | Los monosacáridos modulan las propiedades biológicas del péptido derivado de la proteína E2 del VHC | spa |
dc.type | article | eng |
dc.type.hasVersion | info:eu-repo/semantics/publishedVersion | |
dc.type.spa | Artículo | spa |