Monosaccharides modulate HCV E2 protein-derived peptide biological properties

Adriana Janneth Bermudez Quintero, Javier E García, Ricardo Fierro, Alvaro Puentes, Jimena Cortés, Gladys Cifuentes, Magnolia Vanegas Murcia, Manuel Elkin Patarroyo

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4 Scopus citations


A hepatitis C virus E(2) protein-derived sequence was selected for studying the effect of N-glycosylation on the peptide chain's conformational structure. The results suggested that the (534)TDVF(537) motif contained in peptide 33402 ((529)WGENDTDVFVLNNTRY(544)) had a type III beta-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 Asn(532). 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
Original languageEnglish (US)
Pages (from-to)409-418
Number of pages10
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Apr 6 2007


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