title: Monosaccharides modulate HCV E2 protein-derived peptide biological properties.
abstract: 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.
authors.affiliation: Fundación Instituto de Immunología de Colombia, Carrera 50 #26-00, Bogotá, Colombia.
authors.forename: Javier E
authors.initials: JE
authors.lastname: Garcia
authors.forename: Ricardo
authors.initials: R
authors.lastname: Fierro
authors.forename: Alvaro
authors.initials: A
authors.lastname: Puentes
authors.forename: Jimena
authors.initials: J
authors.lastname: Cortés
authors.forename: Adriana
authors.initials: A
authors.lastname: Bermúdez
authors.forename: Gladys
authors.initials: G
authors.lastname: Cifuentes
authors.forename: Magnolia
authors.initials: M
authors.lastname: Vanegas
authors.forename: Manuel E
authors.initials: ME
authors.lastname: Patarroyo
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004797:Enzyme-Linked Immunosorbent Assay; D006031:Glycosylation; D016174:Hepacivirus / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009005:Monosaccharides / Q000494:pharmacology*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000378:metabolism / Q000494:pharmacology*; D011485:Protein Binding; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*
chemical_list: D009005:Monosaccharides; D010455:Peptides; D014764:Viral Proteins