Monosaccharides modulate HCV E2 protein-derived peptide biological properties Academic Article

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

publication date

  • 2007/4/6

edition

  • 355

keywords

  • Antibodies
  • Antigens
  • Cells
  • Glycopeptides
  • Glycosylation
  • HLA-DRB1*04:01 antigen
  • Hepacivirus
  • Molecules
  • Monosaccharides
  • Peptides
  • Proteins
  • Serum
  • Viruses

International Standard Serial Number (ISSN)

  • 0006-291X

number of pages

  • 10

start page

  • 409

end page

  • 418