Monosaccharides modulate HCV E2 protein-derived peptide biological properties.
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.
Garcia
Javier E
JE
Fundación Instituto de Immunología de Colombia, Carrera 50 #26-00, Bogotá, Colombia.
Fierro
Ricardo
R
Puentes
Alvaro
A
Cortés
Jimena
J
Bermúdez
Adriana
A
Cifuentes
Gladys
G
Vanegas
Magnolia
M
Patarroyo
Manuel E
ME
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*
D009005:Monosaccharides; D010455:Peptides; D014764:Viral Proteins