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Reactivity of synthetic peptides representing selected sections of hepatitis C virus core and envelope proteins with a panel of hepatitis C virus‐seropositive human plasma
Author(s) -
Jackson Peter,
Petrik Juraj,
Alexander Graeme J. M.,
Pearson Gavin,
Allain JeanPierre
Publication year - 1997
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/(sici)1096-9071(199701)51:1<67::aid-jmv11>3.0.co;2-1
Subject(s) - hypervariable region , hepatitis c virus , virology , immunogenicity , virus , biology , antibody , peptide , flaviviridae , hepacivirus , viral envelope , microbiology and biotechnology , immunology , biochemistry
A series of 54 synthetic peptides, 15–20 residues long, that represented selected parts of the structural proteins of hepatitis C virus (HCV) were tested for immunoreactivity with a panel of 45 plasma samples from potential blood donors who were known to be seropositive for anti‐HCV. Most of the ten peptides that represented the core protein showed reactivity with most of the panel samples. All except one of the 20 peptides that represented non‐hypervariable regions of envelope proteins E1 and E2 showed little or no reactivity. In contrast, 18 of the the 24 peptides that represented variants of the hypervariable region 1 of the E2 protein reacted with at least one panel sample. Notably, 40% of the panel samples cross‐reacted with two or more different peptides sequences some of which differed by more than 50%. Two panel samples each cross‐reacted with seven different peptide sequences. The results suggest a broad anti‐hypervariable region antibody specificity in many anti‐HCV‐seropositive samples and possible limits on the mutability of hypervariable region sequences. The work contributes to understanding the immunogenicity and persistence of HCV. J Med Virol 51:67–79, 1997. © 1997 Wiley‐Liss, Inc.