Mimicry of the immunodominant conformation-dependent antigenic site of hepatitis A virus by motifs selected from synthetic peptide libraries.

摘要: Hepatitis A virus (HAV) is a positive-strand RNA with genome length of approximately 7,480 nucleotides. Although HAV morphogenesis thought to be similar that poliovirus, the prototype picornavirus, complete characterization antigenic structure this remains elusive. All available evidences, however, support existence, on virions and empty capsids, an immunodominant neutralization site which conformation dependent whose involves residues both VP1 VP3 capsid proteins. This particular feature difficulty obtaining high yield in tissue cultures make ideal target for developing synthetic peptides simulate its main determinant. To end we utilized, present work, divide-couple-recombine approach generate random library composed millions different hexapeptides. vast was screened well-characterized anti-HAV monoclonal antibody. By strategy identified peptide reacted specifically polyclonal antibodies and, mice, induced specific anti-virus immune response. Furthermore, could also used enzyme-linked immunosorbent assay revealing primary immunoglobulin M response sera acutely infected human patients. Interestingly, no sequence homology found between proteins VP3. Collectively, these data represent additional important paradigm mimotope capable mimicking determinant unknown tertiary structure.