Article ID Journal Published Year Pages File Type
2088007 Journal of Immunological Methods 2015 5 Pages PDF
Abstract

•Sequence analysis of proteins VP1, VP2 and VP3 was achieved by ANTHEPROT software.•Twelve peptides were selected for spot synthesis on functionalized cellulose paper.•Two peptides showed anti-IgG antibodies recognition and were synthesized on resin.•A peptide dimer showed 87–100% of recognition by IgG and 100% specificity.•This dimer showed 100% of recognition by IgM and 100% specificity by MABA.

VP1, VP2 and VP3 molecules of hepatitis A virus are exposed capsid proteins that have shown to be antigenic and are used for diagnosis in recombinant-antigen commercial kits. In this study, we developed a sequence analysis in order to predict diagnostic peptide epitopes, followed by their spot synthesis on functionalized cellulose paper (Pepscan). This paper with synthetic peptides was tested against a sera pool of hepatitis A patients. Two peptide sequences, that have shown an antigenic recognition, were selected for greater scale synthesis on resin. A dimeric form of one of these peptides (IMT-1996), located in the C-Terminus region of protein VP1, was antigenic with a recognition frequency of 87–100% of anti-IgG antibodies and 100% of anti-IgM antibodies employing the immunological assays MABA and ELISA. We propose peptide IMT-1996, with less than twenty residues, as a cheaper alternative for prevalence studies and diagnosis of hepatitis A infection.

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