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Synthetic peptides for the immunodiagnosis of hepatitis A virus infection
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 synth...
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Published in: | Journal of immunological methods 2015-12, Vol.427, p.1-5 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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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•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. |
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ISSN: | 0022-1759 1872-7905 |
DOI: | 10.1016/j.jim.2015.08.013 |