Immune response and epitope mapping of a candidate hiv‐1 p17 vaccine hgp30

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Abstract
A thirty amino acid synthetic peptide (HGP30) representing the conserved region of HIV‐1 p17 induced high titer antibodies to the native pl7 in rabbits. This immune sera neutralized HIV‐1 replication in cell culture and one of the high titer antisera also inhibited CD4‐dependent cell fusion. Pepscan analysis with overlapping nonapeptides derived from the sequence of HIV‐1 pl7 identified the sequence (KE) ALDKIEE (EQ) as the major antibody binding site. Sera of 9% of AIDS patients (7/76) and 18% of HIV‐1 seropositive healthy homosexuals (40/223) were positive for HGP30 antibodies. Decline in HIV‐1 pl7 antibodies has been shown to be related to disease progression in both children and adults, suggesting that HIV‐1 pl7 antibodies may be protective. Hence, a synthetic HIV‐1 pl7 peptide, representing the immunodominant epitope, could be useful as a candidate vaccine for immunization of HIV‐1 seronegative or seropositive healthy homosexuals.