Immunogenicity of Synthetic Peptides Corresponding to Various Epitopes of the Human Immunodeficiency Virus Envelope Protein
The envelope gene of the human immunodeficiency virus (HIV) encodes a 160 kd precursor protein which during virus maturation is cleaved into 120 kd and 41 kd proteins, respectively 1,2. The outer (gp120) and the transmembrane (gp41) proteins are non-covalently associated and are involved in virus infectivity 3-6. The gp120 has been suggested to bear the CD4 binding site mediating the attachment of the virus to the CD4 antigen 4,7. Recently, using deletion mutants8 and monoclonal antibodies9 the CD4 binding site was mapped within the amino acid sequence 420–437 of the gp120 protein. The comparison of sequences among the fusogenic sites of various viruses with the sequence of HIV predicted that the sequence 526-535 of the amino terminal part of gp41 to be the fusogenic site of HIV-I10. Beside these sites playing an important role in infectivity, the gp160 protein bears B cell epitopes inducing neutralizing antibodies and T cell epitopes recognized by T helper and cytotoxic T cells (data reviewed in 11). To date, the best characterized neutralizing epitope is the so called principle neutralizing determinant or PND which maps within the cysteine loop of the gp120 protein 12,13. It has been suggested that the hexapeptide, GPGRAF, which is conserved in the majority of known HIV-1 isolates is responsible for the induction of broadly neutralizing antibodies14. Recently, it was shown that the peptide corresponding to amino acid residues 254–274 of gp120 represents an immunodominant epitope capable of inducing antibodies in HIV-1 infected patients15. Also the C-terminal peptide 504–518 of gp120 reacted with sera of HIV-infected patients16. In the present work, we present data on the immunogenicity of 4 peptides corresponding to various epitopes of the gp160 protein in various animal species.
KeywordsHepatitis Tyrosine Iodine Cysteine Lysine
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