The synthesis and immunological activity of a peptide related to collagen.
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Biomedical subjects
Publications and source records attributed to E Benjamini.
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Various mouse strains were immunized with either SRV-1 or SRV-2 virus adsorbed on alum. Seven to 14 days later spleen cells were removed, and spleen cells were cultured with varying amounts of SRV-1 virus and SRV-2 virus, or varying amounts of selected SRV-1 and SRV-2 synthetic envelope peptides to determine their ability to initiate T cell proliferative responses. Our studies demonstrated that all mouse strains tested gave strong proliferative responses with SRV-2 virus. In contrast, SRV-1 virus induced T cell proliferative responses only in H-2k mouse strains. This apparent major histocompatibility complex (MHC)-restriction of SRV-1 virus-induced T cell proliferation correlates with the increased pathogenicity of SRV-1 virus in rhesus monkeys. The SRV envelope peptide 233-249 which is shared by both SRV-1 and SRV-2 virus initiates strong proliferative responses in both SRV-1 and SRV-2 virus immunized mice. The SRV-2 envelope peptide 96-102 initiates significant proliferative responses in SRV-2 immunized mice, and constitutes both a T and B cell epitope. The SRV-2 envelope peptide 127-152 has a 70% homology with the C-terminal region of SRV-1 peptide 142-167. The ability of SRV-2 peptide 127-152 to initiate T cell proliferation in SRV-1 virus immunized mice and the failure of the SRV-1 peptide 142-162 to initiate proliferation suggests that the region encompassing residues 160-167 must represent a T cell epitope in mice immunized with SRV-1 virus.
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We analyzed SIV-specific monkey sera to localize B-cell epitopes of the envelope glycoprotein of SIV (gp130), using overlapping synthetic peptides representing the entire SIV gp130 protein and sera from experimentally infected monkeys and monkeys immunized with whole, inactivated SIV. A B-cell epitope which induces neutralizing antibody production and T-cell responses was characterized as well as a new B-cell epitope and a previously described neutralizing epitopes. Vaccinated monkey sera recognize the three epitopes differentially relative to unimmunized controls, and a correlation appears to exist between degree of cross-neutralization by infected monkey sera and degree of binding to these three regions.