PMID: 9546801Apr 18, 1998Paper

Immunologic cross-reaction between HIV type 1 p17 and Mycoplasma hyorhinis variable lipoprotein

AIDS Research and Human Retroviruses
S H PincusK S Wise

Abstract

Monoclonal antibodies directed against the HIV-1 matrix protein p17 that react with a component present on the surface of HIV-1-infected cells have previously been described. In this study we show that one of these monoclonal antibodies binds to persistently HIV-1-infected cell lines that are coinfected with Mycoplasma hyorhinis, but not to cell lines that are uninfected with mycoplasma. Mycoplasma-infected cells secrete HIV-1 at a higher rate, have a slight increase in cell surface expression of gp120 and gp41, and are less sensitive to immunotoxins than uninfected cells. The anti-p17 antibody binds to a protein of M. hyorhinis grown in cell-free culture. The variable expression and size of the protein among strains is typical of the variable lipoprotein (Vlp) system of M. hyorhinis. Confirmation of the reactivity of the antibody with a Vlp was provided by demonstrating its specific binding to recombinant VlpF expressed in E. coli, and to a synthetic peptide representing the carboxy-terminal region of VlpF, but not to other recombinant Vlp products or peptides. This is a true cross-reaction because the antibody also binds to recombinant p17 expressed in E. coli and the binding is inhibited by the VlpF peptide. These analyses h...Continue Reading

References

Sep 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·K S WiseR T Action
Mar 1, 1990·AIDS Research and Human Retroviruses·M B VasudevachariN P Salzman
Sep 1, 1995·The Journal of Infectious Diseases·O GrauJ P Clauvel
Jan 1, 1995·Advances in Pharmacology·S H Pincus, V V Tolstikov
Jan 1, 1994·Annual Review of Microbiology·A Blanchard, L Montagnier
May 1, 1993·Trends in Microbiology·K S Wise
Jan 1, 1993·Proceedings of the National Academy of Sciences of the United States of America·S H Pincus, J McClure

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