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Immunologic cross-reaction between HIV type 1 p17 and Mycoplasma hyorhinis variable lipoprotein
S H Pincus1, R L Cole, R Watson-McKown
1Laboratory of Microbial Structure and Function, NIAID Rocky Mountain Laboratories, Hamilton, Montana 59840, USA.
AIDS Research and Human Retroviruses
|April 18, 1998
Summary
Monoclonal antibodies targeting HIV-1 p17 protein may cross-react with Mycoplasma hyorhinis. Mycoplasma contamination in cell cultures can lead to increased HIV-1 secretion and inaccurate experimental results.
Area of Science:
- Immunology
- Virology
- Microbiology
- Cell Biology
Background:
- Monoclonal antibodies against HIV-1 matrix protein p17 have been developed.
- These antibodies were previously thought to target a surface component of HIV-1-infected cells.
Purpose of the Study:
- To investigate the binding specificity of an anti-p17 monoclonal antibody.
- To determine the impact of Mycoplasma hyorhinis coinfection on HIV-1-infected cell lines.
Main Methods:
- Testing monoclonal antibody binding to HIV-1-infected cell lines with and without Mycoplasma hyorhinis coinfection.
- Analyzing the antibody's reactivity with Mycoplasma hyorhinis proteins in cell-free culture.
- Confirming antibody binding using recombinant Mycoplasma variable lipoprotein (Vlp) and synthetic peptides, including VlpF.
Main Results:
- The anti-p17 antibody bound to Mycoplasma-coinfected cells but not to uninfected cells.
- The antibody recognized a protein from Mycoplasma hyorhinis, identified as a variable lipoprotein (Vlp), specifically VlpF.
- A cross-reaction was confirmed as the antibody bound both recombinant p17 and VlpF, with VlpF inhibiting p17 binding.
Conclusions:
- Mycoplasma contamination in cell cultures can lead to anomalous experimental findings.
- Mycoplasma infection increases HIV-1 secretion rates and can cause immunologic cross-reactions with anti-HIV-1 antibodies.
- The presence of a cell surface form of HIV-1 p17 is unlikely.