The purpose of this study was to characterize antigenic determinants on structural polypeptides of human immunodeficiency virus type 2 (HIV-2ben). Therefore, three HIV-2-specific monoclonal antibodies (mAbs) against the p24 core protein (gag) and one mAb against the gpl30 envelope glycoprotein (env)
Generation and characterization of murine monoclonal antibodies reactive against N-terminal and other regions of HIV-1 reverse transcriptase
β Scribed by Xuguang Li; Emily Amandoron; Mark A. Wainberg; Dr. Michael A. Parniak
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 948 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0146-6615
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β¦ Synopsis
We produced a series of monoclonal antibodies against the human immunodeficiency virus (HIV-1) reverse transcriptase by immunizing mice with either purified recombinant HIV-1 p66 protein or with recombinant vaccinia virus which expresses HIV-1 pol sequences. The antibodies generated were specific for the reverse transcriptase protein, and recognized only the p51 and p66 subunits of the enzyme in each of the HIV-1 viral lysates and lysates of HIV-1 infected cells. The antibodies did not cross-react with HIV-2 reverse transcriptase. Most important, several of the antibodies are unique, in that they are the first that can bind to sites close to the N-terminal. This latter region has been suggested to form part of the polymerase domain of the reverse transcriptase. None of the antibodies could neutralize either the RNA-dependent DNA polymerase or RNase H activities of either p66 or ~51166 proteins. The binding patterns of these various antibodies to p66 and ~51166 were dependent on each of three independent variables: the source of antigen amployed, the individual specificity of the antibody, and the method employed t o detect reactivity. These monoclonal antibodies provide useful reagents for the study of reverse transcriptase native structure-function relationships. o 1993 Witey-Liss, Inc.
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