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J Virol. 1990 February; 64(2): 962-965
Characterization of murine monoclonal antibodies to the tat protein from human immunodeficiency virus type 1.
D A Brake,
J Goudsmit,
W J Krone,
P Schammel,
N Appleby,
R H Meloen and
C Debouck
Department of Molecular Genetics, Smith Kline and French Laboratories, King of Prussia, Pennsylvania 19406-0939.
ABSTRACT
A panel of murine monoclonal antibodies (MAbs) to the human immunodeficiency virus type 1 trans-activator tat protein were characterized. The anti-tat MAbs were mapped to the different domains of the tat protein by Western blot (immunoblot) and Pepscan analyses. One-half of the MAbs tested mapped to the amino-terminal proline-rich region, and one-third of the MAbs tested mapped to the lysine-arginine-rich region of tat. The individual MAbs were tested for inhibition of tat-mediated trans activation, using a cell-based in vitro assay system. MAbs which mapped to the amino-terminal region of the tat protein demonstrated the highest degree of inhibition, whereas MAbs reactive to other portions of the molecule exhibited a less pronounced effect on tat function.
J Virol. 1990 February; 64(2): 962-965
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Copyright © 1990 by the American Society for Microbiology. All rights reserved.