Monoclonal antibodies to the MLV protease active site that crossreact with the HIV protease.

Important note: Information in this article was accurate in 1994. The state of the art may have changed since the publication date.

Monoclonal antibodies to the MLV protease active site that crossreact with the HIV protease.

Abstr Gen Meet Am Soc Microbiol. 1994;94:485 (abstract no. T-16). Unique Identifier : AIDSLINE ASM94/94313097
Luftig RB; Calkins P; Yeh HY; Louisiana State University Medical Center, New Orleans.

Abstract: The retroviral proteases are essential for cleavage of gag and gag-pol polyproteins during the virus assembly. Inhibitors that inactivate the protease activity will reduce production of mature particles and, thus, spread of diseases. In this study, we generated mouse monoclonal antibodies specific to protease active site. A thyroglobulin-conjugated 20-mer peptide of the murine leukemia virus (MLV) protease active site (Q-P-V-T-F-L-V-D-T-G-A-Q-H-S-V-L-T-Q-N-P) was used to immunize BALB/c mice. About 40 hybridomas were generated by fusion of spleen cells with a mouse myeloma cell line. A peptide ELISA assay confirmed that the mAbs reacted to the original 20-mer peptide. Further, using immunoblot analysis, we found 13 hybridomas where the mAbs reacted with MLV protease expressed in E. coli, as well with HIV protease. Currently, we are mapping the common epitope using short peptides (6- to 8-mer). The significance of these results may provide another avenue for developing inhibitors that bind specifically to the catalytic site.

Keywords: Amino Acid Sequence Animal *Antibodies, Monoclonal Binding Sites Cloning, Molecular Cross Reactions Enzyme-Linked Immunosorbent Assay/METHODS Epitopes/*ANALYSIS Escherichia coli Hybridomas/ENZYMOLOGY HIV Protease/*IMMUNOLOGY/METABOLISM Leukemia Viruses, Murine/*ENZYMOLOGY Mice Mice, Inbred BALB C/IMMUNOLOGY Molecular Sequence Data Peptide Peptidohydrolases/*IMMUNOLOGY/METABOLISM Recombinant Proteins/IMMUNOLOGY ABSTRACT
941030
M94A0857

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