Characterization Of Murine Monoclonal-Antibodies Directed Against The Submembrane Protein-P17 Of Hiv-1

Monaclonal antibodies (MAbs) were raised against the gag protein of human immunodeficiency virus type 1 (HIV-1). The reactivity of the selected Mabs with the matrix protein p17 of HIV-1 were investigated in several tests, i.e. ELISA, immunostaining of Western blots, and alkaline phosphatase anti-alkaline phosphatase immunocytochemistry (APAAP). All three Mabs reacted exclusively with HIV-1 and showed specific binding to the virus surf ace in pre-embedding immuno-electron-microscopy and useful as diagnostic agents. In an ''in vitro'' cultivation experiment the MAbs showed antiviral activity in concentrations in the range of 25-100 mug/ml. No binding region could be defined using overlapping peptides consisting of the p17 protein sequence of HIV-1 in an epitope mapping system and therefore we concluded, that the MAbs recognize a conformational epitope.