Generation, characterization and cross-reactivities of monoclonal antibodies against the p24 core protein and the gp130 envelope glycoprotein of HIV-2ben

✍ Scribed by Arne-C. Faißt; Ahlert Otteken; Sigrid Nick; Gerhard Hunsmann

• Publisher: Springer-Verlag
• Year: 1993
• Tongue: English
• Weight: 551 KB
• Volume: 182
• Category: Article
• ISSN: 0300-8584
• DOI: 10.1007/bf00190264

✦ Synopsis

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) were produced. In addition to p24 the anti-core mAbs recognized the primary translation product of the viral gag gene p55 and an intermediate cleavage product p41. Core mAbs cross-reacted with another HIV-2 isolate (HIV-2rod), and several simian immunodeficiency viruses (SIVagmTYO7 and SIVmac) , but not with SIVmn d and the HIV-1 isolates investigated (HIV-lhan and HIV-11ai). The env mAb crossreacted with HIV-2rod and SIVma c but not with SIWagm, SIVmn d or HIV-1. In competition assays and with epitope mapping possible binding sites for the mAbs were identified. The processing of HIV-2 core proteins is compared in retrovirusinfected T cell lines and during the expression by recombinant vaccinia virus. Finally, the mAb XIV DC10 which recognized a highly conserved epitope could be useful for an assay to detect HIV-1 and HIV-2 simultaneously. II D8 is the first mAb raised against HIV-2 env glycoprotein.