A POSSIBLE REGULATION OF NEGATIVE FACTOR (NEF) ACTIVITY OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 BY THE VIRAL PROTEASE

Negative factor (Nef) protein from human immunodeficiency virus type 1 (HIV-1) is cleaved into two well-defined domains by the HIV-1-encoded protease. The cleavage site is located between Trp57 and Leu58 and is well conserved. The two domains are stable in the presence of proteas e for more than 48 h. The C-terminal core domain contains a well-conse rved well-folded region. The cleavage releases the core domain from th e myristoylated membrane anchor domain. As is the case for other HIV p roteins, cleavage of Nef could be crucial for correct biological funct ion.