Suppression of Human Immunodeficiency Virus Type-1 Production by Coexpression of Catalytic-Region-Deleted N-Myristoyltransferase Mutants

N-Myristoyltransferase (NMT) isozymes, i e, NMT1 and NMT2, are essential host factors for the AIDS-causing human immunodeficiency virus type-1 (HIV-1), by which the viral proteins Pr55(gag) and Nef are N-myristovlated N-Myristoylation is important for the membrane targeting of modified proteins Since it is predicted that approximately 0 5% of all proteins in the human genome are N-myristoylated, selective inhibition of closely HIV-1-associated NMT isozymes is thought to be important for the improvement of specificity in the anti-HIV-1 strategy with the inhibition of NMT function NMT isozymes contain two characteristic structures, the N-terminal region and the catalytic region Here, it was shown that the N-terminal region of each NMT isozyme is required for isozyme-specific binding to the ribosome The specific binding of each isozyme to the ribosome was associated with HIV-1 production, in which NMT1 and NMT2 in the ribosome were suggested to be mainly related to Pr55(gag) and Nef, respectively These results indicate that the N-terminal region that mediates binding to the ribosome can become a target for NMT-isozyme-specific inhibition, which could block HIV-1 production