The role of zinc in retroviral gag protein function has been studied using high-resolution nuclear magnetic resonance spectroscopy. The nucleocapsid protein (NCP, p7) isolated directly from infectious HIV-1 particles was examined.
It was found that the HIV-1 NCP binds two equivalents of zinc tightly and stoichiometrically. Two-dimensional NMR spectroscopic studies revealed that zinc binding induces the formation of folded domains that are similar to structures observed for relevant retroviral-type (RT) zinc finger peptides WVKCFNCGKEGHIARNCRA.
This finding supports the hypothesis that the inability of mutant proteins (with substituted Cys and His residues) to package viral RNA results from deficient zinc-binding capability. This may have significant consequences in the development of vaccines for the prevention of AIDS.
| 