A non-cleavable hexahistidine affinity tag at the carboxyl-terminus of the HIV-1 Pr55^Gag polyprotein alters nucleic acid binding properties.

ABSTRACT: HIV Gag (Pr55^Gag), a multidomain polyprotein that orchestrates the assembly and release of the human immunodeficiency virus (HIV), is an active target of antiretroviral inhibitor development. However, highly pure, stable, recombinant Pr55^Gag has been difficult to produce in quantities sufficient for biophysical studies due to its susceptibility to proteolysis by cellular proteases during purification. Stability has been improved by using a construct that omits the p6 domain (Δp6). In vivo, p6 is crucial to the budding process and interacts with protein complexes in the ESCRT (Endosomal Sorting Complexes Required for Transport) pathway, it has been difficult to study its role in the context of Gag using in vitro approaches. Here we report the generation of a full lengt

SUBMITTER: Bewley MC 

PROVIDER: S-EPMC5536344 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature