Gag-Gag interactions in the C-terminal domain of human immunodeficiency virus type 1 p24 capsid antigen are essential for Gag particle assembly.

摘要: Seven internal deletions within the p24 domain of human immunodeficiency virus type 1 Gag precursor have been assessed for their effect on particle formation following expression using recombinant baculoviruses. In addition, each deleted molecule was its ability to bind soluble antigen in vitro. The mutants fell into three different phenotypic groups: (i) that had no either binding or assembly, (ii) abolished both features and (iii) one mutant bound vitro but failed assemble particles. Mutations assembly mapped C terminus confirming this region as critical virion assembly. We suggest division at least two distinct phases a model which sequences date are combined with available structural information.