HIV-1 Gag polyprotein (p55) (Gag (p55))

HIV-1 p55gag is the primary structural polyprotein of the human immunodeficiency virus type 1, serving as the master regulator of viral assembly and release (UniProt: P04591). It is synthesized in the host cell cytoplasm and migrates to the plasma membrane, where it multimerizes to drive the budding of immature viral particles (NIH: HIV-1 Gag). Following budding, the viral protease cleaves p55gag into several functional subunits: matrix (MA/p17), capsid (CA/p24), nucleocapsid (NC/p7), and p6, as well as spacer peptides SP1 and SP2 (PubMed: 21115938). This maturation process is essential for the virus to become infectious. Therapeutic strategies targeting p55gag include maturation inhibitors, such as Bevirimat, which bind to the CA-SP1 cleavage site to prevent the final step of processing, resulting in the release of non-infectious, immature particles (PubMed: 19430491). This target represents a novel class of antiretroviral therapy distinct from traditional protease inhibitors.

Other names

Pr55GagGag polyproteinp55 GagGroup-specific antigen

Maturation inhibition by binding to the Gag polyprotein at the CA-SP1 junction, which sterically hinders the HIV-1 protease from cleaving the site, thereby blocking the transition from immature to infectious virions (PubMed: 19430491).