Human immunodeficiency virus type 1 matrix protein (p17) (p17)

The Human immunodeficiency virus type 1 matrix protein (p17) is a 132 amino acid structural protein produced by proteolytic cleavage from the N-terminal of the Gag polyprotein during HIV-1 maturation[1][3][4]. p17 lines the inner surface of the viral envelope and plays critical roles in the HIV-1 life cycle, including targeting the Gag polyprotein to the host plasma membrane for assembly, orchestrating correct viral particle formation, and facilitating nuclear export of the viral preintegration complex[1][3][5]. p17 interacts with host membrane lipids via its myristoylated N-terminus, promotes trimerization, and coordinates the incorporation of viral envelope glycoproteins into budding virions[1][3]. In addition to its essential structural and regulatory functions, extracellular and variant forms of p17 have been linked to pathologies such as lymphoma (via promoting B-cell proliferation) and neurodegeneration (via protein aggregation in brain tissues), making it both a key factor in HIV-1 replication and a contributor to HIV-associated comorbidities[2][3][6].

Other names

HIV-1 matrix protein p17Gag p17HIV-1 MAMA (matrix protein)Matrix protein p17

Maturation inhibitors prevent processing of the Gag polyprotein, thus inhibiting production of mature p17 and other Gag-derived proteins, impairing viral maturation and infectivity[4]. No direct p17-binding drugs are currently approved.