Human immunodeficiency virus type 1 matrix protein p17 (p17)

The Human immunodeficiency virus type 1 (HIV-1) matrix protein p17 is a multifunctional structural protein essential for the viral life cycle. It is generated by the proteolytic cleavage of the Gag polyprotein and forms a shell on the inner surface of the viral envelope, where it mediates the targeting of Gag to the plasma membrane during assembly (UniProt P03367). Additionally, p17 is involved in the nuclear import of the viral pre-integration complex in non-dividing cells. Interestingly, p17 is also released into the extracellular space, where it functions as a viral cytokine by binding to host receptors like CXCR1 and CXCR2, thereby promoting inflammation and B-cell proliferation (PubMed: 22438551). This extracellular activity is implicated in HIV-associated comorbidities, such as lymphoma. Therapeutic strategies targeting p17 include the development of neutralizing antibodies and vaccines designed to block its pathogenic signaling and inhibit viral replication (PubMed: 25847251).

Other names

Matrix proteinMAGag p17p17 proteinHIV-1 MA protein

Neutralization of extracellular p17-mediated signaling and inhibition of viral assembly and budding.