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HIV-1 Matrix protein p17 (MA) is a structural component of the Human Immunodeficiency Virus type 1, derived from the N-terminal region of the Gag polyprotein precursor (UniProt: P03367). It plays a fundamental role in the viral life cycle by directing the Gag polyprotein to the host cell's plasma membrane through its N-terminal myristoyl group and a cluster of basic residues, a process essential for viral assembly and budding (PubMed: 25853488). Beyond its structural functions, p17 is released into the extracellular space where it acts as a viral cytokine, or virokine, by interacting with host receptors such as CXCR1 and CXCR2 (PubMed: 22438551). This interaction triggers signaling pathways that promote inflammation, angiogenesis, and the growth of B-cells, potentially contributing to HIV-associated malignancies like B-cell lymphoma (PubMed: 26433131). Because of its dual role in viral replication and host-cell modulation, p17 is a target for experimental therapeutic vaccines, such as AT20, and small-molecule inhibitors aimed at disrupting the viral life cycle and neutralizing its pathogenic extracellular effects (PubMed: 30104383).
Inhibition of Gag polyprotein membrane targeting and viral assembly; neutralization of extracellular p17-mediated signaling through CXCR1/CXCR2 receptors.
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