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HIV-1 gp160 is a viral envelope glycoprotein precursor synthesized by the human immunodeficiency virus type 1 (HIV-1). This polyprotein is crucial for the virus's ability to infect host cells. It undergoes cleavage by host cellular proteases, primarily furin, into two non-covalently associated subunits: gp120 (surface glycoprotein) and gp41 (transmembrane glycoprotein). The gp120 subunit is responsible for binding to the primary receptor CD4 and co-receptors (CCR5 or CXCR4) on the surface of host T lymphocytes and macrophages, initiating viral entry. The gp41 subunit then mediates the fusion of the viral and host cell membranes, allowing the viral genome to enter the cell. Due to its essential role in viral entry and its exposure on the viral surface, HIV-1 gp160, or its cleaved components, has been extensively studied as a key immunogen for the development of HIV vaccines aimed at eliciting neutralizing antibodies and cellular immune responses to prevent or treat HIV infection.
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