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The human immunodeficiency virus (HIV) envelope glycoprotein, commonly referred to as Env, is a complex protein structure found on the surface of HIV-1 and HIV-2 virions. It plays a central role in viral entry into host cells and is the primary target for neutralizing antibodies and vaccine design efforts. The Env glycoprotein is synthesized as a precursor protein called gp160, which undergoes proteolytic cleavage to yield two non-covalently associated subunits: gp120 (the external subunit responsible for binding to host cell receptors) and gp41 (the transmembrane subunit that mediates fusion between the viral envelope and the host cell membrane). On mature virions, three gp120-gp41 heterodimers assemble into a trimeric spike complex embedded in the viral membrane. Env is essential for determining HIV tropism, mediating initial attachment and subsequent entry steps, and serving as an immunodominant antigen.
Block receptor/coreceptor interactions or prevent necessary conformational changes required for fusion
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