Envelope glycoprotein gp160 (HIV-1 isolate MN) (gp160)

HIV-1 MN gp160 is the envelope glycoprotein precursor of the MN strain of Human Immunodeficiency Virus type 1, a clade B isolate frequently used in early vaccine research [1]. This polyprotein is synthesized in the host cell and subsequently cleaved by furin-like proteases into the surface subunit gp120 and the transmembrane subunit gp41 [2]. These subunits remain non-covalently linked, forming heterotrimeric spikes on the viral envelope that are essential for viral infectivity. The gp120 subunit mediates the initial high-affinity binding to the host CD4 receptor and subsequent interaction with chemokine coreceptors, such as CCR5 or CXCR4 [3]. Following coreceptor binding, gp41 undergoes a dramatic conformational change that facilitates the fusion of the viral and cellular membranes, allowing the viral capsid to enter the cytoplasm [3]. As the sole viral protein exposed on the virion surface, gp160 is the primary target for neutralizing antibodies and various classes of entry inhibitors [4]. Therapeutic agents targeting this molecule include attachment inhibitors like Fostemsavir, which binds gp120 to prevent CD4 interaction, and fusion inhibitors like Enfuvirtide, which targets gp41 [5]. The MN strain specifically served as a key component in the development of early recombinant gp120 vaccines, such as AIDSVAX B/B, highlighting its historical importance in HIV immunology [1]. [1] UniProt: P12449; [2] PubMed: 10644346; [3] NIH: HIV Life Cycle; [4] PubMed: 28455231; [5] DrugBank: DB15357, DB00102.

Other names

EnvEnvelope polyproteingp160 precursorgp120/gp41 complexHIV-1 MN Env

Inhibition of viral attachment to CD4 receptors, prevention of coreceptor binding, and blockade of the conformational changes required for viral-host membrane fusion [3, 5].