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Simian immunodeficiency virus envelope glycoprotein 120 (SIV gp120) is the exterior subunit of the viral envelope protein complex, playing a pivotal role in the infection of non-human primates. It is responsible for the high-affinity binding to the host cell receptor CD4 and the subsequent interaction with chemokine coreceptors, primarily CCR5 (UniProt: P05884). This interaction is the first step in the viral entry process, which eventually leads to the fusion of the viral and host cell membranes mediated by the gp41 subunit (PubMed: 11160744). Because it is exposed on the surface of the virion, SIV gp120 is the primary target for neutralizing antibodies and is a central component in the design of SIV vaccines used in primate models of AIDS (PubMed: 25605925). The protein is characterized by extensive N-linked glycosylation, which forms a glycan shield to protect conserved epitopes from the immune system. Research into SIV gp120 is crucial for developing therapeutic strategies, including entry inhibitors and broadly neutralizing antibodies, that can be translated to HIV-1 treatment and prevention (PubMed: 27099211).
Neutralization of viral particles and inhibition of viral entry by blocking the interaction between the viral envelope and host cell receptors such as CD4 and CCR5.
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