Structural Biology of HIV-1 Entry

HIV-1 entry is mediated by its trimeric Envelope (Env) surface glycoprotein.  Binding of the gp120 subunit to host cell surface CD4 receptor triggers Env conformational changes that expose the binding site for a co-receptor, typically CCR5 or CXCR4. Additional conformational changes that follow co-receptor binding lead to membrane fusion. Env conformational changes on the HIV-1 entry pathway are mediated by an allosteric network of protein contacts that facilitate receptor-mediated structural changes at sites distal from the receptor binding site. Env is the sole target for neutralizing antibodies on the HIV-1 surface. Regions that are critical for entry, such as receptor binding sites and the fusion peptide, are vulnerable and are thus protected by multiple immune evasion mechanisms. The HIV-1 entry pathway can also be effectively targeted by entry inhibitors, exemplified by enfuvirtide and maraviroc, both licensed antiretroviral drugs that target different steps on the entry pathway.  Structural biology of HIV-1 entry has been a subject of intense investigations for many years, and is closely tied to efforts to develop an effective HIV-1 vaccine. In this Special Issue, we will gather and connect existing knowledge in the field on the structural biology of HIV-1 entry and reflect on how this informs HIV-1 vaccine and therapeutics development.

Dr. Priyamvada Acharya
Guest Editor

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