Background: HIV-1 gains entry into host (CD4+) cells via interaction between the viral (Env) and host cell (CD4+) receptor complexes.

 

The viral receptor is a trimeric protein containing 3 identical heterodimers, each composed of the glycoproteins gp41 and gp120. gp41 is a transmembrane protein that embeds the viral complex in the viral membrane, while gp120, through noncovalent association with gp41, is presented on exterior of the viral particle and exposed to the host cell receptor protein CD4.

 

gp120 undergoes extensive N-glycosylation during secretion through the ER/Golgi pathway, with the result that almost 50% of the molecular weight of this protein is contributed by sugar.

 

Furthermore, there is extensive phylogenetic diversity among gp120 proteins present on different viral isolates, and these factors contribute to the well-documented difficulty of achieving broadly effective HIV-neutralisation immunologically.

 

Nevertheless, gp120 is highly immunogenic, and high titers of (type-specific) antigp120 antibodies are typically generated during the acute phase of HIV infection.

 

For this reason, this protein has attracted considerable research interest, both with respect to its diagnostic utility and potential use as a component of an anti-HIV vaccine.

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