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Background The HIV-1 envelope spike, which consists of a compact, heterodimeric trimer of the glycoprotein gp120 and gp41, is the sole viral target of neutralizing antibodies. The gp120 component of the viral spike is known to be heavily glycosylated, and glycosylation can affect the conformation of envelope spikes. V1/V2 variable loops of gp120 are key target regions for a number of broadly neutralizing human antibodies, such as PG9 and PG16, CH01-CH04, and PGT141-145. Two glycosylation sites (N156 and N160) have been shown by mutagenesis studies to be important in forming the PG9 and PG16 epitopes. Recently, Peter Kwong and coworkers have resolved crystal structure of V1/V2 domain of HIV-1 gp120 from strains CAP45 and ZM109 complexes with antigen-binding fragment of PG9.

Conformational study of quaternary epitope region of V1/V2 loop: influence of disulfide bonds and glycosylations