Abstract
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.
Highlights
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
Two glycosylation sites (N156 and N160) have been shown by mutagenesis studies to be important in forming the PG9 and PG16 epitopes
Summary
The HIV-1 envelope spike, which consists of a compact, heterodimeric trimer of the glycoprotein gp120 and gp, 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. 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. Characterization indicates that glycans predominantly influence the entropy of the V1/V2 loops
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