Abstract
Background The somatically related antibodies, PG9 and PG16, neutralize 70-80% of HIV-1 isolates and bind a glycosylated epitope in the V1/V2 domain of HIV-1 gp120. Mutations in V1/V2, and sometimes V3 depending on the HIV-1 strain, affect neutralization and a glycan on Asn160 is required for neutralization. Both antibodies also preferentially bind the native trimer over monomeric gp120, especially PG16. The structure of PG9 in complex with its epitope, a scaffolded V1/V2 from HIV-1 strain ZM109, was recently solved and showed that PG9 targets a site of vulnerability comprising 2 glycans and a b-strand.
Highlights
The somatically related antibodies, PG9 and PG16, neutralize 70-80% of HIV-1 isolates and bind a glycosylated epitope in the V1/V2 domain of HIV-1 gp120
Mutations in V1/V2, and sometimes V3 depending on the HIV-1 strain, affect neutralization and a glycan on Asn160 is required for neutralization
A stable complex could be obtained between PG16 and a scaffolded V1/V2 domain from ZM109, and this complex was crystallized
Summary
The somatically related antibodies, PG9 and PG16, neutralize 70-80% of HIV-1 isolates and bind a glycosylated epitope in the V1/V2 domain of HIV-1 gp120. Mutations in V1/V2, and sometimes V3 depending on the HIV-1 strain, affect neutralization and a glycan on Asn160 is required for neutralization. Both antibodies preferentially bind the native trimer over monomeric gp120, especially PG16. The structure of PG9 in complex with its epitope, a scaffolded V1/V2 from HIV-1 strain ZM109, was recently solved and showed that PG9 targets a site of vulnerability comprising 2 glycans and a b-strand
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