Abstract
Background Antibodies PGT141-145 are broadly neutralizing and recognize a glycan-dependent epitope in the V1/V2 loop, similar to antibodies PG9 and PG16. Collectively, this class of antibodies binds preferentially to the functional viral spike. Although PG9, and to a lesser extent, PG16, bind monomeric gp120s and V1/V2 scaffolds, to date no recombinant env-derived proteins have been identified that bind to antibodies PGT141-145.
Highlights
Antibodies PGT141-145 are broadly neutralizing and recognize a glycan-dependent epitope in the V1/V2 loop, similar to antibodies PG9 and PG16
PG9, and to a lesser extent, PG16, bind monomeric gp120s and V1/V2 scaffolds, to date no recombinant env-derived proteins have been identified that bind to antibodies PGT141-145
As a first step toward obtaining structural information of the epitope recognized by PGT141-145, we have created and characterized novel gp140s and epitope scaffolds designed to present the V1/V2 conformation recognized by PGT141-145
Summary
Antibodies PGT141-145 are broadly neutralizing and recognize a glycan-dependent epitope in the V1/V2 loop, similar to antibodies PG9 and PG16. Recombinant Env proteins that bind the quaternary-specific, V1/V2-directed PGT antibodies J Gorman1*, J McLellan1, Y Yang1, T Zhou1, J Zhu1, S Bangaru2, N Bayless2, P Alff2, CP Marshall2, PD Kwong1 From AIDS Vaccine 2012 Boston, MA, USA.
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