Outer Domain of HIV-1 gp120: Antigenic Optimization, Structural Malleability, and Crystal Structure with Antibody VRC-PG04

Joyce, M G , 87(4), 2294-306, J Virol, 2013

The authors describe design and antigenic optimization of an HIV-1 gp120 soluble outer domain as a minimal immunogen that can be recognized by broadly neutralizing antibodies that target the CD4 binding site. The outer domain variant OD4.2.2 was shown to bind known broadly neutralizing antibodies with nanomolar affinity. The Octet RED384 system was used with Anti-Human Fc Capture biosensors to measure binding kinetics of outer domain molecules to broadly neutralizing antibodies VRC01, VRC-PG04 and b12 and also to a group of poorly neutralizing antibodies.

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