Structure-Guided Alterations of the gp41-directed HIV-1 Broadly Neutralizing Antibody 2F5 Reveal New Properties Regarding its Neutralizing Function

J. Guenaga, R.T. Wyatt, 8(7), e1002806, PLoS Pathogens, 2012

Mutagenesis and functional analysis of the broadly neutralizing HIV-1 antibody 2F5 was performed. Data were presented describing a new property of the antibody, an ability to first bind downstream of its known core epitope in a two-step process not directly involving the lipid membrane. The Octet RED system was utilized to determine binding affinities to MPER peptides to test variations in length of core binding region and to determine whether 2F5 antibody might interact with residues downstream of its core epitope. For these binding studies, 2F5 wild-type and variant antibodies were immobilized using Anti-Human IgG Fc Capture (AHC) biosensors.

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