Broadly Neutralizing Antibody PGT121 Allosterically Modulates CD4 Binding via Recognition of the HIV-1 gp120 V3 Base and Multiple Surrounding Glycans

@inproceedings{Julien2013BroadlyNA,
  title={Broadly Neutralizing Antibody PGT121 Allosterically Modulates CD4 Binding via Recognition of the HIV-1 gp120 V3 Base and Multiple Surrounding Glycans},
  author={Jean-Philippe Julien and Devin Sok and Reza Khayat and Jeong Hyun Lee and Katie J. Doores and Laura M Walker and Alejandra G. Ramos and Devan C. Diwanji and Robert Pejchal and Albert Cupo and Umesh Chandra Katpally and Rafael S. Depetris and Robyn L Stanfield and Ryan McBride and Andre J. Marozsan and James C Paulson and Rogier W. Sanders and John P. Moore and Dennis R. Burton and Pascal Poignard and Andrew B. Ward and Ian A. Wilson},
  booktitle={PLoS pathogens},
  year={2013}
}
New broad and potent neutralizing HIV-1 antibodies have recently been described that are largely dependent on the gp120 N332 glycan for Env recognition. Members of the PGT121 family of antibodies, isolated from an African donor, neutralize ∼70% of circulating isolates with a median IC50 less than 0.05 µg ml(-1). Here, we show that three family members, PGT121, PGT122 and PGT123, have very similar crystal structures. A long 24-residue HCDR3 divides the antibody binding site into two functional… CONTINUE READING
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