Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9.

@article{Julien2013AsymmetricRO,
  title={Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9.},
  author={Jean-Philippe Julien and Jeong Hyun Lee and Albert Cupo and Charles D. Murin and Ronald Derking and Simon Hoffenberg and Michael J Caulfield and Charles R. King and Andre J. Marozsan and Per Johan Klasse and Rogier W. Sanders and John P. Moore and Ian A. Wilson and Andrew B. Ward},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 11},
  pages={4351-6}
}
PG9 is the founder member of an expanding family of glycan-dependent human antibodies that preferentially bind the HIV (HIV-1) envelope (Env) glycoprotein (gp) trimer and broadly neutralize the virus. Here, we show that a soluble SOSIP.664 gp140 trimer constructed from the Clade A BG505 sequence binds PG9 with high affinity (∼11 nM), enabling structural and biophysical characterizations of the PG9:Env trimer complex. The BG505 SOSIP.664 gp140 trimer is remarkably stable as assessed by electron… CONTINUE READING
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