Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation.

@article{Ringe2013CleavageSI,
  title={Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation.},
  author={Rajesh P. Ringe and Rogier W. Sanders and Anila Yasmeen and Helen J Kim and Jeong Hyun Lee and Albert Cupo and Jacob Korzun and Ronald Derking and Thijs van Montfort and Jean-Philippe Julien and Ian A. Wilson and Per Johan Klasse and Andrew B. Ward and John P. Moore},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 45},
  pages={18256-61}
}
We compare the antigenicity and conformation of soluble, cleaved vs. uncleaved envelope glycoprotein (Env gp)140 trimers from the subtype A HIV type 1 (HIV-1) strain BG505. The impact of gp120-gp41 cleavage on trimer structure, in the presence or absence of trimer-stabilizing modifications (i.e., a gp120-gp41 disulfide bond and an I559P gp41 change, together designated SOSIP), was assessed. Without SOSIP changes, cleaved trimers disintegrate into their gp120 and gp41-ectodomain (gp41ECTO… CONTINUE READING
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Crystal structure of a soluble cleaved HIV-1 envelope trimer in complex with a glycan-dependent broadly neutralizing antibody

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