Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120

@article{Kong2013SupersiteOI,
  title={Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120},
  author={L. Kong and J. H. Lee and K. Doores and C. D. Murin and J. Julien and R. McBride and Y. Liu and A. Marozsan and A. Cupo and P. Klasse and S. Hoffenberg and M. Caulfield and C. King and Y. Hua and Khoa Le and R. Khayat and M. Deller and T. Clayton and H. Tien and T. Feizi and R. Sanders and J. Paulson and John P. Moore and R. Stanfield and D. Burton and A. Ward and I. Wilson},
  journal={Nature structural \& molecular biology},
  year={2013},
  volume={20},
  pages={796 - 803}
}
A substantial proportion of the broadly neutralizing antibodies (bnAbs) identified in certain HIV-infected donors recognize glycan-dependent epitopes on HIV-1 gp120. Here we elucidate how the bnAb PGT 135 binds its Asn332 glycan–dependent epitope from its 3.1-Å crystal structure with gp120, CD4 and Fab 17b. PGT 135 interacts with glycans at Asn332, Asn392 and Asn386, using long CDR loops H1 and H3 to penetrate the glycan shield and access the gp120 protein surface. EM reveals that PGT 135 can… Expand
The HIV glycan shield as a target for broadly neutralizing antibodies
  • K. Doores
  • Biology, Medicine
  • The FEBS journal
  • 2015
Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike.
Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers.
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