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-Structure paper
Title | Structural evolution of glycan recognition by a family of potent HIV antibodies. |
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Journal, issue, pages | Cell, Vol. 159, Issue 1, Page 69-79, Year 2014 |
Publish date | Sep 25, 2014 |
![]() | Fernando Garces / Devin Sok / Leopold Kong / Ryan McBride / Helen J Kim / Karen F Saye-Francisco / Jean-Philippe Julien / Yuanzi Hua / Albert Cupo / John P Moore / James C Paulson / Andrew B Ward / Dennis R Burton / Ian A Wilson / ![]() |
PubMed Abstract | The HIV envelope glycoprotein (Env) is densely covered with self-glycans that should help shield it from recognition by the human immune system. Here, we examine how a particularly potent family of ...The HIV envelope glycoprotein (Env) is densely covered with self-glycans that should help shield it from recognition by the human immune system. Here, we examine how a particularly potent family of broadly neutralizing antibodies (Abs) has evolved common and distinct structural features to counter the glycan shield and interact with both glycan and protein components of HIV Env. The inferred germline antibody already harbors potential binding pockets for a glycan and a short protein segment. Affinity maturation then leads to divergent evolutionary branches that either focus on a single glycan and protein segment (e.g., Ab PGT124) or engage multiple glycans (e.g., Abs PGT121-123). Furthermore, other surrounding glycans are avoided by selecting an appropriate initial antibody shape that prevents steric hindrance. Such molecular recognition lessons are important for engineering proteins that can recognize or accommodate glycans. |
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Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.4969 - 17.8 Å |
Structure data | ![]() EMDB-2753: ![]() PDB-4r26: ![]() PDB-4r2g: |
Chemicals | ![]() ChemComp-GOL: ![]() ChemComp-HOH: ![]() ChemComp-NAG: ![]() ChemComp-CL: |
Source |
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![]() | IMMUNE SYSTEM / IGG Fold / Antibody / HIV-1 binding / Protein-Protein complex / IgG / Anti-HIV antibodies / gp120 |