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TitleStructural Survey of Broadly Neutralizing Antibodies Targeting the HIV-1 Env Trimer Delineates Epitope Categories and Characteristics of Recognition.
Journal, issue, pagesStructure, Vol. 27, Issue 1, Page 196-206.e6, Year 2019
Publish dateJan 2, 2019
AuthorsGwo-Yu Chuang / Jing Zhou / Priyamvada Acharya / Reda Rawi / Chen-Hsiang Shen / Zizhang Sheng / Baoshan Zhang / Tongqing Zhou / Robert T Bailer / Venkata P Dandey / Nicole A Doria-Rose / Mark K Louder / Krisha McKee / John R Mascola / Lawrence Shapiro / Peter D Kwong /
PubMed AbstractOver the past decade, structures have been determined for broadly neutralizing antibodies that recognize all major exposed surfaces of the prefusion-closed HIV-1-envelope (Env) trimer. To understand ...Over the past decade, structures have been determined for broadly neutralizing antibodies that recognize all major exposed surfaces of the prefusion-closed HIV-1-envelope (Env) trimer. To understand this recognition and its implications, we analyzed 206 antibody-HIV-1 Env structures from the Protein Data Bank with resolution suitable to define interaction chemistries and measured antibody neutralization on a 208-strain panel. Those with >25% breadth segregated into almost two dozen classes based on ontogeny and recognition and into six epitope categories based on recognized Env residues. For paratope, the number of protruding loops and level of somatic hypermutation were significantly higher for broad HIV-1 neutralizing antibodies than for a comparison set of non-HIV-1 antibodies (p < 0.0001). For epitope, the number of independent sequence segments was higher (p < 0.0001), as well as the glycan component surface area (p = 0.0005). The unusual characteristics of epitope and paratope delineated here are likely to reflect respectively virus-immune evasion and antibody-recognition solutions that allow effective neutralization of HIV-1.
External linksStructure / PubMed:30471922 / PubMed Central
MethodsEM (single particle)
Resolution8.8 Å
Structure data

8981

6e5p

EMDB-8981: Cryo-EM reconstruction of domain-swapped, glycan-reactive, neutralizing antibody 2G12 bound to HIV-1 Env BG505 DS-SOSIP, which was also bound to CD4-binding site antibody VRC03
PDB-6e5p: Backbone model based on cryo-EM map at 8.5 A of domain-swapped, glycan-reactive, neutralizing antibody 2G12 bound to HIV-1 Env BG505 DS-SOSIP, which was also bound to CD4-binding site antibody VRC03
Method: EM (single particle) / Resolution: 8.8 Å

Source
  • human immunodeficiency virus 1
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / HIV-1 Env / complex / neutralizing / domain-swapped antibody

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