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TitleBroad and Potent Neutralizing Antibodies Recognize the Silent Face of the HIV Envelope.
Journal, issue, pagesImmunity, Vol. 50, Issue 6, Page 1513-11529.e9, Year 2019
Publish dateJun 18, 2019
AuthorsTill Schoofs / Christopher O Barnes / Nina Suh-Toma / Jovana Golijanin / Philipp Schommers / Henning Gruell / Anthony P West / Franziska Bach / Yu Erica Lee / Lilian Nogueira / Ivelin S Georgiev / Robert T Bailer / Julie Czartoski / John R Mascola / Michael S Seaman / M Juliana McElrath / Nicole A Doria-Rose / Florian Klein / Michel C Nussenzweig / Pamela J Bjorkman /
PubMed AbstractBroadly neutralizing antibodies (bNAbs) against HIV-1 envelope (Env) inform vaccine design and are potential therapeutic agents. We identified SF12 and related bNAbs with up to 62% neutralization ...Broadly neutralizing antibodies (bNAbs) against HIV-1 envelope (Env) inform vaccine design and are potential therapeutic agents. We identified SF12 and related bNAbs with up to 62% neutralization breadth from an HIV-infected donor. SF12 recognized a glycan-dominated epitope on Env's silent face and was potent against clade AE viruses, which are poorly covered by V3-glycan bNAbs. A 3.3Å cryo-EM structure of a SF12-Env trimer complex showed additional contacts to Env protein residues by SF12 compared with VRC-PG05, the only other known donor-derived silentface antibody, explaining SF12's increased neutralization breadth, potency, and resistance to Env mutation routes. Asymmetric binding of SF12 was associated with distinct N-glycan conformations across Env protomers, demonstrating intra-Env glycan heterogeneity. Administrating SF12 to HIV-1-infected humanized mice suppressed viremia and selected for viruses lacking the N448 glycan. Effective bNAbs can therefore be raised against HIV-1 Env's silent face, suggesting their potential for HIV-1 prevention, therapy, and vaccine development.
External linksImmunity / PubMed:31126879 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.2 - 4.36 Å
Structure data

20100

6okp

EMDB-20100, PDB-6okp:
B41 SOSIP.664 in complex with the silent-face antibody SF12 and V3-targeting antibody 10-1074
Method: EM (single particle) / Resolution: 3.28 Å

EMDB-20101:
B41 SOSIP.664 trimer in complex with two Fab fragments of the silent-face targeting bNAb SF12, and one Fab fragment of the V3-targeting bNAb 10-1074
Method: EM (single particle) / Resolution: 4.36 Å

PDB-6okq:
Crystal structure of the SF12 Fab
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • human immunodeficiency virus 1
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / HIV-1 broadly-neutralizing antibody / Env trimer structure / silent face / VIRAL PROTEIN-IMMUNE SYSTEM complex / IMMUNE SYSTEM / Fab structure / Envelope

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