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Structure paper

TitleA naturally arising broad and potent CD4-binding site antibody with low somatic mutation.
Journal, issue, pagesSci Adv, Vol. 8, Issue 32, Page eabp8155, Year 2022
Publish dateAug 12, 2022
AuthorsChristopher O Barnes / Till Schoofs / Priyanthi N P Gnanapragasam / Jovana Golijanin / Kathryn E Huey-Tubman / Henning Gruell / Philipp Schommers / Nina Suh-Toma / Yu Erica Lee / Julio C Cetrulo Lorenzi / Alicja Piechocka-Trocha / Johannes F Scheid / Anthony P West / Bruce D Walker / Michael S Seaman / Florian Klein / Michel C Nussenzweig / Pamela J Bjorkman /
PubMed AbstractThe induction of broadly neutralizing antibodies (bNAbs) is a potential strategy for a vaccine against HIV-1. However, most bNAbs exhibit features such as unusually high somatic hypermutation, ...The induction of broadly neutralizing antibodies (bNAbs) is a potential strategy for a vaccine against HIV-1. However, most bNAbs exhibit features such as unusually high somatic hypermutation, including insertions and deletions, which make their induction challenging. VRC01-class bNAbs not only exhibit extraordinary breadth and potency but also rank among the most highly somatically mutated bNAbs. Here, we describe a VRC01-class antibody isolated from a viremic controller, BG24, that is much less mutated than most relatives of its class while achieving comparable breadth and potency. A 3.8-Å x-ray crystal structure of a BG24-BG505 Env trimer complex revealed conserved contacts at the gp120 interface characteristic of the VRC01-class Abs, despite lacking common CDR3 sequence motifs. The existence of moderately mutated CD4-binding site (CD4bs) bNAbs such as BG24 provides a simpler blueprint for CD4bs antibody induction by a vaccine, raising the prospect that such an induction might be feasible with a germline-targeting approach.
External linksSci Adv / PubMed:35960796 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.25 - 4 Å
Structure data

26443

7ucg

EMDB-26443, PDB-7ucg:
Structure of the DU422 SOSIP.664 trimer in complex with neutralizing antibody Fab fragments 10-1074 and BG24
Method: EM (single particle) / Resolution: 3.5 Å

PDB-7uce:
Structure of the anti-HIV-1 neutralizing antibody BG24 Fab fragment
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-7ucf:
Structure of the BG505 SOSIP.664 trimer in complex with neutralizing antibody Fab fragments 10-1074 and BG24
Method: X-RAY DIFFRACTION / Resolution: 4.0 Å

Chemicals

ChemComp-HOH:
WATER / Water

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

ChemComp-FUC:
alpha-L-fucopyranose / Fucose

Source
  • homo sapiens (human)
  • human immunodeficiency virus 1
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / broadly neutralizing antibody / bNAb / HIV-1 / CD4 binding site / VH1-2 / VRC01-class / antiviral protein / VIRAL PROTEIN-IMMUNE SYSTEM complex

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