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Structure paper

TitleStructural basis for breadth development in the HIV-1 V3-glycan targeting DH270 antibody clonal lineage.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 2782, Year 2023
Publish dateMay 15, 2023
AuthorsRory Henderson / Ye Zhou / Victoria Stalls / Kevin Wiehe / Kevin O Saunders / Kshitij Wagh / Kara Anasti / Maggie Barr / Robert Parks / S Munir Alam / Bette Korber / Barton F Haynes / Alberto Bartesaghi / Priyamvada Acharya /
PubMed AbstractAntibody affinity maturation enables adaptive immune responses to a wide range of pathogens. In some individuals broadly neutralizing antibodies develop to recognize rapidly mutating pathogens with ...Antibody affinity maturation enables adaptive immune responses to a wide range of pathogens. In some individuals broadly neutralizing antibodies develop to recognize rapidly mutating pathogens with extensive sequence diversity. Vaccine design for pathogens such as HIV-1 and influenza has therefore focused on recapitulating the natural affinity maturation process. Here, we determine structures of antibodies in complex with HIV-1 Envelope for all observed members and ancestral states of the broadly neutralizing HIV-1 V3-glycan targeting DH270 antibody clonal B cell lineage. These structures track the development of neutralization breadth from the unmutated common ancestor and define affinity maturation at high spatial resolution. By elucidating contacts mediated by key mutations at different stages of antibody development we identified sites on the epitope-paratope interface that are the focus of affinity optimization. Thus, our results identify bottlenecks on the path to natural affinity maturation and reveal solutions for these that will inform immunogen design aimed at eliciting a broadly neutralizing immune response by vaccination.
External linksNat Commun / PubMed:37188681 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 4.9 Å
Structure data

EMDB-40273, PDB-8sal:
CryoEM structure of VRC01-CH848.0358.80
Method: EM (single particle) / Resolution: 4.9 Å

EMDB-40274, PDB-8san:
CryoEM structure of VRC01-CH848.0836.10
Method: EM (single particle) / Resolution: 4.6 Å

EMDB-40275, PDB-8saq:
CryoEM structure of DH270.6-CH848.0526.25
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-40277, PDB-8sar:
CryoEM structure of DH270.6-CH848.10.17
Method: EM (single particle) / Resolution: 3.82 Å

EMDB-40278, PDB-8sas:
CryoEM structure of DH270.5-CH848.10.17
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-40279, PDB-8sat:
CryoEM structure of VRC01-CH848.10.17
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-40280, PDB-8sau:
CryoEM structure of DH270.4-CH848.10.17
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-40281, PDB-8sav:
CryoEM structure of VRC01-CH848.0526.25
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-40282, PDB-8saw:
CryoEM structure of DH270.UCA.G57R-CH848.10.17DT
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-40283, PDB-8sax:
CryoEM structure of DH270.UCA-CH848.10.17DT
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-40284, PDB-8say:
CryoEM structure of DH270.3-CH848.10.17
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-40285, PDB-8saz:
CryoEM structure of DH270.I5.6-CH848.10.17
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-40286, PDB-8sb0:
CryoEM structure of DH270.I4.6-CH848.10.17
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-40287, PDB-8sb1:
CryoEM structure of DH270.I3-CH848.10.17
Method: EM (single particle) / Resolution: 4.3 Å

EMDB-40288, PDB-8sb2:
CryoEM structure of DH270.I2-CH848.10.17
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-40289, PDB-8sb3:
CryoEM structure of DH270.2-CH848.10.17
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-40290, PDB-8sb4:
CryoEM structure of DH270.1-CH848.10.17
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-40291, PDB-8sb5:
CryoEM structure of DH270.I1.6-CH848.10.17
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
  • hiv-1 06tg.ht008 (virus)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / HIV-1 / antibody / VRC01 / CH848.0358.80 / VIRAL PROTEIN-IMMUNE SYSTEM complex / CH848.0836.10 / DH270.6 / CH848.0526.25 / CH848.10.17 / DH270.5 / DH270.4 / DH270.UCA.G57R CH848.10.17DT / DH270.UCA / DH270.3 / DH270.I5.6 / DH270.I3 / DH270.I2 / DH270.2 / DH270.1 / DH270.I1.6

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