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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

40273

8sal

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

40274

8san

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

40275

8saq

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

40277

8sar

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

40278

8sas

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

40279

8sat

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

40280

8sau

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

40281

8sav

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

40282

8saw

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

40283

8sax

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

40284

8say

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

40285

8saz

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

40286

8sb0

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

40287

8sb1

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

40288

8sb2

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

40289

8sb3

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

40290

8sb4

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

40291

8sb5

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 / N-Acetylglucosamine

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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