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Structure paper

TitleA generalized HIV vaccine design strategy for priming of broadly neutralizing antibody responses.
Journal, issue, pagesScience, Vol. 366, Issue 6470, Year 2019
Publish dateDec 6, 2019
AuthorsJon M Steichen / Ying-Cing Lin / Colin Havenar-Daughton / Simone Pecetta / Gabriel Ozorowski / Jordan R Willis / Laura Toy / Devin Sok / Alessia Liguori / Sven Kratochvil / Jonathan L Torres / Oleksandr Kalyuzhniy / Eleonora Melzi / Daniel W Kulp / Sebastian Raemisch / Xiaozhen Hu / Steffen M Bernard / Erik Georgeson / Nicole Phelps / Yumiko Adachi / Michael Kubitz / Elise Landais / Jeffrey Umotoy / Amanda Robinson / Bryan Briney / Ian A Wilson / Dennis R Burton / Andrew B Ward / Shane Crotty / Facundo D Batista / William R Schief /
PubMed AbstractVaccine induction of broadly neutralizing antibodies (bnAbs) to HIV remains a major challenge. Germline-targeting immunogens hold promise for initiating the induction of certain bnAb classes; yet for ...Vaccine induction of broadly neutralizing antibodies (bnAbs) to HIV remains a major challenge. Germline-targeting immunogens hold promise for initiating the induction of certain bnAb classes; yet for most bnAbs, a strong dependence on antibody heavy chain complementarity-determining region 3 (HCDR3) is a major barrier. Exploiting ultradeep human antibody sequencing data, we identified a diverse set of potential antibody precursors for a bnAb with dominant HCDR3 contacts. We then developed HIV envelope trimer-based immunogens that primed responses from rare bnAb-precursor B cells in a mouse model and bound a range of potential bnAb-precursor human naïve B cells in ex vivo screens. Our repertoire-guided germline-targeting approach provides a framework for priming the induction of many HIV bnAbs and could be applied to most HCDR3-dominant antibodies from other pathogens.
External linksScience / PubMed:31672916 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.296 - 4.42 Å
Structure data

7875

6dfg

EMDB-7875, PDB-6dfg:
BG505 MD39 SOSIP trimer in complex with mature BG18 fragment antigen binding
Method: EM (single particle) / Resolution: 4.42 Å

7876

6dfh

EMDB-7876, PDB-6dfh:
BG505 MD64 N332-GT2 SOSIP trimer in complex with germline-reverted BG18 fragment antigen binding
Method: EM (single particle) / Resolution: 3.85 Å

7884

6nf5

EMDB-7884: BG505 MD64 N332-GT5 SOSIP trimer in complex with BG18-like precursor HMP1 fragment antigen binding and base-binding RM20A3 fragment antigen binding
PDB-6nf5: BG505 MD64 N332-GT5 SOSIP trimer in complex with BG18-like precursor HMP1 fragmentantigen binding and base-binding RM20A3 fragment antigen binding
Method: EM (single particle) / Resolution: 3.71 Å

7885

6nfc

EMDB-7885: BG505 MD64 N332-GT5 SOSIP trimer in complex with BG18-like precursor HMP42 fragment antigen binding and base-binding RM20A3 fragment antigen binding
PDB-6nfc: BG505 MD64 N332-GT5 SOSIP trimer in complex with BG18-like precursor HMP42 fragmentantigen binding and base-binding RM20A3 fragment antigen binding
Method: EM (single particle) / Resolution: 3.43 Å

PDB-6oc7:
HMP42 Fab in complex with Protein G
Method: X-RAY DIFFRACTION / Resolution: 1.296 Å

Chemicals

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

ChemComp-HOH:
WATER

Source
  • human immunodeficiency virus 1
  • homo sapiens (human)
  • macaca mulatta (Rhesus monkey)
  • streptococcus sp. group g (bacteria)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / HIV-1 / HIV Envelope / SOSIP / germline targeting / antibody / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex / trimer / precursor antibody / IMMUNE SYSTEM / Anti-HIV antibody / Fab fragment / crystallization chaperone

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