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TitleBroad cross-reactivity across sarbecoviruses exhibited by a subset of COVID-19 donor-derived neutralizing antibodies.
Journal, issue, pagesCell Rep, Vol. 36, Issue 13, Page 109760, Year 2021
Publish dateSep 28, 2021
AuthorsClaudia A Jette / Alexander A Cohen / Priyanthi N P Gnanapragasam / Frauke Muecksch / Yu E Lee / Kathryn E Huey-Tubman / Fabian Schmidt / Theodora Hatziioannou / Paul D Bieniasz / Michel C Nussenzweig / Anthony P West / Jennifer R Keeffe / Pamela J Bjorkman / Christopher O Barnes /
PubMed AbstractMany anti-severe acute respiratory syndrome coronavirus 2 (anti-SARS-CoV-2) neutralizing antibodies target the angiotensin-converting enzyme 2 (ACE2) binding site on viral spike receptor-binding ...Many anti-severe acute respiratory syndrome coronavirus 2 (anti-SARS-CoV-2) neutralizing antibodies target the angiotensin-converting enzyme 2 (ACE2) binding site on viral spike receptor-binding domains (RBDs). Potent antibodies recognize exposed variable epitopes, often rendering them ineffective against other sarbecoviruses and SARS-CoV-2 variants. Class 4 anti-RBD antibodies against a less-exposed, but more-conserved, cryptic epitope could recognize newly emergent zoonotic sarbecoviruses and variants, but they usually show only weak neutralization potencies. Here, we characterize two class 4 anti-RBD antibodies derived from coronavirus disease 2019 (COVID-19) donors that exhibit breadth and potent neutralization of zoonotic coronaviruses and SARS-CoV-2 variants. C118-RBD and C022-RBD structures reveal orientations that extend from the cryptic epitope to occlude ACE2 binding and CDRH3-RBD main-chain H-bond interactions that extend an RBD β sheet, thus reducing sensitivity to RBD side-chain changes. A C118-spike trimer structure reveals rotated RBDs that allow access to the cryptic epitope and the potential for intra-spike crosslinking to increase avidity. These studies facilitate vaccine design and illustrate potential advantages of class 4 RBD-binding antibody therapeutics.
External linksCell Rep / PubMed:34534459 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.7 - 4.53 Å
Structure data

24504

7rkv

EMDB-24504, PDB-7rkv:
Structure of the SARS-CoV-2 S 6P trimer in complex with neutralizing antibody C118 (State 1)
Method: EM (single particle) / Resolution: 3.45 Å

EMDB-24505:
Structure of the SARS-CoV-2 S 6P trimer in complex with neutralizing antibody C118 (State 2)
Method: EM (single particle) / Resolution: 4.53 Å

PDB-7rks:
Structure of the SARS-CoV receptor binding domain in complex with the human neutralizing antibody Fab fragment, C118
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-7rku:
Structure of the SARS-CoV-2 receptor binding domain in complex with the human neutralizing antibody Fab fragment, C022
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

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

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
  • severe acute respiratory syndrome coronavirus
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / Antibody / Surface protein / Fab / coronavirus / fusion protein / binding domain / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex / SARS-CoV-2 / broadly neutralizing / virus / ANTIVIRAL PROTEIN

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