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TitleAn antibody class with a common CDRH3 motif broadly neutralizes sarbecoviruses.
Journal, issue, pagesSci Transl Med, Vol. 14, Issue 646, Page eabn6859, Year 2022
Publish dateMay 25, 2022
AuthorsLihong Liu / Sho Iketani / Yicheng Guo / Eswar R Reddem / Ryan G Casner / Manoj S Nair / Jian Yu / Jasper F-W Chan / Maple Wang / Gabriele Cerutti / Zhiteng Li / Nicholas C Morano / Candace D Castagna / Laura Corredor / Hin Chu / Shuofeng Yuan / Vincent Kwok-Man Poon / Chris Chun-Sing Chan / Zhiwei Chen / Yang Luo / Marcus Cunningham / Alejandro Chavez / Michael T Yin / David S Perlin / Moriya Tsuji / Kwok-Yung Yuen / Peter D Kwong / Zizhang Sheng / Yaoxing Huang / Lawrence Shapiro / David D Ho /
PubMed AbstractThe devastation caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has made clear the importance of pandemic preparedness. To address future zoonotic outbreaks due to related ...The devastation caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has made clear the importance of pandemic preparedness. To address future zoonotic outbreaks due to related viruses in the sarbecovirus subgenus, we identified a human monoclonal antibody, 10-40, that neutralized or bound all sarbecoviruses tested in vitro and protected against SARS-CoV-2 and SARS-CoV in vivo. Comparative studies with other receptor-binding domain (RBD)-directed antibodies showed 10-40 to have the greatest breadth against sarbecoviruses, suggesting that 10-40 is a promising agent for pandemic preparedness. Moreover, structural analyses on 10-40 and similar antibodies not only defined an epitope cluster in the inner face of the RBD that is well conserved among sarbecoviruses but also uncovered a distinct antibody class with a common CDRH3 motif. Our analyses also suggested that elicitation of this class of antibodies may not be overly difficult, an observation that bodes well for the development of a pan-sarbecovirus vaccine.
External linksSci Transl Med / PubMed:35438546 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.53 - 6.5 Å
Structure data

EMDB-25146: Broadly Neutralizing Antibody 10-40 in complex with prefusion SARS-CoV-2 B.1.351 Spike glycoprotein
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-25166: Antibody 10-28 in complex with prefusion SARS-CoV-2 B.1.351 Spike glycoprotein
Method: EM (single particle) / Resolution: 6.5 Å

EMDB-25167: Antibody 11-11 in complex with prefusion SARS-CoV-2 B.1.351 Spike glycoprotein
Method: EM (single particle) / Resolution: 6.4 Å

PDB-7sd5:
Crystallographic structure of neutralizing antibody 10-40 in complex with SARS-CoV-2 spike receptor binding domain
Method: X-RAY DIFFRACTION / Resolution: 1.53 Å

PDB-7si2:
Crystal structure of neutralizing antibody 10-28 in complex with SARS-CoV-2 spike receptor binding domain (RBD)
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-7ttm:
Crystal structure of potent neutralizing antibody 10-40 in complex with Sarbecovirus bat SHC014 receptor-binding domain
Method: X-RAY DIFFRACTION / Resolution: 2.24 Å

PDB-7ttx:
Crystal structure of potent neutralizing antibody 10-40 in complex with Sarbecovirus bat RaTG13 receptor-binding domain
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-7tty:
Crystal structure of potent neutralizing antibody 10-40 in complex with bat WIV1 receptor-binding domain
Method: X-RAY DIFFRACTION / Resolution: 3.11 Å

Chemicals

ChemComp-HOH:
WATER / Water

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

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
  • bat sars-like coronavirus rsshc014
  • bat coronavirus ratg13
  • bat sars-like coronavirus wiv1
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / COVID-19 / SARS-CoV-2 / Viral protein / Spike glycoprotein / Receptor Binding Protein / RBD / Neutralizing antibody / 10-40 / Fab / VIRAL PROTEIN-IMMUNE SYSTEM complex / 10-28 / SarbecoVirus / SCH014 RBD / potent / RaTG13 RBD / WIV1 RBD

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