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TitleUltrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms.
Journal, issue, pagesScience, Vol. 370, Issue 6519, Page 950-957, Year 2020
Publish dateNov 20, 2020
AuthorsM Alejandra Tortorici / Martina Beltramello / Florian A Lempp / Dora Pinto / Ha V Dang / Laura E Rosen / Matthew McCallum / John Bowen / Andrea Minola / Stefano Jaconi / Fabrizia Zatta / Anna De Marco / Barbara Guarino / Siro Bianchi / Elvin J Lauron / Heather Tucker / Jiayi Zhou / Alessia Peter / Colin Havenar-Daughton / Jason A Wojcechowskyj / James Brett Case / Rita E Chen / Hannah Kaiser / Martin Montiel-Ruiz / Marcel Meury / Nadine Czudnochowski / Roberto Spreafico / Josh Dillen / Cindy Ng / Nicole Sprugasci / Katja Culap / Fabio Benigni / Rana Abdelnabi / Shi-Yan Caroline Foo / Michael A Schmid / Elisabetta Cameroni / Agostino Riva / Arianna Gabrieli / Massimo Galli / Matteo S Pizzuto / Johan Neyts / Michael S Diamond / Herbert W Virgin / Gyorgy Snell / Davide Corti / Katja Fink / David Veesler /
PubMed AbstractEfficient therapeutic options are needed to control the spread of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) that has caused more than 922,000 fatalities as of 13 September 2020. We ...Efficient therapeutic options are needed to control the spread of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) that has caused more than 922,000 fatalities as of 13 September 2020. We report the isolation and characterization of two ultrapotent SARS-CoV-2 human neutralizing antibodies (S2E12 and S2M11) that protect hamsters against SARS-CoV-2 challenge. Cryo-electron microscopy structures show that S2E12 and S2M11 competitively block angiotensin-converting enzyme 2 (ACE2) attachment and that S2M11 also locks the spike in a closed conformation by recognition of a quaternary epitope spanning two adjacent receptor-binding domains. Antibody cocktails that include S2M11, S2E12, or the previously identified S309 antibody broadly neutralize a panel of circulating SARS-CoV-2 isolates and activate effector functions. Our results pave the way to implement antibody cocktails for prophylaxis or therapy, circumventing or limiting the emergence of viral escape mutants.
External linksScience / PubMed:32972994 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.38 - 3.7 Å
Structure data

22659

7k43

EMDB-22659, PDB-7k43:
SARS-CoV-2 spike in complex with the S2M11 neutralizing antibody Fab fragment
Method: EM (single particle) / Resolution: 2.6 Å

22660

7k45

EMDB-22660, PDB-7k45:
SARS-CoV-2 spike in complex with the S2E12 neutralizing antibody Fab fragment (local refinement of the RBD and Fab variable domains)
Method: EM (single particle) / Resolution: 3.7 Å

22668

7k4n

EMDB-22668, PDB-7k4n:
SARS-CoV-2 spike in complex with the S2E12 neutralizing antibody Fab fragment
Method: EM (single particle) / Resolution: 3.3 Å

PDB-7k3q:
An ultra-potent human neutralizing antibody locks the SARS-CoV-2 spike in the closed conformation
Method: X-RAY DIFFRACTION / Resolution: 1.38 Å

Chemicals

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-EDO:
1,2-ETHANEDIOL / Ethylene glycol

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)
KeywordsIMMUNE SYSTEM / SARS-CoV-2 / neutralizing mAb / ANTIVIRAL PROTEIN / VIRAL PROTEIN/IMMUNE SYSTEM / COVID-19 / spike glycoprotein / fusion protein / neutralizing antibodies / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex

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