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TitlePotent and broad neutralization of SARS-CoV-2 variants of concern (VOCs) including omicron sub-lineages BA.1 and BA.2 by biparatopic human VH domains.
Journal, issue, pagesiScience, Vol. 25, Issue 8, Page 104798, Year 2022
Publish dateAug 19, 2022
AuthorsChuan Chen / James W Saville / Michelle M Marti / Alexandra Schäfer / Mary Hongying Cheng / Dhiraj Mannar / Xing Zhu / Alison M Berezuk / Anupam Banerjee / Michele D Sobolewski / Andrew Kim / Benjamin R Treat / Priscila Mayrelle Da Silva Castanha / Nathan Enick / Kevin D McCormick / Xianglei Liu / Cynthia Adams / Margaret Grace Hines / Zehua Sun / Weizao Chen / Jana L Jacobs / Simon M Barratt-Boyes / John W Mellors / Ralph S Baric / Ivet Bahar / Dimiter S Dimitrov / Sriram Subramaniam / David R Martinez / Wei Li /
PubMed AbstractThe emergence of SARS-CoV-2 variants of concern (VOCs) requires the development of next-generation biologics with high neutralization breadth. Here, we characterized a human V domain, F6, which we ...The emergence of SARS-CoV-2 variants of concern (VOCs) requires the development of next-generation biologics with high neutralization breadth. Here, we characterized a human V domain, F6, which we generated by sequentially panning large phage-displayed V libraries against receptor binding domains (RBDs) containing VOC mutations. Cryo-EM analyses reveal that F6 has a unique binding mode that spans a broad surface of the RBD and involves the antibody framework region. Attachment of an Fc region to a fusion of F6 and ab8, a previously characterized V domain, resulted in a construct (F6-ab8-Fc) that broadly and potently neutralized VOCs including Omicron. Additionally, prophylactic treatment using F6-ab8-Fc reduced live Beta (B.1.351) variant viral titers in the lungs of a mouse model. Our results provide a new potential therapeutic against SARS-CoV-2 variants including Omicron and highlight a vulnerable epitope within the spike that may be exploited to achieve broad protection against circulating variants.
External linksiScience / PubMed:35875685 / PubMed Central
MethodsEM (single particle)
Resolution2.83 - 3.04 Å
Structure data

EMDB-27438: Cryo-EM structure of SARS-CoV-2 Beta (B.1.351) spike protein in complex with VH domain F6
Method: EM (single particle) / Resolution: 2.83 Å

27439

8di5

EMDB-27439, PDB-8di5:
Cryo-EM structure of SARS-CoV-2 Beta (B.1.351) spike protein in complex with VH domain F6 (focused refinement of RBD and VH F6)
Method: EM (single particle) / Resolution: 3.04 Å

Chemicals

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

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 / glycoprotein / fusion protein / viral protein / VH domain / F6 / VIRAL PROTEIN-IMMUNE SYSTEM complex

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