Development of potency, breadth and resilience to viral escape mutations in SARS-CoV-2 neutralizing antibodies
Open accessAbstract
Summary: Antibodies elicited in response to infection undergo somatic mutation in germinal centers that can result in higher affinity for the cognate antigen. To determine the effects of somatic mutation on the properties of SARS-CoV-2 spike receptor-binding domain (RBD)-specific antibodies, we analyzed six independent antibody lineages. As well as increased neutralization potency, antibody evolution changed pathways for acquisition of resistance and, in some cases, restricted the range of neutralization escape options. For some antibodies, maturation apparently imposed a requirement for multiple spike mutations to enable escape. For certain antibody lineages, maturation enabled neutralization of circulating SARS-CoV-2 variants of concern and heterologous sarbecoviruses. Antibody-antigen structures revealed that these properties resulted from substitutions that allowed additional variability at the interface with the RBD. These findings suggest that increasing antibody diversity through prolonged or repeated antigen exposure may improve protection against diversifying SARS-CoV-2 populations, and perhaps against other pandemic threat coronaviruses.
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The memory B cell compartment accumulates mutations and undergoes clonal evolution over the initial six months after infection.
“The memory B cell compartment accumulates mutations and undergoes clonal evolution over the initial six months after infection4,9,21,22.”
From Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection (2021) · cites this paper as [9]
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Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection
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Nanobodies from camelid mice and llamas neutralize SARS-CoV-2 variants
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B cell genomics behind cross-neutralization of SARS-CoV-2 variants and SARS-CoV
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Highly synergistic combinations of nanobodies that target SARS-CoV-2 and are resistant to escape
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Spike protein of SARS-CoV-2 variants: a brief review and practical implications
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- Authors
- Muecksch, F., Weisblum, Y., Barnes, C. O., Schmidt, F., Schaefer-Babajew, D., Lorenzi, J. C. C., Flyak, A. I., DeLaitsch, A. T., Huey-Tubman, K. E., Hou, S., Schiffer, C. A., Gaebler, C., Wang, Z., Da Silva, J., Poston, D., Finkin, S., Cho, A., Cipolla, M., Oliveira, T. Y., Millard, K. G., Ramos, V., Gazumyan, A., Rutkowska, M., Caskey, M., Nussenzweig, M. C., Bjorkman, P. J., Hatziioannou, T., & Bieniasz, P. D.
- Affiliations
- Rockefeller University (US)
- California Institute of Technology (US)
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Nussenzweig, Michel C.
- Bieniasz, Paul D.
- ORCID
- Muecksch, Frauke
- Weisblum, Yiska
- Barnes, Christopher O.
- Schmidt, Fabian
- Schaefer-Babajew, Dennis
- Lorenzi, Julio C C
- Flyak, Andrew I
- DeLaitsch, Andrew T
- Hou, Shurong
- Schiffer, Celia A.
- Gaebler, Christian
- Wang, Zijun
- Poston, Daniel
- Finkin, Shlomo
- Cho, Alice
- Cipolla, Melissa
- Oliveira, Thiago Y.
- Millard, Katrina G.
- Gazumyan, Anna
- Rutkowska, Magdalena
- Caskey, Marina
- Nussenzweig, Michel C.
- Bieniasz, Paul D.
- Venue
- bioRxiv (Cold Spring Harbor Laboratory)
- Publisher
- openRxiv
- Published
- 2021-03-08
- PMC
- PMC7987023
- OpenAlex
- W3134460024
- Cited by
- 39
- References
- 80
- Citations by year
- 2025: 3 · 2023: 2 · 2022: 9 · 2021: 25
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion, cc-by-nc-nd)
- Funders
- National Science Foundation (P41GM103393, 1745301)
- Howard Hughes Medical Institute (UL1TR001866)
- U.S. Department of Energy (COVID-19, P41GM103393, DE-AC02-)
- Burroughs Wellcome Fund
- George Mason University
- California Institute of Technology
- National Institutes of Health (COVID-19, AI138938, P01 AI138938-S1, TR001866, UL1TR001866)
- Office of Science (P41GM103393, DE-AC02)
- Beckman Institute, California Institute of Technology
- National Institute of General Medical Sciences (P41GM103393)
- National Institute of Allergy and Infectious Diseases (COVID-19, R01AI78788, R01AI078788, K99AI153465, U19AI111825, P01AI138938, R37AI064003)
- National Center for Advancing Translational Sciences (TR001866)
- Basic Energy Sciences (DE-AC02, P41GM103393)
- Biological and Environmental Research (P41 GM103393)
- SLAC National Accelerator Laboratory (P41GM103393)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Keywords
- SARS-CoV-2, neutralizing antibodies, spike protein receptor-binding domain, viral escape mutations, somatic hypermutation, antibody maturation, antibody diversity, variants of concern, antibody-antigen interface
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