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TitleAffinity maturation of SARS-CoV-2 neutralizing antibodies confers potency, breadth, and resilience to viral escape mutations.
Journal, issue, pagesImmunity, Vol. 54, Issue 8, Page 1853-11868.e7, Year 2021
Publish dateAug 10, 2021
AuthorsFrauke Muecksch / Yiska Weisblum / Christopher O Barnes / Fabian Schmidt / Dennis Schaefer-Babajew / Zijun Wang / Julio C C Lorenzi / Andrew I Flyak / Andrew T DeLaitsch / Kathryn E Huey-Tubman / Shurong Hou / Celia A Schiffer / Christian Gaebler / Justin Da Silva / Daniel Poston / Shlomo Finkin / Alice Cho / Melissa Cipolla / Thiago Y Oliveira / Katrina G Millard / Victor Ramos / Anna Gazumyan / Magdalena Rutkowska / Marina Caskey / Michel C Nussenzweig / Pamela J Bjorkman / Theodora Hatziioannou / Paul D Bieniasz /
PubMed AbstractAntibodies elicited by infection accumulate somatic mutations in germinal centers that can increase affinity for cognate antigens. We analyzed 6 independent groups of clonally related severe acute ...Antibodies elicited by infection accumulate somatic mutations in germinal centers that can increase affinity for cognate antigens. We analyzed 6 independent groups of clonally related severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2) Spike receptor-binding domain (RBD)-specific antibodies from 5 individuals shortly after infection and later in convalescence to determine the impact of maturation over months. In addition to increased affinity and neutralization potency, antibody evolution changed the mutational pathways for the acquisition of viral resistance and restricted neutralization escape options. For some antibodies, maturation imposed a requirement for multiple substitutions to enable escape. For certain antibodies, affinity maturation enabled the 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.
External linksImmunity / PubMed:34331873 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.26 - 3.55 Å
Structure data

24318

7r8m

EMDB-24318, PDB-7r8m:
Structure of the SARS-CoV-2 S 6P trimer in complex with neutralizing antibody C032
Method: EM (single particle) / Resolution: 3.4 Å

24319

7r8n

EMDB-24319, PDB-7r8n:
Structure of the SARS-CoV-2 S 6P trimer in complex with neutralizing antibody C051
Method: EM (single particle) / Resolution: 3.55 Å

24320

7r8o

EMDB-24320, PDB-7r8o:
Structure of the SARS-CoV-2 S 6P trimer in complex with neutralizing antibody C548
Method: EM (single particle) / Resolution: 3.5 Å

PDB-7n3e:
Crystal structure of an anti-SARS-CoV-2 human neutralizing antibody Fab fragment C032
Method: X-RAY DIFFRACTION / Resolution: 2.06 Å

PDB-7n3f:
Crystal structure of an anti-SARS-CoV-2 human neutralizing antibody Fab fragment C080
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-7n3g:
Crystal structure of an anti-SARS-CoV-2 human neutralizing antibody Fab fragment C098
Method: X-RAY DIFFRACTION / Resolution: 1.42 Å

PDB-7n3h:
Crystal structure of an anti-SARS-CoV-2 human neutralizing antibody Fab fragment C099
Method: X-RAY DIFFRACTION / Resolution: 1.26 Å

PDB-7n3i:
Crystal structure of the SARS-CoV-2 receptor binding domain in complex with the human neutralizing antibody Fab fragment C098
Method: X-RAY DIFFRACTION / Resolution: 2.03 Å

PDB-7r8l:
Structure of the SARS-CoV-2 RBD in complex with neutralizing antibody C099 and CR3022
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-HOH:
WATER / Water

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

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
KeywordsIMMUNE SYSTEM / severe acute respiratory syndrome coronavirus-2 / spike protein / neutralizing antibodies / IMMUNE SYSTEM/VIRAL PROTEIN / IMMUNE SYSTEM-VIRAL PROTEIN complex / VIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 / receptor binding domain / RBD / neutralizing antibody / COVID-19 / spike / ANTIVIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex

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