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Structure paper

TitleStructures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies.
Journal, issue, pagesCell, Vol. 182, Issue 4, Page 828-842.e16, Year 2020
Publish dateAug 20, 2020
AuthorsChristopher O Barnes / Anthony P West / Kathryn E Huey-Tubman / Magnus A G Hoffmann / Naima G Sharaf / Pauline R Hoffman / Nicholas Koranda / Harry B Gristick / Christian Gaebler / Frauke Muecksch / Julio C Cetrulo Lorenzi / Shlomo Finkin / Thomas Hägglöf / Arlene Hurley / Katrina G Millard / Yiska Weisblum / Fabian Schmidt / Theodora Hatziioannou / Paul D Bieniasz / Marina Caskey / Davide F Robbiani / Michel C Nussenzweig / Pamela J Bjorkman /
PubMed AbstractNeutralizing antibody responses to coronaviruses mainly target the receptor-binding domain (RBD) of the trimeric spike. Here, we characterized polyclonal immunoglobulin Gs (IgGs) and Fabs from COVID- ...Neutralizing antibody responses to coronaviruses mainly target the receptor-binding domain (RBD) of the trimeric spike. Here, we characterized polyclonal immunoglobulin Gs (IgGs) and Fabs from COVID-19 convalescent individuals for recognition of coronavirus spikes. Plasma IgGs differed in their focus on RBD epitopes, recognition of alpha- and beta-coronaviruses, and contributions of avidity to increased binding/neutralization of IgGs over Fabs. Using electron microscopy, we examined specificities of polyclonal plasma Fabs, revealing recognition of both S1 and RBD epitopes on SARS-CoV-2 spike. Moreover, a 3.4 Å cryo-electron microscopy (cryo-EM) structure of a neutralizing monoclonal Fab-spike complex revealed an epitope that blocks ACE2 receptor binding. Modeling based on these structures suggested different potentials for inter-spike crosslinking by IgGs on viruses, and characterized IgGs would not be affected by identified SARS-CoV-2 spike mutations. Overall, our studies structurally define a recurrent anti-SARS-CoV-2 antibody class derived from VH3-53/VH3-66 and similarity to a SARS-CoV VH3-30 antibody, providing criteria for evaluating vaccine-elicited antibodies.
External linksCell / PubMed:32645326 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.8 - 21.0 Å
Structure data

EMDB-22124:
SARS-CoV-2 S 2P negative-stain EM
Method: EM (single particle) / Resolution: 16.72 Å

EMDB-22125:
SARS-CoV-2 S 2P trimer complexed with COV57 polyclonal Fabs
Method: EM (single particle) / Resolution: 21.0 Å

EMDB-22126:
SARS-CoV-2 S 2P trimer complexed with polyclonal Fabs from recovered COVID-19 individual COV21
Method: EM (single particle) / Resolution: 21.0 Å

22127

6xcm

EMDB-22127, PDB-6xcm:
Structure of the SARS-CoV-2 spike glycoprotein in complex with the C105 neutralizing antibody Fab fragment (state 1)
Method: EM (single particle) / Resolution: 3.42 Å

22128

6xcn

EMDB-22128, PDB-6xcn:
Structure of the SARS-CoV-2 spike glycoprotein in complex with the C105 neutralizing antibody Fab fragment (state 2)
Method: EM (single particle) / Resolution: 3.66 Å

PDB-6xca:
Crystal structure of an anti-SARS-CoV-2 human neutralizing antibody Fab fragment, C105
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-SO4:
SULFATE ION / Sulfate

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 / Antibody / SARS-CoV-2 / SARS2 / Coronavirus / Neutralizing / VIRAL PROTEIN/IMMUNE SYSTEM / Spike glycoprotein / COVID-19 / monoclonal neutralizing antibody / Fabs / nsEMPEM / VIRAL PROTEIN-IMMUNE SYSTEM complex

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