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TitleB cell genomics behind cross-neutralization of SARS-CoV-2 variants and SARS-CoV.
Journal, issue, pagesCell, Vol. 184, Issue 12, Page 3205-3221.e24, Year 2021
Publish dateJun 10, 2021
AuthorsJohannes F Scheid / Christopher O Barnes / Basak Eraslan / Andrew Hudak / Jennifer R Keeffe / Lisa A Cosimi / Eric M Brown / Frauke Muecksch / Yiska Weisblum / Shuting Zhang / Toni Delorey / Ann E Woolley / Fadi Ghantous / Sung-Moo Park / Devan Phillips / Betsabeh Tusi / Kathryn E Huey-Tubman / Alexander A Cohen / Priyanthi N P Gnanapragasam / Kara Rzasa / Theodora Hatziioanno / Michael A Durney / Xiebin Gu / Takuya Tada / Nathaniel R Landau / Anthony P West / Orit Rozenblatt-Rosen / Michael S Seaman / Lindsey R Baden / Daniel B Graham / Jacques Deguine / Paul D Bieniasz / Aviv Regev / Deborah Hung / Pamela J Bjorkman / Ramnik J Xavier /
PubMed AbstractMonoclonal antibodies (mAbs) are a focus in vaccine and therapeutic design to counteract severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and its variants. Here, we combined B cell ...Monoclonal antibodies (mAbs) are a focus in vaccine and therapeutic design to counteract severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and its variants. Here, we combined B cell sorting with single-cell VDJ and RNA sequencing (RNA-seq) and mAb structures to characterize B cell responses against SARS-CoV-2. We show that the SARS-CoV-2-specific B cell repertoire consists of transcriptionally distinct B cell populations with cells producing potently neutralizing antibodies (nAbs) localized in two clusters that resemble memory and activated B cells. Cryo-electron microscopy structures of selected nAbs from these two clusters complexed with SARS-CoV-2 spike trimers show recognition of various receptor-binding domain (RBD) epitopes. One of these mAbs, BG10-19, locks the spike trimer in a closed conformation to potently neutralize SARS-CoV-2, the recently arising mutants B.1.1.7 and B.1.351, and SARS-CoV and cross-reacts with heterologous RBDs. Together, our results characterize transcriptional differences among SARS-CoV-2-specific B cells and uncover cross-neutralizing Ab targets that will inform immunogen and therapeutic design against coronaviruses.
External linksCell / PubMed:34015271 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.1 - 4.0 Å
Structure data

23693

7m6e

EMDB-23693, PDB-7m6e:
Structure of the SARS-CoV-2 S 6P trimer in complex with the human neutralizing antibody Fab fragment, BG10-19
Method: EM (single particle) / Resolution: 3.3 Å

23694

7m6f

EMDB-23694, PDB-7m6f:
Structure of the SARS-CoV-2 S 6P trimer in complex with the human neutralizing antibody Fab fragment, BG1-22
Method: EM (single particle) / Resolution: 3.9 Å

23695

7m6g

EMDB-23695, PDB-7m6g:
Structure of the SARS-CoV-2 S 6P trimer in complex with the human neutralizing antibody Fab fragment, BG7-15
Method: EM (single particle) / Resolution: 3.7 Å

23696

7m6h

EMDB-23696, PDB-7m6h:
Structure of the SARS-CoV-2 S 2P trimer in complex with the human neutralizing antibody Fab fragment, BG7-20
Method: EM (single particle) / Resolution: 4.0 Å

23697

7m6i

EMDB-23697, PDB-7m6i:
Structure of the SARS-CoV-2 S 2P trimer in complex with the human neutralizing antibody Fab fragment, BG1-24
Method: EM (single particle) / Resolution: 4.0 Å

PDB-7m6d:
Structure of the SARS-CoV-2 RBD in complex with neutralizing antibodies BG4-25 and CR3022
Method: X-RAY DIFFRACTION / Resolution: 3.1 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/ANTIVIRAL PROTEIN / SARS-CoV-2 / Coronavirus / COVID-19 / antibody / neutralizing antibody / receptor binding domain / spike glycoprotein / ANTIVIRAL PROTEIN / VIRAL PROTEIN-ANTIVIRAL PROTEIN complex

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