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TitleIdentification of broad, potent antibodies to functionally constrained regions of SARS-CoV-2 spike following a breakthrough infection.
Journal, issue, pagesbioRxiv, Year 2023
Publish dateMar 29, 2023
AuthorsJamie Guenthoer / Michelle Lilly / Tyler N Starr / Bernadeta Dadonaite / Klaus N Lovendahl / Jacob T Croft / Caitlin I Stoddard / Vrasha Chohan / Shilei Ding / Felicitas Ruiz / Mackenzie S Kopp / Andr S Finzi / Jesse D Bloom / Helen Y Chu / Kelly K Lee / Julie Overbaugh
PubMed AbstractThe antiviral benefit of antibodies can be compromised by viral escape especially for rapidly evolving viruses. Therefore, durable, effective antibodies must be both broad and potent to counter newly ...The antiviral benefit of antibodies can be compromised by viral escape especially for rapidly evolving viruses. Therefore, durable, effective antibodies must be both broad and potent to counter newly emerging, diverse strains. Discovery of such antibodies is critically important for SARS-CoV-2 as the global emergence of new variants of concern (VOC) has compromised the efficacy of therapeutic antibodies and vaccines. We describe a collection of broad and potent neutralizing monoclonal antibodies (mAbs) isolated from an individual who experienced a breakthrough infection with the Delta VOC. Four mAbs potently neutralize the Wuhan-Hu-1 vaccine strain, the Delta VOC, and also retain potency against the Omicron VOCs through BA.4/BA.5 in both pseudovirus-based and authentic virus assays. Three mAbs also retain potency to recently circulating VOCs XBB.1.5 and BQ.1.1 and one also potently neutralizes SARS-CoV-1. The potency of these mAbs was greater against Omicron VOCs than all but one of the mAbs that had been approved for therapeutic applications. The mAbs target distinct epitopes on the spike glycoprotein, three in the receptor binding domain (RBD) and one in an invariant region downstream of the RBD in subdomain 1 (SD1). The escape pathways we defined at single amino acid resolution with deep mutational scanning show they target conserved, functionally constrained regions of the glycoprotein, suggesting escape could incur a fitness cost. Overall, these mAbs are novel in their breadth across VOCs, their epitope specificity, and include a highly potent mAb targeting a rare epitope outside of the RBD in SD1.
External linksbioRxiv / PubMed:36561191 / PubMed Central
MethodsEM (single particle)
Resolution6.72 - 9.2 Å
Structure data

EMDB-29052: SARS-CoV-2 Spike Hexapro - C68.59 Fab (Class 3 - disordered)
Method: EM (single particle) / Resolution: 9.2 Å

EMDB-29053: SARS-CoV-2 Spike Hexapro - C59.68 Fab (Class 1 - No Fab bound)
Method: EM (single particle) / Resolution: 6.72 Å

EMDB-29054: SARS-CoV-2 Spike Hexapro - C68.59 Fab (Class 2 - Fab bound)
Method: EM (single particle) / Resolution: 6.72 Å

Source
  • Severe acute respiratory syndrome coronavirus 2
  • Homo sapiens (human)

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