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TitleA combination of cross-neutralizing antibodies synergizes to prevent SARS-CoV-2 and SARS-CoV pseudovirus infection.
Journal, issue, pagesCell Host Microbe, Vol. 29, Issue 5, Page 806-818.e6, Year 2021
Publish dateMay 12, 2021
AuthorsHejun Liu / Meng Yuan / Deli Huang / Sandhya Bangaru / Fangzhu Zhao / Chang-Chun D Lee / Linghang Peng / Shawn Barman / Xueyong Zhu / David Nemazee / Dennis R Burton / Marit J van Gils / Rogier W Sanders / Hans-Christian Kornau / S Momsen Reincke / Harald Prüss / Jakob Kreye / Nicholas C Wu / Andrew B Ward / Ian A Wilson /
PubMed AbstractCoronaviruses have caused several human epidemics and pandemics including the ongoing coronavirus disease 2019 (COVID-19). Prophylactic vaccines and therapeutic antibodies have already shown striking ...Coronaviruses have caused several human epidemics and pandemics including the ongoing coronavirus disease 2019 (COVID-19). Prophylactic vaccines and therapeutic antibodies have already shown striking effectiveness against COVID-19. Nevertheless, concerns remain about antigenic drift in SARS-CoV-2 as well as threats from other sarbecoviruses. Cross-neutralizing antibodies to SARS-related viruses provide opportunities to address such concerns. Here, we report on crystal structures of a cross-neutralizing antibody, CV38-142, in complex with the receptor-binding domains from SARS-CoV-2 and SARS-CoV. Recognition of the N343 glycosylation site and water-mediated interactions facilitate cross-reactivity of CV38-142 to SARS-related viruses, allowing the antibody to accommodate antigenic variation in these viruses. CV38-142 synergizes with other cross-neutralizing antibodies, notably COVA1-16, to enhance neutralization of SARS-CoV and SARS-CoV-2, including circulating variants of concern B.1.1.7 and B.1.351. Overall, this study provides valuable information for vaccine and therapeutic design to address current and future antigenic drift in SARS-CoV-2 and to protect against zoonotic SARS-related coronaviruses.
External linksCell Host Microbe / PubMed:33894127 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.53 - 31.0 Å
Structure data

EMDB-23469:
SARS-CoV spike complexed with Fab CV38-142 (3 Fabs bound)
Method: EM (single particle) / Resolution: 27.8 Å

EMDB-23470:
SARS-CoV spike complexed with Fab CV38-142 (2 Fabs bound)
Method: EM (single particle) / Resolution: 29.3 Å

EMDB-23471:
SARS-CoV-2 spike complexed with Fab CV38-142 (3 Fabs bound)
Method: EM (single particle) / Resolution: 27.8 Å

EMDB-23472:
SARS-CoV-2 spike complexed with Fab CV38-142 (2 Fabs bound)
Method: EM (single particle) / Resolution: 31.0 Å

PDB-7lm8:
Crystal structure of SARS-CoV-2 spike protein receptor-binding domain in complex with two cross-neutralizing antibodies CV38-142 and COVA1-16 Fabs isolated from COVID-19 patients
Method: X-RAY DIFFRACTION / Resolution: 1.936 Å

PDB-7lm9:
Crystal structure of SARS-CoV spike protein receptor-binding domain in complex with a cross-neutralizing antibody CV38-142 Fab isolated from COVID-19 patient
Method: X-RAY DIFFRACTION / Resolution: 1.53 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL / Ethylene glycol

ChemComp-HOH:
WATER / Water

Source
  • Severe acute respiratory syndrome-related coronavirus
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
  • sars coronavirus ma15
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 / SARS-CoV / Antibody / Spike / Coronavirus / COVID-19 / SARS / IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM complex / Cross-Neutralization / Synergy / VIRAL PROTEIN

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