Cross-neutralizing antibodies bind a SARS-CoV-2 cryptic site and resist circulating variants.
Nat Commun
; 12(1): 5652, 2021 09 27.
Article
in English
| MEDLINE | ID: covidwho-1440473
ABSTRACT
The emergence of numerous variants of SARS-CoV-2, the causative agent of COVID-19, has presented new challenges to the global efforts to control the COVID-19 pandemic. Here, we obtain two cross-neutralizing antibodies (7D6 and 6D6) that target Sarbecoviruses' receptor-binding domain (RBD) with sub-picomolar affinities and potently neutralize authentic SARS-CoV-2. Crystal structures show that both antibodies bind a cryptic site different from that recognized by existing antibodies and highly conserved across Sarbecovirus isolates. Binding of these two antibodies to the RBD clashes with the adjacent N-terminal domain and disrupts the viral spike. Both antibodies confer good resistance to mutations in the currently circulating SARS-CoV-2 variants. Thus, our results have direct relevance to public health as options for passive antibody therapeutics and even active prophylactics. They can also inform the design of pan-sarbecovirus vaccines.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Immunization, Passive
/
Broadly Neutralizing Antibodies
/
SARS-CoV-2
/
COVID-19
/
Antibodies, Viral
Type of study:
Observational study
/
Randomized controlled trials
Topics:
Vaccines
/
Variants
Language:
English
Journal:
Nat Commun
Journal subject:
Biology
/
Science
Year:
2021
Document Type:
Article
Affiliation country:
S41467-021-25997-3
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