Characterization of a broadly cross reactive tetravalent human monoclonal antibody, recognizing conformational epitopes in receptor binding domain of SARS-CoV-2.
3 Biotech
; 12(9): 202, 2022 Sep.
Article
in English
| MEDLINE | ID: covidwho-1971859
ABSTRACT
We used human semi-synthetic phage antibody gene libraries to select anti-SARS-CoV-2 RBD scFv antibody fragment and subsequent characterization of this novel tetravalent monoclonal antibody targeting conformational epitopes in the receptor binding domain of SARS-CoV-2. Binding studies suggest that II62 tetravalent antibody cross-reacts with RBD protein of SARS-CoV2 and its different variants of concerns. The epitope mapping data reveals that II62 tetravalent antibody targets an epitope that does not directly interferes with RBD ACE2 interaction. Neutralization studies with live authentic SARS-CoV2 virus suggests that increase in valency of II62 mAb from monovalent to tetravalent doesn't perturbate virus interactions with the ACE2 expressing host cells in cytopathic effect-based (CPE) assay. Supplementary Information The online version contains supplementary material available at 10.1007/s13205-022-03272-6.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Type of study:
Case report
/
Randomized controlled trials
Topics:
Variants
Language:
English
Journal:
3 Biotech
Year:
2022
Document Type:
Article
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