AI Article Synopsis
- * Binding studies indicate that II62 effectively interacts with various SARS-CoV-2 variants without disrupting the virus's ability to bind to the ACE2 receptor.
- * Neutralization tests show that increasing the antibody's valency from monovalent to tetravalent does not negatively affect its interaction with host cells in virus testing assays.
Article Abstract
Unlabelled: 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.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9345016 | PMC |
| http://dx.doi.org/10.1007/s13205-022-03272-6 | DOI Listing |
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