Characterization of a broadly cross reactive tetravalent human monoclonal antibody, recognizing conformational epitopes in receptor binding domain of SARS-CoV-2

• DOI: 10.1007/s13205-022-03272-6
• Publication Date: 2022-08-02T16:02:57Z
• Authors: Sonal Garg; Nisha Raj; Asha Lukose; Deepti Jamwal; Hilal Ahmed Parray; Sandeep Kumar; Samridhi Dhyani; Kamini Jakhar; Sudipta Sonar; Mahima Tiwari; Reema; Shailendra Mani; Sankar Bhattacharyya; Chandresh Sharma; Tripti Shrivastava; Rajesh Kumar
• Keywords: Conformational epitope; Epitope mapping

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.