PMC:7243778 / 12246-13855 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7243778","sourcedb":"PMC","sourceid":"7243778","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7243778","text":"The human single-chain variable region fragment (scFv) antibody 80R blocked ACE-RBD interaction (epitope aa 324–503) [32] but some 80R-escape variants were found with the mutations mostly locating at lysine D480 [33]. The target epitope of 80R is not conserved in SARS-CoV-2 then it does not affect this novel virus [34]. Another nAb generated from a non-immune scFv library, named 256, could bind to an epitope of RBD but did not inhibit RBD binding. 256 is weak but specific to D480A-muted strains of 80R-escape variants. Some engineered broad nAbs, fm6 and fm39, also showed a high affinity to D480A-muted strains [33]. m396 (epitope aa 482–491) from human antibody fab library was cross-reactive [35] and used the D95 of m396 to form a salt bridge with R395 or an electrostatic interaction with D408 of SARS-CoV RBD [34]. m396 potently neutralized GD03 strain isolated from the second outbreak which resisted neutralization by 80R and S3.1. m396 also neutralized isolates from the first SARS-CoV outbreak (Urbani, Tor2) and from palm civets (SZ3, SZ16) [36]. Another human monoclonal antibody from scFv libraries CR3014 (epitope aa 318–510) showed potent effects on SARS-CoV neutralization; however, this virus can escape CR3014 upon P426L mutation in the S glycoprotein [37]. Same as 80R, m396 and CR3014 RBD-specific SARS-CoV antibodies failed to bind the S protein of SARS-CoV-2 [34]. CR3022, always from scFv libraries, could bind noncompetitively the SARS-CoV RBD (epitope aa 318–510) and had a synergistic neutralizing effect with CR3014 on SARS-CoV, even with the escaped P426L-muted variants 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