Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody

By D. Pinto, Young-Jun Park, M. Beltramello, A. Walls, M. Tortorici, S. Bianchi, S. Jaconi, K. Culap, F. Zatta, A. De Marco and 15 more. 2020

1,849 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Deep mutational scanning of SARS-CoV-2 receptor binding domain reveals constraints on folding and ACE2 binding (2020, positive): “These core-RBD epitopes are highly conserved across the sarbecovirus alignment (Figure S7E), explaining the cross-reactivity of these antibodies between SARS-CoV-1 and SARS-CoV-2 (Huo et al., 2020; Pinto et al., 2020; Wrapp et al., 2020c).”
SARS-CoV-2 D614G Variant Exhibits Efficient Replication ex vivo and Transmission in vivo (2020, neutral): “The nAbs S309, REGN10933, REGN10987, and JS016 were reported previously (28, 29) and were kindly”
Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding (2020, positive): “Mutational Constraint of Antibody Epitopes The RBD is the dominant target of neutralizing antibodies to SARS-CoV-2 (Brouwer et al., 2020; Cao et al., 2020; Ju et al., 2020; Pinto et al., 2020; Premkumar et al., 2020; Rogers et al., 2020; Suthar et al., 2020; Yuan et al., 2020a; Zhang et al., 2020; Z”
Controlling the SARS-CoV-2 spike glycoprotein conformation (2020, positive): “…double mutant (rS2d) would presumably not elicit antibodies targeting the receptor binding site, which make up the majority of observed responses in convalescent patients 39,40 , but it would still be capable of eliciting antibodies such as S309 that are able to bind the ‘down’ state RBD 41 .”