The antigenic anatomy of SARS-CoV-2 receptor binding domain
Journal
Cell
Journal Volume
184
Journal Issue
8
Pages
2183-2.2E+25
Date Issued
2021
Author(s)
Dejnirattisai W.
Zhou D.
Ginn H.M.
Duyvesteyn H.M.E.
Supasa P.
Case J.B.
Zhao Y.
Walter T.S.
Mentzer A.J.
Liu C.
Wang B.
Paesen G.C.
Slon-Campos J.
López-Camacho C.
Kafai N.M.
Bailey A.L.
Chen R.E.
Ying B.
Thompson C.
Bolton J.
Fyfe A.
Gupta S.
Tan T.K.
Gilbert-Jaramillo J.
James W.
Knight M.
Carroll M.W.
Skelly D.
Dold C.
Peng Y.
Levin R.
Dong T.
Pollard A.J.
Knight J.C.
Klenerman P.
Temperton N.
Hall D.R.
Williams M.A.
Paterson N.G.
Bertram F.K.R.
Siebert C.A.
Clare D.K.
Howe A.
Radecke J.
Song Y.
Townsend A.R.
Fry E.E.
Mongkolsapaya J.
Diamond M.S.
Ren J.
Stuart D.I.
Screaton G.R.
Abstract
< 0.1 μg/mL) blocking receptor interaction, except for one that binds a unique epitope in the N-terminal domain. Many of these neutralizing mAbs use public V-genes and are close to germline. We dissect the structural basis of recognition for this large panel of antibodies through X-ray crystallography and cryoelectron microscopy of 19 Fab-antigen structures. We find novel binding modes for some potently inhibitory antibodies and demonstrate that strongly neutralizing mAbs protect, prophylactically or therapeutically, in animal models.
SDGs
Publisher
Elsevier B.V.
Type
journal article