A highly conserved cryptic epitope in the receptor-binding domains of SARS-CoV-2 and SARS-CoV.
Ian Wilson group (Scripps Research Institute) and collaborators
Ian Wilson's lab at The Scripps Research Institute
reports the structure of the receptor-binding domain (RBD) of the
SARS-CoV-2 spike protein with a bound Fab fragment of the human
neutralizing antibody CR3022. CR3022, isolated more than 15 years ago
from a convalescent SARS patient, targets a highly conserved epitope on
the RBD.
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Figure:
Crystal structure of CR3022 in complex with SARS-CoV-2 RBD.
(A) Overall topology of the SARS-CoV-2 spike glycoprotein. NTD: N-terminal
domain, RBD: receptor-binding domain, SD1: subdomain 1, SD2: subdomain 2,
FP: fusion peptide, HR1: heptad repeat 1, HR2: heptad repeat 2, TM:
transmembrane region, IC: intracellular domain.
(B) Structure of CR3022 Fab in complex with SARS-CoV-2 RBD. CR3022 heavy
chain is colored in orange, CR3022 light chain in yellow, and SARS-CoV-2
RBD in light grey.
(C-D) Epitoperesidues on SARS-CoV-2 are colored in cyan and green. CDR
loops are labeled.
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Citation:
M. Yuan, N.C. Wu, X. Zhu, C.D. Lee, R.T.Y. So, H. Lv, C.K.P. Mok,
I.A. Wilson, Science, 03 April 2020,
DOI: 10.1126/science.abb7269.
See also
the Scripps Institute News Report.
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