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PDBsum entry 7lxw
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Viral protein/immune system
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PDB id
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7lxw
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Contents |
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100 a.a.
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121 a.a.
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96 a.a.
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References listed in PDB file
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Key reference
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Title
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N-Terminal domain antigenic mapping reveals a site of vulnerability for sars-Cov-2.
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Authors
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M.Mccallum,
A.De marco,
F.A.Lempp,
M.A.Tortorici,
D.Pinto,
A.C.Walls,
M.Beltramello,
A.Chen,
Z.Liu,
F.Zatta,
S.Zepeda,
J.Di iulio,
J.E.Bowen,
M.Montiel-Ruiz,
J.Zhou,
L.E.Rosen,
S.Bianchi,
B.Guarino,
C.S.Fregni,
R.Abdelnabi,
S.C.Foo,
P.W.Rothlauf,
L.M.Bloyet,
F.Benigni,
E.Cameroni,
J.Neyts,
A.Riva,
G.Snell,
A.Telenti,
S.P.J.Whelan,
H.W.Virgin,
D.Corti,
M.S.Pizzuto,
D.Veesler.
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Ref.
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Cell, 2021,
184,
2332.
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PubMed id
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Abstract
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The SARS-CoV-2 spike (S) glycoprotein contains an immunodominant
receptor-binding domain (RBD) targeted by most neutralizing antibodies (Abs) in
COVID-19 patient plasma. Little is known about neutralizing Abs binding to
epitopes outside the RBD and their contribution to protection. Here, we describe
41 human monoclonal Abs (mAbs) derived from memory B cells, which recognize the
SARS-CoV-2 S N-terminal domain (NTD) and show that a subset of them neutralize
SARS-CoV-2 ultrapotently. We define an antigenic map of the SARS-CoV-2 NTD and
identify a supersite (designated site i) recognized by all known NTD-specific
neutralizing mAbs. These mAbs inhibit cell-to-cell fusion, activate effector
functions, and protect Syrian hamsters from SARS-CoV-2 challenge, albeit
selecting escape mutants in some animals. Indeed, several SARS-CoV-2 variants,
including the B.1.1.7, B.1.351, and P.1 lineages, harbor frequent mutations
within the NTD supersite, suggesting ongoing selective pressure and the
importance of NTD-specific neutralizing mAbs for protective immunity and vaccine
design.
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