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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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PDB id:
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| Name: |
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Viral protein/immune system
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Title:
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Sars-cov-2 s/s2m11/s2x333 local refinement
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Structure:
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S2x333 fab light chain variable region. Chain: l. Engineered: yes. S2x333 fab heavy chain variable region. Chain: h. Engineered: yes. Spike glycoprotein. Chain: a. Synonym: s glycoprotein,e2,peplomer protein.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Severe acute respiratory syndrome coronavirus 2. 2019-ncov, sars-cov-2. Organism_taxid: 2697049.
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Authors:
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M.Mccallum,D.Veesler,Seattle Structural Genomics Center For Infectious Disease (Ssgcid)
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Key ref:
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M.McCallum
et al.
(2021).
N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2.
Cell,
184,
2332.
PubMed id:
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Date:
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05-Mar-21
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Release date:
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14-Apr-21
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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Cell
184:2332
(2021)
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PubMed id:
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N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2.
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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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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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Links
