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PDBsum entry 3w2d
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Immune system
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PDB id
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3w2d
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Contents |
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225 a.a.
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215 a.a.
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223 a.a.
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PDB id:
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| Name: |
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Immune system
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Title:
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Crystal structure of staphylococcal eenterotoxin b in complex with a novel neutralization monoclonal antibody fab fragment
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Structure:
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Enterotoxin type b. Chain: a. Synonym: seb. Engineered: yes. Monoclonal antibody 3e2 fab figment light chain. Chain: l. Engineered: yes. Monoclonal antibody 3e2 fab figment heavy chain. Chain: h.
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Source:
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Staphylococcus aureus. Organism_taxid: 1280. Gene: entb. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. Mouse. Organism_taxid: 10090. Expression_system_taxid: 562
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Resolution:
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3.10Å
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R-factor:
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0.200
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R-free:
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0.261
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Authors:
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S.Y.Liang,S.Hu,J.X.Dai,Y.J.Guo,Z.Y.Lou
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Key ref:
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T.Xia
et al.
(2014).
Structural basis for the neutralization and specificity of Staphylococcal enterotoxin B against its MHC Class II binding site.
Mabs,
6,
119-129.
PubMed id:
DOI:
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Date:
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28-Nov-12
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Release date:
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25-Dec-13
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PROCHECK
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Headers
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References
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P01552
(ETXB_STAAU) -
Enterotoxin type B from Staphylococcus aureus
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Seq:
Struc:
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266 a.a.
225 a.a.
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DOI no:
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Mabs
6:119-129
(2014)
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PubMed id:
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Structural basis for the neutralization and specificity of Staphylococcal enterotoxin B against its MHC Class II binding site.
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T.Xia,
S.Liang,
H.Wang,
S.Hu,
Y.Sun,
X.Yu,
J.Han,
J.Li,
S.Guo,
J.Dai,
Z.Lou,
Y.Guo.
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ABSTRACT
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Staphylococcal enterotoxin (SE) B is among the potent toxins produced by
Staphylococcus aureus that cause toxic shock syndrome (TSS), which can result in
multi-organ failure and death. Currently, neutralizing antibodies have been
shown to be effective immunotherapeutic agents against this toxin, but the
structural basis of the neutralizing mechanism is still unknown. In this study,
we generated a neutralizing monoclonal antibody, 3E2, against SEB, and analyzed
the crystal structure of the SEB-3E2 Fab complex. Crystallographic analysis
suggested that the neutralizing epitope overlapped with the MHC II molecule
binding site on SEB, and thus 3E2 could inhibit SEB function by preventing
interaction with the MHC II molecule. Mutagenesis studies were done on SEB, as
well as the related Staphylococcus aureus toxins SEA and SEC. These studies
revealed that tyrosine (Y)46 and lysine (K)71 residues of SEB are essential to
specific antibody-antigen recognition and neutralization. Substitution of Y at
SEA glutamine (Q)49, which corresponds to SEB Y46, increased both 3E2's binding
to SEA in vitro and the neutralization of SEA in vivo. These results suggested
that SEB Y46 is responsible for distinguishing SEB from SEA. These findings may
be helpful for the development of antibody-based therapy for SEB-induced TSS.
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Links
