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PDBsum entry 4b5c
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Lipid transport
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PDB id
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4b5c
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PDB id:
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Lipid transport
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Title:
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Crystal structure of the peptidoglycan-associated lipoprotein from burkholderia pseudomallei
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Structure:
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Putative ompa family lipoprotein. Chain: a, b, c. Fragment: residues 36-170. Synonym: peptidoglycan-associated lipoprotein. Engineered: yes
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Source:
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Burkholderia pseudomallei. Organism_taxid: 28450. Strain: k96423. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: star.
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Resolution:
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2.30Å
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R-factor:
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0.209
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R-free:
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0.249
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Authors:
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L.J.Gourlay,C.Peri,O.Conchillo-Sole,M.Ferrer-Navarro,A.Gori,R.Longhi, D.Rinchai,G.Lertmemongkolchai,P.Lassaux,X.Daura,G.Colombo, M.Bolognesi
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Key ref:
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L.J.Gourlay
et al.
(2013).
Exploiting the Burkholderia pseudomallei acute phase antigen BPSL2765 for structure-based epitope discovery/design in structural vaccinology.
Chem Biol,
20,
1147-1156.
PubMed id:
DOI:
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Date:
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03-Aug-12
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Release date:
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14-Aug-13
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PROCHECK
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Headers
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References
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Q63RA7
(Q63RA7_BURPS) -
Peptidoglycan-associated lipoprotein from Burkholderia pseudomallei (strain K96243)
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Seq: Struc:
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170 a.a.
119 a.a.
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Key: |
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Secondary structure |
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CATH domain |
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DOI no:
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Chem Biol
20:1147-1156
(2013)
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PubMed id:
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Exploiting the Burkholderia pseudomallei acute phase antigen BPSL2765 for structure-based epitope discovery/design in structural vaccinology.
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L.J.Gourlay,
C.Peri,
M.Ferrer-Navarro,
O.Conchillo-Solé,
A.Gori,
D.Rinchai,
R.J.Thomas,
O.L.Champion,
S.L.Michell,
C.Kewcharoenwong,
A.Nithichanon,
P.Lassaux,
L.Perletti,
R.Longhi,
G.Lertmemongkolchai,
R.W.Titball,
X.Daura,
G.Colombo,
M.Bolognesi.
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ABSTRACT
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We solved the crystal structure of Burkholderia pseudomallei acute phase antigen
BPSL2765 in the context of a structural vaccinology study, in the area of
melioidosis vaccine development. Based on the structure, we applied a recently
developed method for epitope design that combines computational epitope
predictions with in vitro mapping experiments and successfully identified a
consensus sequence within the antigen that, when engineered as a synthetic
peptide, was selectively immunorecognized to the same extent as the recombinant
protein in sera from melioidosis-affected subjects. Antibodies raised against
the consensus peptide were successfully tested in opsonization bacterial killing
experiments and antibody-dependent agglutination tests of B. pseudomallei. Our
strategy represents a step in the development of immunodiagnostics, in the
production of specific antibodies and in the optimization of antigens for
vaccine development, starting from structural and physicochemical principles.
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');
}
}
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