5n2b

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==The crystal structure of Burkholderia pseudomallei antigen and type I fimbria protein BPSL1626.==
==The crystal structure of Burkholderia pseudomallei antigen and type I fimbria protein BPSL1626.==
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<StructureSection load='5n2b' size='340' side='right' caption='[[5n2b]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='5n2b' size='340' side='right'caption='[[5n2b]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5n2b]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N2B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N2B FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5n2b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei_K96243 Burkholderia pseudomallei K96243]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N2B FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5n2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n2b OCA], [http://pdbe.org/5n2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n2b RCSB], [http://www.ebi.ac.uk/pdbsum/5n2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n2b ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5n2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n2b OCA], [https://pdbe.org/5n2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n2b RCSB], [https://www.ebi.ac.uk/pdbsum/5n2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n2b ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q63UH6_BURPS Q63UH6_BURPS]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Due to significant advances in computational biology, protein prediction, together with antigen and epitope design, have rapidly moved from conventional methods, based on experimental approaches, to in silico-based bioinformatics methods. In this context, we report a reverse vaccinology study that identified a panel of 104 candidate antigens from the Gram-negative bacterial pathogen Burkholderia pseudomallei, which is responsible for the disease melioidosis. B. pseudomallei can cause fatal sepsis in endemic populations in the tropical regions of the world and treatment with antibiotics is mostly ineffective. With the aim of identifying potential vaccine candidates, we report the experimental validation of predicted antigen and type I fimbrial subunit, BPSL1626, which we show is able to recognize and bind human antibodies from the sera of Burkholderia infected patients and to stimulate T-lymphocytes in vitro. The prerequisite for a melioidosis vaccine, in fact, is that both antibody- and cell-mediated immune responses must be triggered. In order to reveal potential antigenic regions of the protein that may aid immunogen re-design, we also report the crystal structure of BPSL1626 at 1.9 A resolution on which structure-based epitope predictions were based. Overall, our data suggest that BPSL1626 and three epitope regions here-identified can represent viable candidates as potential antigenic molecules.
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BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design against Burkholderia pseudomallei.,Capelli R, Peri C, Villa R, Nithichanon A, Conchillo-Sole O, Yero D, Gagni P, Chiari M, Lertmemongkolchai G, Cretich M, Daura X, Bolognesi M, Colombo G, Gourlay LJ Antibodies (Basel). 2018 Jul 19;7(3). pii: antib7030026. doi:, 10.3390/antib7030026. PMID:31544878<ref>PMID:31544878</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5n2b" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bolognesi, M]]
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[[Category: Burkholderia pseudomallei K96243]]
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[[Category: Gourlay, L J]]
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[[Category: Large Structures]]
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[[Category: Antigen]]
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[[Category: Bolognesi M]]
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[[Category: Fimbrial subunit]]
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[[Category: Gourlay LJ]]
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[[Category: Immune system]]
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[[Category: Incomplete immunoglobulin-like fold]]
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[[Category: Melioidosis]]
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Current revision

The crystal structure of Burkholderia pseudomallei antigen and type I fimbria protein BPSL1626.

PDB ID 5n2b

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