4o49: Difference between revisions
New page: '''Unreleased structure''' The entry 4o49 is ON HOLD Authors: Calmettes, C, Yu, RH, Schryvers, AB, Moraes, TF Description: Crystal structure of the vaccine antigen Transferrin Binding ... |
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==Crystal structure of the vaccine antigen Transferrin Binding Protein B (TbpB) mutant Tyr-174-Ala from Actinobacillus pleuropneumoniae H87== | |||
<StructureSection load='4o49' size='340' side='right'caption='[[4o49]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4o49]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinobacillus_pleuropneumoniae Actinobacillus pleuropneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O49 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4o49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o49 OCA], [https://pdbe.org/4o49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o49 RCSB], [https://www.ebi.ac.uk/pdbsum/4o49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o49 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Host adapted Gram-negative bacterial pathogens from the Pasteurellaceae, Neisseriaceae and Moraxellaceae families normally reside in the upper respiratory or genitourinary tracts of their hosts and rely on utilizing iron from host transferrin (Tf) for growth and survival. The surface receptor proteins that mediate this critical iron acquisition pathway have been proposed as ideal vaccine targets due to the critical role that they play in survival and disease pathogenesis in vivo. In particular, the surface lipoprotein component of the receptor, Tf binding protein B (TbpB), had received considerable attention as a potential antigen for vaccines in humans and food production animals but this has not translated into the series of successful vaccine products originally envisioned. Preliminary immunization experiments suggesting that host Tf could interfere with development of the immune response prompted us to directly address this question with site-directed mutant proteins defective in binding Tf. Site-directed mutants with dramatically reduced binding of porcine transferrin and nearly identical structure to the native proteins were prepared. A mutant Haemophilus parasuis TbpB was shown to induce an enhanced B-cell and T-cell response in pigs relative to native TbpB and provide superior protection from infection than the native TbpB or a commercial vaccine product. The results indicate that binding of host transferrin modulates the development of the immune response against TbpBs and that strategies designed to reduce or eliminate binding can be used to generate superior antigens for vaccines. | |||
Nonbinding site-directed mutants of transferrin binding protein B enhances their immunogenicity and protective capabilities.,Frandoloso R, Martinez-Martinez S, Calmettes C, Fegan J, Costa E, Curran D, Yu RH, Gutierrez-Martin CB, Rodriguez Ferri EF, Moraes TF, Schryvers AB Infect Immun. 2014 Dec 29. pii: IAI.02572-14. PMID:25547790<ref>PMID:25547790</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4o49" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transferrin-binding protein|Transferrin-binding protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Actinobacillus pleuropneumoniae]] | |||
[[Category: Large Structures]] | |||
[[Category: Calmettes C]] | |||
[[Category: Moraes TF]] | |||
[[Category: Schryvers AB]] | |||
[[Category: Yu RH]] | |||
Latest revision as of 06:21, 21 November 2024
Crystal structure of the vaccine antigen Transferrin Binding Protein B (TbpB) mutant Tyr-174-Ala from Actinobacillus pleuropneumoniae H87Crystal structure of the vaccine antigen Transferrin Binding Protein B (TbpB) mutant Tyr-174-Ala from Actinobacillus pleuropneumoniae H87
Structural highlights
Publication Abstract from PubMedHost adapted Gram-negative bacterial pathogens from the Pasteurellaceae, Neisseriaceae and Moraxellaceae families normally reside in the upper respiratory or genitourinary tracts of their hosts and rely on utilizing iron from host transferrin (Tf) for growth and survival. The surface receptor proteins that mediate this critical iron acquisition pathway have been proposed as ideal vaccine targets due to the critical role that they play in survival and disease pathogenesis in vivo. In particular, the surface lipoprotein component of the receptor, Tf binding protein B (TbpB), had received considerable attention as a potential antigen for vaccines in humans and food production animals but this has not translated into the series of successful vaccine products originally envisioned. Preliminary immunization experiments suggesting that host Tf could interfere with development of the immune response prompted us to directly address this question with site-directed mutant proteins defective in binding Tf. Site-directed mutants with dramatically reduced binding of porcine transferrin and nearly identical structure to the native proteins were prepared. A mutant Haemophilus parasuis TbpB was shown to induce an enhanced B-cell and T-cell response in pigs relative to native TbpB and provide superior protection from infection than the native TbpB or a commercial vaccine product. The results indicate that binding of host transferrin modulates the development of the immune response against TbpBs and that strategies designed to reduce or eliminate binding can be used to generate superior antigens for vaccines. Nonbinding site-directed mutants of transferrin binding protein B enhances their immunogenicity and protective capabilities.,Frandoloso R, Martinez-Martinez S, Calmettes C, Fegan J, Costa E, Curran D, Yu RH, Gutierrez-Martin CB, Rodriguez Ferri EF, Moraes TF, Schryvers AB Infect Immun. 2014 Dec 29. pii: IAI.02572-14. PMID:25547790[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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