4o4x

Crystal structure of the vaccine antigen Transferrin Binding Protein B (TbpB) double mutant Tyr-167-Ala and Trp-176-Ala from Haemophilus parasuis Hp5

spinqualitylabelsall models 4o4x, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4o4x is a 2 chain structure with sequence from Glaesserella parasuis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: GOL, NA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2UKY6_GLAPU 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transferrin-binding protein

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