Conserved Interaction between Transferrin and Transferrin-binding Proteins from Porcine Pathogens

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dc.contributor.authorSilva, Leslie P.
dc.contributor.authorYu, Ronghua
dc.contributor.authorCalmettes, Charles
dc.contributor.authorYang, Xue
dc.contributor.authorMoraes, Trevor F.
dc.contributor.authorSchryvers, Anthony B.
dc.contributor.authorSchriemer, David C.
dc.date.accessioned2017-08-17T19:23:12Z
dc.date.available2017-08-17T19:23:12Z
dc.date.issued2011-06-17
dc.description.abstractGram-negative porcine pathogens from the Pasteurellaceae family possess a surface receptor complex capable of acquiring iron from porcine transferrin (pTf). This receptor consists of transferrin-binding protein A (TbpA), a transmembrane iron transporter, and TbpB, a surface-exposed lipoprotein. Questions remain as to how the receptor complex engages pTf in such a way that iron is positioned for release, and whether divergent strains present distinct recognition sites on Tf. In this study, the TbpB-pTf interface was mapped using a combination of mass shift analysis and molecular docking simulations, localizing binding uniquely to the pTf C lobe for multiple divergent strains of Actinobacillus plueropneumoniae and suis. The interface was further characterized and validated with site-directed mutagenesis. Although targeting a common lobe, variants differ in preference for the two sublobes comprising the iron coordination site. Sublobes C1 and C2 participate in high affinity binding, but sublobe C1 contributes in a minor fashion to the overall affinity. Further, the TbpB-pTf complex does not release iron independent of other mediators, based on competitive iron binding studies. Together, our findings support a model whereby TbpB efficiently captures and presents iron-loaded pTf to other elements of the uptake pathway, even under low iron conditions.en_US
dc.description.refereedYesen_US
dc.description.sponsorshipThis work was supported by the Canadian Foundation for Innovation, the Canada Research Chair program, the Alberta Heritage Foundation for Medical Research, and the Canadian Institutes of Health Research.en_US
dc.identifier.citationSilva, L. P., Yu, R., Calmettes, C., Yang, X., Moraes, T. F., Schryvers, A. B., & Schriemer, D. C. (2011). Conserved interaction between transferrin and transferrin-binding proteins from porcine pathogens. Journal of Biological Chemistry, 286(24), 21353-21360. doi:10.1074/jbc.M111.226449en_US
dc.identifier.doi10.1074/jbc.M111.226449
dc.identifier.doihttp://dx.doi.org/10.11575/PRISM/33786
dc.identifier.urihttp://hdl.handle.net/1880/52192
dc.language.isoenen_US
dc.publisherJournal of Biological Chemistryen_US
dc.publisher.departmentBiochemistry and Molecular Biology; Immunology, and Infectious Diseasesen_US
dc.publisher.facultyFaculty of Medicineen_US
dc.publisher.institutionUniversity of Calgaryen_US
dc.publisher.urlhttp://www.jbc.org/en_US
dc.subjectBacterial Metabolismen_US
dc.subjectIronen_US
dc.subjectMass Spectrometry (MS)en_US
dc.subjectProtein-Protein Interactionsen_US
dc.subjectReceptorsen_US
dc.subjectMass Shift Analysisen_US
dc.subjectTransferrinen_US
dc.titleConserved Interaction between Transferrin and Transferrin-binding Proteins from Porcine Pathogensen_US
dc.typejournal article
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