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Structural Variations within the Transferrin Binding Site on Transferrin-binding Protein B, TbpB

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Author
Calmettes, Charles
Yu, Rong-hua
Silva, Leslie P.
Curran, Dave
Schriemer, David C.
Schryvers, Anthony B.
Moraes, Trevor F.
Accessioned
2017-08-17T16:25:23Z
Available
2017-08-17T16:25:23Z
Issued
2011-04-08
Subject
Bacteria
Cell Surface Protein
Iron
Protein Structure
X-ray Crystallography
Bacterial Lipoprotein
Bacterial Transferrin Receptor
Iron Acquisition
Vaccine Candidate
Membrane Protein
Type
journal article
Metadata
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Abstract
Pathogenic bacteria acquire the essential element iron through specialized uptake pathways that are necessary in the iron-limiting environments of the host. Members of the Gram-negative Neisseriaceae and Pasteurellaceae families have adapted to acquire iron from the host iron binding glycoprotein, transferrin (Tf), through a receptor complex comprised of transferring-binding protein (Tbp) A and B. Because of the critical role they play in the host, these surface-exposed proteins are invariably present in clinical isolates and thus are considered prime vaccine targets. The specific interactions between TbpB and Tf are essential and ultimately might be exploited to create a broad-spectrum vaccine. In this study, we report the structure of TbpBs from two porcine pathogens, Actinobacillus pleuropneumoniae and suis. Paradoxically, despite a common Tf target, these swine related TbpBs show substantial sequence variation in their Tf-binding site. The TbpB structures, supported by docking simulations, surface plasmon resonance and hydrogen/deuterium exchange experiments with wild-type and mutant TbpBs, explain why there are structurally conserved elements within TbpB homologs despite major sequence variation that are required for binding Tf.
Grantingagency
Canadian Foundation for Innovation (CFI), Alberta Heritage Foundation for Medical Research (AHFMR), and Canadian Institutes of Health Research (CIHR).
Refereed
Yes
Sponsorship
We thank members of Canadian Light Source (CLS) beamline staff at CMCF-08ID-1 for assistance with data collection and members of the Moraes and Schryvers laboratories for valuable discussion.
Citation
Calmettes, C., Yu, R., Silva, L. P., Curran, D., Schriemer, D. C., Schryvers, A. B., & Moraes, T. F. (2011). Structural variations within the transferrin binding site on transferrin-binding protein B, TbpB. Journal of Biological Chemistry, 286(14), 12683-12692. doi:10.1074/jbc.M110.206102
Department
Department of Biology
Institution
University of Toronto
Url
http://www.jbc.org/
Publisher
Journal of Biological Chemistry
Doi
http://dx.doi.org/10.1074/jbc.M110.206102
http://dx.doi.org/10.11575/PRISM/33875
Uri
http://hdl.handle.net/1880/52191
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