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Please use this identifier to cite or link to this item: http://bura.brunel.ac.uk/handle/2438/4269

Title: Homology modelling of transferrin-binding protein A from Neisseria meningitidis
Authors: Oakhill, JS
Gorringe, AR
Sutton, BJ
Evans, RW
Keywords: Iron
Meningococcal
TbpA
Transferrin
Publication Date: 2005
Publisher: Oxford University Press
Citation: Protein Engineering, Design & Selection. 18 (5) 221–228
Abstract: Neisseria meningitidis, a causative agent of bacterial meningitis, obtains transferrin-bound iron by expressing two outer membrane located transferrin-binding proteins, TbpA and TbpB. TbpA is thought to be an integral outer membrane pore that facilitates iron uptake. Evidence suggests that TbpA is a useful antigen for inclusion in a vaccine effective against meningococcal disease, hence the identification of regions involved in ligand binding is of paramount importance to design strategies to block uptake of iron. The protein shares sequence and functional similarities to the Escherichia coli siderophore receptors FepA and FhuA, whose structures have been determined. These receptors are composed of two domains, a 22-stranded b-barrel and an N-terminal plug region that sits within the barrel and occludes the transmembrane pore. A three-dimensional TbpA model was constructed using FepA and FhuA structural templates, hydrophobicity analysis and homology modelling. TbpA was found to possess a similar architecture to the siderophore receptors. In addition to providing insights into the highly immunogenic nature of TbpA and allowing the prediction of potentially important ligandbinding epitopes, the model also reveals a narrow channel through its entire length. The relevance of this channel and the spatial arrangement of external loops, to the mechanism of iron translocation employed by TbpA is discussed.
URI: http://bura.brunel.ac.uk/handle/2438/4269
Appears in Collections:School of Health Sciences and Social Care Research Papers
Biosciences

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