|2012 -||Professor and Chair of Molecular Biophysics||Department of Biology|
|2005 -||Anniversary Reader.
British Heart Foundation Senior Basic Science Research Fellow
|Departments of Biology and Chemistry, University of York|
|2002 - 2005||BHF Basic Science Lecturer||Department of Biochemistry, University of Oxford|
|1997 - 2002||Research Associate||Department of Biochemistry, University of Oxford|
|1992 - 1996||Postdoctoral Fellow||Department of Biochemistry, University of Oxford|
|1992||PhD||University of Sydney|
|1987||BSc||University of Sydney|
Norris, N.C., Bingham, R.J., Harris, G., Speakman, A., Jones, R.P.O., Leech, A.P, Turkenburg, J.P. and Potts, J.R.* Analysis of the tandem β-zipper interaction of a bacterial protein with human fibronectin J. Biol. Chem. 286. 31311-38320 (2011), Paper of the Week
Marjenberg, Z.R. Ellis, I.R., Hagan, R.M., Prabhakaran, S., Hook, M., Talay, S.R., Potts, J.R., Staunton, D., & Schwarz-Linek, U. J. Biol. Chem. 286, 1884-1894 (2011).
Atkin, K. E., Brentnall, A.S., Harris, G., Bingham, R.J., Erat, M., Millard, C.J., Schwarz-Linek, U., Staunton, D, Vakonakis, I., Campbell, I.D., and Potts, J.R*. The streptococcal binding site in the gelatine-binding domain of fibronectin is consistent with a non-linear arrangement of modules. J. Biol. Chem. 285, 36977-36983 (2010)
Geoghegan, J.A., Corrigan, R.M., Gruszka, D.T., Speziale, P., O’Gara, J.P., Potts, J.R., & Foster, T.J. (2010) Role of surface protein SasG in biofilm formation by Staphylococcus aureus. J. Bacteriol. 192, 5663-5673
Edwards, A.M., Potts, J.R., Josefsson, E. and Massey, R.C. (2010) PLoS Pathog. 6, e1000964 Staphylococcus aureus host cell invasion and virulence in sepsis is facilitated by the multiple repeats within FnBPA.
Bingham, R.J. & Potts, J.R.* (2010) Fibronectin structure: a new piece of the puzzle emerges. Structure 18, 660-661
Ellis, I.R, Jones, S.J., Staunton, D., Vakonakis, I., Norman, D.G., Potts, J.R., Milner, C.M., Meenan, N.A., Raibaud, S., Schor, A.M. & Schor, S.L. (2010) Multi-factorial modulation of IGD motogenic potential in MSF (Migration Stimulating Factor). Exp Cell Res. 316, 2465-2476
Horler, R.S., Muller, A., Williamson, D.C., Potts, J.R., Wilson, K.S., and Thomas, G.H. (2009) Furanose-specific sugar transport: Characterisation of a bacterial galactofuranose binding protein. J. Biol. Chem. 284, 31156-31163
Prabhakaran, S. Liang, X. Skare, J.T., Potts, J.R., & Höök, M. (2009) A novel fibronectin binding motif in MSCRAMMs targets F3 modules. PLoS One 4, e5412
Gloster, T.M. Turkenburg, J.P., Potts, J.R., Henrissat, B. & Davies, G.J. (2008) Divergence of catalytic mechanism within a glycosidase family provides insight into evolution of carbohydrate metabolism by human gut flora. Chem. Biol 15, 1058-1067
Bingham, R.J., Rudiño-Piñera, E., Meenan, N.A.G., Schwarz-Linek, U., Turkenburg, J.P., Höök, M., Garman, E.F., & Potts, J.R.* (2008) Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains. Proc. Natl Acad. Sci. USA 105, 12254-12258
Severi, E., Muller, A., Potts, J.R., Leech, A., Williamson, D., Wilson, K.S. & Thomas, G.H. (2008) Sialic acid mutarotation is catalysed by the Escherichia coli beta-propeller protein YjhT. J. Biol. Chem. 283, 4841-4849.
Meenan, N.A.G., Visai, L., Valtulina, V., Schwarz-Linek, U., Norris, N.C., Gurusidappa, s., Höök, M., Speziale, P., & Potts, J.R.* (2007) The tandem beta-zipper model defines high affinity fibronectin-binding repeats within Staphylococcus aureus FnBPA. J. Biol. Chem. 282, 25893-25902
Rudino-Pinera, E., Ravelli, R.B., Sheldrick, G.M., Nanao, M.H., Korostelev, V.V., Werner, J.M., Schwarz-Linek, U., Potts, J.R.*, & Garman, E.F. (2007) The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin--a tale with a twist. J. Mol. Biol. 368, 833-844.
Schwarz-Linek, U., Höök, M and Potts, J.R. (2006) Fibronectin-binding proteins of Gram-positive cocci.
Microbes. Infect. 8, 2291-2298
Pilka E.S., Werner, J.M., Schwarz-Linek, U., Pickford, A.R., Meenan, N.A.G. Campbell, I.D. & Potts, J.R.* (2006) Structural insight into binding of Staphylococcus aureus to human fibronectin. FEBS Lett. 580, 273-277
Raibaud, S., Schwarz-Linek, U., Kim, J.H., Jenkins, H.T., Baines, E.R., Gurusidappa, S., Hook, M, & Potts, J.R.* (2005) Borrelia burgdorferi binds fibronectin through a tandem beta zipper – a common mechanism of fibronectin-binding in staphylococci, streptococci and spirochetes. J. Biol. Chem. 280, 18803-18809
Dechamps, M.L., Pilka, E.S., Potts, J.R., Campbell, I.D., and Boyd, J. Probing protein-peptide binding surfaces using charged stable free radicals and transverse paramagnetic relaxation enhancement (PRE). J. Biomol. NMR 31, 155-160 (2005)
Kim, J.H., Singvall, J., Schwarz-Linek, U., Johnson, B.J.B., Potts, J.R., Höök, M. (2004) BBK32, a fibronectin-binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. J. Biol. Chem 279, 41706-14
Rudino-Pinera, E., Schwarz-Linek, U., Potts, J.R., & Garman, E.F. (2004) Twinned or not twinned, that is the question: crystallization and preliminary crystallographic analysis of the 2F13F1 module pair of human fibronectin. Acta Crystallogr. D 60, 1341-1345
Schwarz-Linek, U., Pilka, E.S. Pickford, A. Kim, J.H., Höök, M., Campbell, I.D., & Potts, J.R.* (2004) High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules. J. Biol. Chem. 279, 39017-39025
Schwarz-Linek, U., Höök, M and Potts, J.R. (2004) The Molecular Basis of Fibronectin-Mediated Bacterial Adherence to Host Cells. Mol. Microbiol. 52, 631-641
Brown, P.J., Mulvey, D., Potts, J.R., Tomley, F.M., and Campbell, I.D. (2003) Solution structure of a PAN module from the apicomplexan parasite Eimeria tenella. J. Struct. Funct. Genomics 4, 227-234
Schwarz-Linek, U., Werner, J.M., Pickford, A.R., Gurusiddappa, S., Kim, J.H., , Pilka, E.S., Briggs, J.A.G., Gough, T.S., Höök, M., Campbell, I.D., and Potts, J.R.* (2003) Pathogenic bacteria attach to human fibronectin through a tandem--zipper. Nature 423, 177-181
Schwarz-Linek, U., Plevin, M.J., Pickford, A.R., Höök, M., Campbell, I.D., & Potts, J.R.* (2001) Binding of a peptide from a Streptococcus dysgalactiae MSCRAMM to the N-terminal F1 module pair of human fibronectin involves both modules. FEBS Lett 497, 137-40.
Penkett, C.J., Dobson, C.M., Smith, L.J., Bright, J.R., Pickford, A.R., Campbell, I.D., & Potts, J.R.* (2000) Identification of residues involved in Staphylococcus aureus FnBP binding to the 4F15F1 module pair of human fibronectin using heteronuclear NMR spectroscopy. Biochemistry 39, 2887-2893
Bright, J.R. Pickford, A.R., Potts, J.R., & Campbell, I.D. (2000) Preparation of isotopically-labelled recombinant fragments of fibronectin for functional and structural study by heteronuclear magnetic resonance spectroscopy. Methods in Molecular Biology139: Extracellular matrix Protocols. Eds: Streuli, C. and Grant, M. Humana Press Inc.
In the early stages of infection, bacteria attach to host tissue. Interactions between host and bacterial proteins are also likely to play an important role in the maintenance and dissemination of infection. One aim of our research is to elucidate mechanisms of host-pathogen interactions. For example, the ability to bind the human protein fibronectin (Fn) is a characteristic that has been demonstrated for a number of pathogens. For Staphylococcus aureus, Fn-binding appears to play a role in infective endocarditis. S. aureus can also form difficult to eradicate aggregates, known as biofilms, on the surfaces of prosthetic devices such as mechanical heart valves. We are studying proteins involved in biofilm formation using techniques such as nuclear magnetic resonance spectroscopy, X-ray crystallography, isothermal titration calorimetry, surface plasmon resonance and multi-angle light scattering.
|Postdoctoral Research Associate||Kate Atkin|
|Postdoctoral Research Associate||Gemma Harris|
|Postdoctoral Research Associate||Richard Jones|
|Postdoctoral Research Associate||Vaclav Stemberk|
|PhD student||Andrew Brentnall|
|PhD student||Dominika Gruszka|
|PhD student||Adrian Speakman|
Structure determination of the fibrin/fibronectin complex involved in thrombosis and haemostasis (for 2012 -13)
Formation of blood clots is important for the prevention of blood loss and wound healing but, when they form in the wrong place, they can also be potentially life-threatening. So it is very important to understand the molecules involved in clot formation and, particularly, how they bind to each other. Fibronectin is a protein found in the plasma, during clot formation it binds to another protein fibrin, which is the main component of blood clots. We have studied the regions of these two proteins that interact and the affinity of the interaction. The aim of the current project is to solve the three-dimensional structure of the complex. The project is likely to involve recombinant protein expression and purification and a variety of biophysical techniques including NMR spectroscopy and X-ray crystallography. The aim of the work is to obtain a better understanding of clot formation.