Profile

Career

Publications

Selected publications

Publications 2000 - present

2011

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).

2010

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

2009

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

2008

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.

2007

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.

2006

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

2005

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)

2004

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

2003

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

2001

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.

2000

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.

External activities

Memberships

• Biochemical Society, Member of Theme Panel II, Molecular Structure and Function
• BBSRC Research Committee D

Research

Overview

Key research interests

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.

Two references

• Norris, N.C., Bingham, R.J., Harris, G., Speakman, A., Jones, R.P.O., Leech, A.P, Turkenburg, J.P. and Potts, J.R. (2011) Analysis of the tandem β-zipper interaction of a bacterial protein with human fibronectin J. Biol. Chem. 286, 38311-38320 (Paper of the Week)


• 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. (2010) 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

Current projects

• Structure and folding of proteins with identical tandemly arrayed domains. (BBSRC)
• Investigating protein-mediated staphylococcal biofilm formation (MRC).
• Exploiting bacterial proteins in the development of new therapeutics for the reduction of pathological vascular remodelling. (BHF)
• Structural studies of protein complexes involved in platelet activation, infective endocarditis and fibrinolysis (BHF)
• Structure and Function of an FnBPA domain implicated in MRSA biofilm formation (BHF studentship)

Research group(s)

Available PhD research projects

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.