Mark Banfield

Project Leader

Biological Chemistry

Contact details

mark.banfield@bbsrc.ac.uk

Research interests

Research theme: Structural biology of host:pathogen interactions

The Banfield group primarily investigates molecular interactions at the host:pathogen interface, with a particular focus on 'effector' proteins that are translocated into host cells during infection. These proteins interfere with host cell processes, presumably to the benefit of the pathogen. The Lab. works on proteins from both mammalian and plant pathogens (and their respective hosts). Our experimental method of choice is structure determination by X-ray crystallography, but we also use a wide variety of other biophysical techniques appropriate to answering relevant biological questions.

The work on plant pathogens greatly benefits from close collaboration with The Sainsbury Laboratory (www.tsl.ac.uk), on-site at the The John Innes Centre. In plants, effector proteins can not only have a 'virulence' function (promoting disease) but can also be specifically recognised within plant cells leading to localised cell death (so-called 'avirulence' function as it restricts pathogen growth). The latter function forms part of the plant innate immune system. We are using protein biochemistry and structural biology to further understanding of effector function/evolution in plant pathogens. We also contribute to other work on plant pathogenesis.

The research group also has interests in surface-presented virulence factors of Streptococcus pyogenes (group A streptococci) and understanding structural aspects of metal binding/trafficking in model systems.

Protein production/crystallisation

The Laboratory has good facilities for medium/high throughput in production of proteins for structural study (in E. coli - we are also engaging in work on in planta expression systems), and crystallisation. These include AKTA-XPress modules, liquid handling/crystallisation robotics and a crystal imaging system.

Current Funding

BBSRC, Gatsby Charitable Foundation, Royal Society, FEBS

Recent Publications

Badarau A., Firbank S. J., McCarthy A., Banfield M. J., Dennison C. (2010)
Visualizing the Metal-Binding Versatility of Copper Trafficking Sites
Biochemistry

Oliva R., Win J., Raffaele S., Boutemy L., Bozkurt T. O., Chaparro-Garcia A., Segretin M. E., Stam R., Schornack S., Cano L. M., van Damme M., Huitema E., Thines M., Banfield M. J., Kamoun S. (2010)
Recent developments in effector biology of filamentous plant pathogens
Cellular Microbiology 12 (7) 1015
DOI:10.1111/j.1462-5822.2010.01484.x

Pointon J. A., Smith W. D., Saalbach G., Crow A., Kehoe M. A., Banfield M. J. (2010)
A highly unusual thioester bond in a pilus adhesin is required for efficient host cell interaction
Journal of Biological Chemistry
DOI:10.1074/jbc.M110.149385

Smith W. D., Pointon J. A., Abbot E., Kang H. J., Baker E. N., Hirst B. H., Wilson J. A., Banfield M. J., Kehoe M. A. (2010)
Roles of minor pilin subunits Spy0125 and Spy0130 in the Serotype M1 Streptococcus pyogenes strain SF370
Journal of Bacteriology 192 (18)
DOI:10.1128/JB.00071-10

Crow A., Race P. R., Jubelin G., Varela Chavez C., Escoubas J. M., Oswald E., Banfield M. J. (2009)
Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei
PLoS ONE 4 (5) e5582
DOI:10.1371/journal.pone.0005582

Jubelin G., Chavez C. V., Taieb F., Banfield M. J., Samba-Louaka A., Nobe R., Nougayrède J. P., Zumbihl R., Givaudan A., Escoubas J. M., Oswald E. (2009)
Cycle inhibiting factors (CIFs) are a growing family of functional cyclomodulins present in invertebrate and mammal bacterial pathogens.
PLoS ONE 4 (3) e4855
DOI:10.1371/journal.pone.0004855

Race P. R., Bentley M. L., Melvin J. A., Crow A., Hughes R. K., Smith W. D., Sessions R. B., Kehoe M. A., McCafferty D. G., Banfield M. J. (2009)
Crystal structure of Streptococcus pyogenes sortase A: Implications for sortase mechanism
Journal of Biological Chemistry 284 (11) 6924-6933
DOI:10.1074/jbc.M805406200

Sato K., Li C., Salard I., Thompson A. J., Banfield M. J., Dennison C. (2009)
Metal-binding loop length and not sequence dictates structure.
Proceedings of the National Academy of Sciences USA 106 (14) 5616-5621
DOI:10.1073/pnas.0811324106

Solovyova A. S., Pointon J. A., Race P. R., Smith W. D., Kehoe M. A., Banfield M. J. (2009)
Solution structure of the major (Spy0128) and minor (Spy0125 and Spy0130) pili subunits from Streptococcus pyogenes
European Biophysics Journal E-pub
DOI:10.1007/s00249-009-0432-2

Badarau A., Firbank S. J., Waldron K. J., Yanagisawa S., Robinson N. J., Banfield M. J., Dennison C. (2008)
FutA2 is a ferric binding protein from Synechocystis PCC 6803.
Journal of Biological Chemistry 283 (18) 12520-7
DOI:10.1074/jbc.M709907200

Crowley P. B., Matias P. M., Mi H., Firbank S. J., Banfield M. J., Dennison C. (2008)
Regulation of protein function: crystal packing interfaces and conformational dimerization
Biochemistry 47 (25) 6583-6589
DOI:10.1021/bi800125h

Rath O., Park S., Tang H. H., Banfield M. J., Brady R. L., Lee Y. C., Dignam J. D., Sedivy J. M., Kolch W., Yeung K. C. (2008)
The RKIP (Raf-1 Kinase Inhibitor Protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK.
Cellular Signalling 20 (5) 935-41
DOI:10.1016/j.cellsig.2008.01.012

Sato K., Firbank S. J., Li C., Banfield M. J., Dennison C. (2008)
The importance of the long type 1 copper-binding loop of nitrite reductase for structure and function.
Chemistry 14 (19) 5820-8
DOI:10.1002/chem.200701997

Tottey S., Waldron K. J., Firbank S. J., Reale B., Bessant C., Sato K., Cheek T. R., Gray J., Banfield M. J., Dennison C., Robinson N. J. (2008)
Protein-folding location can regulate manganese-binding versus copper- or zinc-binding.
Nature 455 (7216) 1138-42
DOI:10.1038/nature07340

Yanagisawa S., Crowley P. B., Firbank S. J., Lawler A. T., Hunter D. M., McFarlane W., Li C., Kohzuma T., Banfield M. J., Dennison C. (2008)
Pi-interaction tuning of the active site properties of metalloproteins.
Journal of the American Chemical Society 130 (46) 15420-8
DOI:10.1021/ja8038135

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