John Innes Centre

Dr Mark Banfield

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Curriculum Vitae

  • 1994 BSc (Hons.) Biochemistry. University of Sheffield
  • 1997 PhD. University of Bristol
  • 1997-1999 PDRA. University of Bristol
  • 1999-2000 Traveling fellow. Auckland University, New Zealand
  • 2000-2002 PDRA. University of Bristol
  • 2002-2003 Royal Society University Research Fellow. University of Bristol
  • 2003-2008 Royal Society University Research Fellow and Lecturer. Newcastle University
  • 2008-present Royal Society University Research Fellow and Project Leader. JIC and University of East Anglia

Mark Banfield

Project Leader

Biological Chemistry

Contact details

mark.banfield@jic.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

Bozkurt T. O., Schornack S., Banfield M. J., Kamoun S. (2012)
Oomycetes, effectors, and all that jazz
Current Opinion in Plant Biology 15 1-10
DOI:10.1016/j.pbi.2012.03.008
Giacomelli L., Nanni V., Lenzi L., Zhuang J., Dalla Serra M., Banfield M. J., Town C. D., Silverstein K. A., Baraldi E., Moser C. (2012)
Identification and characterization of the defensin-like gene family of grapevine
Molecular Plant-Microbe Interactions
DOI:10.1094/MPMI-12-11-0323
Win J., Krasileva K. V., Kamoun S., Shirasu K., Staskawicz B. J., Banfield M. J. (2012)
Sequence divergent RXLR effectors share a structural fold conserved across plant pathogenic oomycete species
PLoS Pathogens 8 (1) e1002400
DOI:10.1371/journal.ppat.1002400
Win J., Krasileva K. V., Kamoun S., Shirasu K., Staskawicz B. J., Banfield M. J. (2012)
Sequence divergent RXLR effectors share a structural fold conserved across plant pathogenic Oomycete species
PLoS Pathogens 8 (1) e1002400
DOI:10.1371/journal.ppat.1002400
Boutemy L. S., King S. R., Win J., Hughes R. K., Clarke T. A., Blumenschein T. M., Kamoun S., Banfield M. J. (2011)
Structures of Phytophthora RXLR effector proteins: a conserved but adaptable fold underpins functional diversity
Journal of Biological Chemistry 286 (41) 35834-35842
DOI:10.1074/jbc.M111.262303
Boutemy L. S., King S. R., Win J., Hughes R. K., Clarke T. A., Blumenschein T. M., Kamoun S., Banfield M. J. (2011)
Structures of Phytophthora RXLR effector proteins: A conserved but adaptable fold underpins functional diversity
Journal of Biological Chemistry 286 (41) 35834-35842
DOI:10.1074/jbc.M111.262303
Wirthmueller L., Jones J. D., Banfield M. J. (2011)
Crystallization and preliminary X-ray analysis of the RXLR-type effector RXLR3 from the oomycete pathogen Hyaloperonospora arabidopsis
Acta Crystallographica F67 1417-1420
Badarau A., Firbank S. J., McCarthy A., Banfield M. J., Dennison C. (2010)
Visualizing the metal-binding versatility of copper trafficking sites
Biochemistry 49 (36) 7798-7810
Li C., Sato K., Monari S., Salard I., Sola M., Banfield M. J., Dennison C. (2010)
Metal-binding loop length is a determinant of the pKa of a histidine ligand at a type 1 copper site
Inorganic Chemistry 50 482-488
DOI:10.1021/ic101413e
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 285 (44) 33858-33866
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) 4651-4659
DOI:10.1128/JB.00071-10