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
  • 2008-2010 Royal Society University Research Fellow and Project Leader. JIC and University of East Anglia
  • 2010-present Project Leader, JIC

Mark Banfield

Project Leader

Biological Chemistry

Contact details

mark.banfield@jic.ac.uk

Research interests

Research theme: Structural biology and biochemistry 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 group mostly works on proteins from plant pathogens (and their hosts), but retains interests in mammalian host/pathogen systems. We also investigate the molecular basis of host cell adhesion mediated by internal thioester bonds, highly unusual protein cross-links we discovered in pili from gram-positive pathogens.

We greatly benefit from close collaboration with research groups at The Sainsbury Laboratory, on-site at the the John Innes Centre.

In plants, effector proteins can not only have a virulence function (to promote 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 and is a major target for both the breeding and engineering of disease resistance in important crop plants. We use a wide range of experimental approaches to investigate the activity and significance of effector proteins in the outcome of host/pathogen interactions. These approaches include protein structure determination by X-ray crystallography, a variety of other biophysical techniques appropriate to answering relevant biological questions, biochemistry, protein interaction studies (e.g. Y2H and co-IP) and in planta expression of proteins to assess phenotypes/activities.

For further details of past and present activities, group members, facilities, publications, funding etc. please take a look at our Lab website.

Follow on Twitter for up to date news, job opportunities and opinions (my own not JIC's): @mjbanfield

Current Funding

BBSRC     FEBS     Gatsby     Royal Society

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 (4) 483-492
DOI:10.1016/j.pbi.2012.03.008
Crow A., Hughes R. K., Taieb F., Oswald E., Banfield M. J. (2012)
The molecular basis of ubiquitin-like protein NEDD8 deamidation by the bacterial effector protein Cif
Proceedings of the National Academy of Sciences of the United States of America 109 (27) E1830-E1838
DOI:10.1073/pnas.1112107109
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 25 (8) 1118-1131
DOI:10.1094/MPMI-12-11-0323
Sohn K. H., Hughes R. K., Piquerez S. J., Jones J. D., Banfield M. J. (2012)
Distinct regions of the Pseudomonas syringae coiled-coil effector AvrRps4 are required for activation of immunity.
Proceedings of the National Academy of Sciences of the United States of America 109 (40) 16371-16376
DOI:10.1073/pnas.1212332109
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
Wirthmueller L., Banfield M. J. (2012)
mADP-RTs: versatile virulence factors from bacterial pathogens of plants and mammals
Frontiers in Plant Science 3 142
DOI:DOI: 10.3389/fpls.2012.00142
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