Rob Delahay

Contact

• workRoom B88, Molecular Bacteriology Centre for Biomolecular Sciences
  University Park
  Nottingham
  NG7 2RD
  UK
• work0115 823 1095
• rob.delahay@nottingham.ac.uk

Research Summary

Numerous bacterial pathogens employ specialized secretion systems to interact with and modify the host cellular environment. Our research is focused on the functional characterisation of two such… read more

Recent Publications

• TEGTMEYER, NICOLE, HARTIG, ROLAND, DELAHAY, ROBIN M, ROHDE, MANFRED, BRANDT, SABINE, CONRADI, JENS, TAKAHASHI, SEIICHIRO, SMOLKA, ADAM J, SEWALD, NORBERT and BACKERT, STEFFEN, 2010. A small fibronectin-mimicking protein from bacteria induces cell spreading and focal adhesion formation. The Journal of biological chemistry. 285(30), 23515-26
• DELAHAY, R.M AND LETLEY D.P., 2009. The role of secreted proteins in the pathogenesis of H. pylori infection.. In: K. WOOLDRIDGE, ed., Bacterial Secreted Proteins: Secretory Mechanisms and Role in Pathogenesis Caister Academic Press. 366-400
• DELAHAY, R.M, BALKWILL, G.D, BUNTING, K.A, EDWARDS, W, ATHERTON, J.C and AND SEARLE, M.S., 2008. The highly repetitive region of the Helicobacter pylori CagY protein comprises tandem arrays of an alpha-helical repeat module. Journal Molecular Biology. 377(3), 956-71
• DELAHAY, R.M. AND ATHERTON, J.C., 2007. Sequence motifs within the extensive repetitive mid-region of the Helicobacter pylori CagY protein are conserved and broadly discriminate strain subsets Zoonoses and Public Health. 54, 66-67

• View all publications

Current Research

Numerous bacterial pathogens employ specialized secretion systems to interact with and modify the host cellular environment. Our research is focused on the functional characterisation of two such secretion systems; the type III secretion system (T3SS) of the pediatric diarrheal pathogen enteropathogenic Escherichia coli (EPEC), and two functionally disparate type IV secretion systems (T4SS) of the gastric pathogen Helicobacter pylori. Working within the Centre for Biomolecular Sciences (CBS) building (http://www.nottingham.ac.uk/cbs/index.aspx), we use an extensive array of molecular and protein biochemical techniques, together with in vitro models of infection, epifluorescence microscopy and comprehensive bioinformatics analyses. Our main projects aim to dissect key stages in the host-pathogen interaction by characterisation of major bacterial virulence determinants which promote successful host colonisation and predispose towards disease.

Projects presently include:

• Characterisation of protein components of the surface filament structure of the cag pathogenicity island encoded-T4SS of H. pylori

• Functional characterisation of a novel T4SS associated with the most severe disease outcomes of H. pylori infection (gastric cancer and duodenal ulcer)

• Development of novel protein transfection technology for the study of bacterial effector protein function.

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Grant funding

• MRC
• University of Nottingham.

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Group members

• Dr Jane Grove
• Nicola Croxall
• Amin Jalili
• Maher Alandiyjany.

Informal enquiries from overseas students regarding self-funded postgraduate (PhD) study within the group are welcome at any time.

• TEGTMEYER, NICOLE, HARTIG, ROLAND, DELAHAY, ROBIN M, ROHDE, MANFRED, BRANDT, SABINE, CONRADI, JENS, TAKAHASHI, SEIICHIRO, SMOLKA, ADAM J, SEWALD, NORBERT and BACKERT, STEFFEN, 2010. A small fibronectin-mimicking protein from bacteria induces cell spreading and focal adhesion formation. The Journal of biological chemistry. 285(30), 23515-26
• DELAHAY, R.M AND LETLEY D.P., 2009. The role of secreted proteins in the pathogenesis of H. pylori infection.. In: K. WOOLDRIDGE, ed., Bacterial Secreted Proteins: Secretory Mechanisms and Role in Pathogenesis Caister Academic Press. 366-400
• DELAHAY, R.M, BALKWILL, G.D, BUNTING, K.A, EDWARDS, W, ATHERTON, J.C and AND SEARLE, M.S., 2008. The highly repetitive region of the Helicobacter pylori CagY protein comprises tandem arrays of an alpha-helical repeat module. Journal Molecular Biology. 377(3), 956-71
• DELAHAY, R.M. AND ATHERTON, J.C., 2007. Sequence motifs within the extensive repetitive mid-region of the Helicobacter pylori CagY protein are conserved and broadly discriminate strain subsets Zoonoses and Public Health. 54, 66-67
• CREASEY, E.A., DELAHAY, R.M., BISHOP, A.A., SHAW, R.K., KENNY, B., KNUTTON, S. and FRANKEL, G., 2003. CesT is a bivalent enteropathogenic <i>Escherichia coli</i> chaperone required for translocation of both Tir and Map. Molecular Microbiology. 47(1), 209-221
• CREASEY, E.A., DELAHAY, R.M., DANIELL, S.J. and FRANKEL, G., 2003. Yeast two-hybrid system survey of interactions between LEE-encoded proteins of enteropathogenic <i>Escherichia coli</i> Microbiology. 149(8), 2093-2106
• DELAHAY, R.M., SHAW, R.K, ELLIOTT S.J, KAPER, J.B, KNUTTON, S. and FRANKEL, G., 2002. Functional analysis of the enteropathogenic <i>Escherichia coli</i> type III secretion system chaperone CesT identifies domains that mediate substrate interactions. Molecular Microbiology. 43(1), 61-73
• DELAHAY, R. M. and FRANKEL, G., 2002. Coiled-coil proteins associated with type III secretion systems: a versatile domain revisited Molecular Microbiology. VOL 45(PART 4), 905-916
• DANIELL, S.J., DELAHAY, R.M., SHAW, R.K., HARTLAND, E.L., PALLEN, M.J., BOOY, F., EBEL, F., KNUTTON, S. and FRANKEL, G., 2001. Coiled-coil domain of enteropathogenic <i>Escherichia coli </i>type III secreted protein EspD is involved in EspA filament-mediated cell attachment and hemolysis Infection and Immunity. 69(6), 4055-4064
• DELAHAY, R.M, FRANKEL, G and AND KNUTTON, S., 2001. Intimate interactions of enteropathogenic Escherichia coli at the host cell surface. Current Opinion in Infectious Diseases. 14(5), 559-65
• JENKINS, C, CHART, H, SMITH, H.R, HARTLAND, E.L, BATCHELOR, M, DELAHAY, R.M, DOUGAN, G and AND FRANKEL, G., 2000. Antibody response of patients infected with verocytotoxin-producing Escherichia coli to protein antigens encoded on the LEE locus. Journal of Medical Microbiology. 49(1), 97-101
• SPERANDIO, V, MELLIES, J.L, DELAHAY, R.M, FRANKEL, G, CRAWFORD, J.A, NGUYEN, W and AND KAPER, J.B., 2000. Activation of enteropathogenic Escherichia coli (EPEC) LEE2 and LEE3 operons by Ler. Molecular Microbiology. 38(4), 781-93
• HARTLAND, E.L, DANIELL, S.J, DELAHAY, R.M, NEVES, B.C, WALLIS, T, SHAW, R.K, HALE, C, KNUTTON, S and AND FRANKEL, G., 2000. The type III protein translocation system of enteropathogenic Escherichia coli involves EspA-EspB protein interactions. Molecular Microbiology. 35(6), 1483-92
• HERRMANN, J.L, DELAHAY, R, GALLAGHER, A, ROBERTSON, B and AND YOUNG, D., 2000. Analysis of post-translational modification of mycobacterial proteins using a cassette expression system. FEBS Letters. 473(3), 358-62
• HARTLAND, E., BATCHELOR, M., DELAHAY, R., HALE, C., MATTHEWS, S., DOUGAN, G., KNUTTON, S., CONNERTON, I.F. and FRANKEL, G., 1999. Binding of intimin from enterophathogenic<i> Escherichia coli</i> to Tir and to host cells Molecular Microbiology. 32, 151-158
• FRANKEL, G, WREN, B, DOUGAN, G, DELAHAY, R.M, BATCHELOR, M, HALE, C, HARTLAND, E.L, PALLEN, M.J, ROSENSHINE, I and AND KNUTTON, S., 1999. Host/pathogen interactions during infection by enteropathogenic Escherichia coli: A role for signalling.. In: R. ENGLAND, G. HOBBS, N. BAINTON, D. MCL. ROBERTS, ed., Microbial Signalling and Communication Cambridge University Press.
• DELAHAY, R.M, KNUTTON, S, SHAW, R.K, HARTLAND, E.L, PALLEN, M.J and AND FRANKEL, G., 1999. The coiled-coil domain of EspA is essential for the assembly of the type III secretion translocon on the surface of enteropathogenic Escherichia coli. Journal of Biological Chemistry. 274(50), 35969-74
• MCKEAN, P.G, DELAHAY, R, PIMENTA, P.F and AND SMITH, D.F., 1997. Characterisation of a second protein encoded by the differentially regulated LmcDNA16 gene family of Leishmania major. Molecular and Biochemical Parasitology. 85(2), 221-31
• DELAHAY, R.M, ROBERTSON, B.D, BALTHAZAR, J.T, SHAFER, W.M and AND ISON, C.A., 1997. Involvement of the gonococcal MtrE protein in the resistance of Neisseria gonorrhoeae to toxic hydrophobic agents. Microbiology. 143 ( Pt 7), 2127-33