Biography
- BA, University of Oxford, 1988
- DPhil, University of Oxford, 1991
- Post-doctoral fellow, Ontario Cancer Institute and University of Toronto, 1992-1999
- Lecturer-Senior Lecturer/Senior Tutor, University of Bath,1999 to date
Dr Stefan Bagby
Profile
Current Research
Our research concerns the structure and function of proteins involved in organ size control and stem cell self-maintenance, memory and bacterial infections. We use a combination of multidimensional heteronuclear NMR spectroscopy, X-ray crystallography and other biophysical techniques and biochemical and molecular biology methods to provide novel information on protein structure, dynamics and energetics.
Organ size control and stem cell self-maintenance
The Hippo pathway is a core conserved signalling pathway and central mechanism of organ size regulation, spatial patterning, regulation of early embryo development, homeostasis, and stem cell self-renewal and differentiation. We study the structures and interactions of numerous proteins involved in this pathway and collaborate with Drosophila and fish researchers to combine in vitro with in vivo studies.
Memory
Understanding the complex mechanisms by which memories are acquired, maintained and recalled is a neuroscience holy grail. KIBRA is a postsynaptic density protein important for memory. We study the structures and interactions of KIBRA. By combining data from these molecular studies with our collaborator's cellular and in vivo data, we aim to achieve detailed understanding of KIBRA function at the postsynaptic site.
Bacterial infections
We aim to provide new insights into bacterial pathogenesis through studies of the structure and function of bacterial pathogen proteins and of their complexes with host cell target proteins. Current projects focus on proteins from Burkholderia pseudomallei and Staphylococcus aureus.
Graphene-biomolecule interactions
We are studying biomolecular interactions with graphene as the basis for new nano-devices.
Publications
Posner, M. G., Upadhyay, A., Crennell, S., Watson, A. J. A., Dorus, S., Danson, M. J. and Bagby, S., 2013. Post-translational modification in the archaea: structural characterization of multi-enzyme complex lipoylation. Biochemical Journal, 449 (2), pp. 415-425.
Bagby, S., 2013. J coupling. In: Roberts, G. C. K., ed. Encyclopedia of Biophysics. Springer Science and Business Media.
Cherrett, C., Furutani-Seiki, M. and Bagby, S., 2012. The Hippo pathway : key interaction and catalytic domains in organ growth control, stem cell self-renewal and tissue regeneration. Essays in Biochemistry, 53, pp. 111-127.
Webb, C., Upadhyay, A., Giuntini, F., Eggleston, I., Furutani-Seiki, M., Ishima, R. and Bagby, S., 2011. Structural features and ligand binding properties of tandem WW domains from YAP and TAZ, nuclear effectors of the Hippo pathway. Biochemistry, 50 (16), pp. 3300-3309.
Clark, E. A., Crennell, S., Upadhyay, A., Zozulya, A. V., Mackay, J. D., Svergun, D. I., Bagby, S. and van den Elsen, J. M. H., 2011. A structural basis for Staphylococcal complement subversion : X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3d. Molecular Immunology, 48 (4), pp. 452-462.
Alshammari, A., Posner, M., Jones, G., Upadhyay, A., Bagby, S., Ilie, A. and Estrela, P., 2011. Graphene-based amperometric and field-effect biosensing with supramolecular protein complexes. In: Electrochem 2011, 2011-09-05 - 2011-09-06, Bath.
Jones, R. T., Sanchez-Contreras, M., Vlisidou, I., Amos, M. R., Yang, G., Munoz-Berbel, X., Upadhyay, A., Potter, U. J., Joyce, S. A., Ciche, T. A., Jenkins, A. T. A., Bagby, S., ffrench-Constant, R. H. and Waterfield, N. R., 2010. Photorhabdus adhesion modification protein (Pam) binds extracellular polysaccharide and alters bacterial attachment. BMC Microbiology, 10, 141.
Isenman, D. E., Leung, E., Mackay, J. D., Bagby, S. and van den Elsen, J. M. H., 2010. Mutational analyses reveal that the staphylococcal immune evasion molecule Sbi and complement receptor 2 (CR2) share overlapping contact residues on C3d: implications for the controversy regarding the CR2/C3d cocrystal structure. The Journal of Immunology, 184 (4), pp. 1946-1955.
Posner, M. G., Upadhyay, A., Bagby, S., Hough, D. W. and Danson, M. J., 2009. A unique lipoylation system in the Archaea: lipoylation in Thermoplasma acidophilum requires two proteins. FEBS Journal, 276 (15), pp. 4012-4022.
Clark, E., Upadhyay, A., Bagby, S. and van den Elsen, J., 2009. IsaB, a new immunoglobulin-binding protein from Staphylococcus aureus. Molecular Immunology, 46 (14), pp. 2834-2835.
Isenman, D. E., Leung, E., Mackay, J. D., Bagby, S. and van den Elsen, J. M. H., 2008. Mutational analyses reveal that the staphylococcal immune evasion molecule Sbi and complement eeceptor 2 (CR2) share overlapping contact residues on C3d: Implications for the controversy regarding the CR2/C3d cocrystal structure. Molecular Immunology, 45 (16), pp. 4095-4096.
Upadhyay, A., Burman, J. D., Clark, E. A., Leung, E., Isenman, D. E., van den Elsen, J. M. H. and Bagby, S., 2008. Structure-function analysis of the C3 binding region of Staphylococcus aureus immune subversion protein Sbi. Journal of Biological Chemistry, 283 (32), pp. 22113-22120.
Burman, J. D., Leung, E., Atkins, K. L., O'Seaghdha, M. N., Lango, L., Bernado, P., Bagby, S., Svergun, D. I., Foster, T. J., Isenman, D. E. and van den Elsen, J. M. H., 2008. Interaction of human complement with Sbi, a staphylococcal immunoglobulin-binding protein: indications of a novel mechanism of complement evasion by Staphylococcus aureus. Journal of Biological Chemistry, 283 (25), pp. 17579-17593.
Upadhyay, A., Wu, H.-L., Williams, C., Field, T., Galyov, E. E., van den Elsen, J. M. H. and Bagby, S., 2008. The guanine-nucleotide-exchange factor BopE from Burkholderia pseudomallei adopts a compact version of the Salmonella SopE/SopE2 fold and undergoes a closed-to-open conformational change upon interaction with Cdc42. Biochemical Journal, 411 (3), pp. 485-493.
Atkins, K. L., Burman, J. D., Chamberlain, E. S., Cooper, J. E., Poutrel, B., Bagby, S., Jenkins, T. A., Feil, E. J. and van den Elsen, J. M. H., 2008. S. aureus IgG-binding proteins SpA and Sbi: host specificity and mechanisms of immune complex formation. Molecular Immunology, 45 (6), pp. 1600-1611.
van den Elsen, J., Upadhyay, A., Burman, J., Leung, E., Clark, E., Isenman, D. and Bagby, S., 2008. Structure–function analysis of the novel Staphylococcus aureus immune subversion protein Sbi. Molecular Immunology, 45 (16), p. 4119.
