Home| Professor of Mycobacteriology |
Contact details:
| Tel: | +44 20 7882 2306 |
| Fax: | +44 20 7882 2189 |
| Email: | t.parish@qmul.ac.uk |
| Address: | Centre for Immunology and Infectious Disease, |
Biography
Tanya Parish studied for her PhD at the National Institute for Medical Research with Philip Draper, where she investigated gene regulation in mycobacteria. She subsequently conducted post-doctoral research at the London School of Hygiene & Tropical Medicine with Neil Stoker, studying several facets of the biology of Mycobacterium tuberculosis. In 2000, she was appointed as a Lecturer in Bacterial Pathogenesis at Barts and the London and established her own research group in tuberculosis. She currently holds the post of Professor of Mycobacteriology.
Tanya is also the Director of Drug Discovery at the Infectious Disease Research Institute in Seattle. IDRI is a not-for profit corporation with the mission of finding treatments and cures for diseases that continue to burden individuals and countries in the developing world.
See http://www.idri.org/index.php?name=about&subName=staff&id=17
Research Activity
Our group is involved in researching pathogenic mechanisms of the global pathogen Mycobacterium tuberculosis. Using molecular genetics we aim to identify genes involved in virulence, and to contribute to the understanding of mycobacterial biology which is fundamental to the identification of new drug targets and vaccine strategies.
Our work involves the study of:
• basic metabolic pathways including isoprenoid and menaquinone biosynthesis;
• the role of cytochrome P450s in metabolism;
• the role of the Clp proteases in M. tuberculosis;
• the genetics of cell wall biosynthesis - mycolic acids, arabinogalactan, and lipoarabinomannan;
• the control of gene expression;
• the identification and validation of novel drug targets; and
• the development of molecular tools for M. tuberculosis.
Key Publications
• The non-mevalonate pathway of isoprenoid biosynthesis in Mycobacterium tuberculosis is essential and transcriptionally-regulated by Dxs activity. A.C. Brown, M. Eberl, D.C. Crick, H. Jomaa and T. Parish. J. Bacteriol. 2010. 192: 2424-2433
• Sensitive detection of gene expression in mycobacteria under replicating and non-replicating conditions using optimized far-red reporters. P. Carroll, L.J. Schreuder, J. Muwanguzi-Karugaba, S. Wiles, B. D. Robertson, J. Ripoll, T. H. Ward, G. J. Bancroft, U. E. Schaible, and T. Parish. PLoS One. 2010. 5:e9823.
• The EmbC arabinosyltransferase is inhibited by ethambutol in Mycobacterium tuberculosis. R.Goude, A.G. Amin, D. Chatterjee, and T. Parish. Antimicrob. Ag. Chemother. 2009. 53: 4138-4146.
• Characterization of active site structure in CYP121: A cytochrome P450 essential for viability of Mycobacterium tuberculosis H37Rv. K.J. McLean, P. Carroll, D.G. Lewis, A.J. Dunford, H.E. Seward, R. Neeli, M.R. Cheesman, L. Marsollier, P. Douglas, W.E. Smith, I. Rosenkrands, S.T. Cole, D. Leys, T. Parish, and A.W. Munro. J Biol Chem. 2008. 283: 33406-33416.
• Functional analysis of GlnE, an essential adenylyl transferase in Mycobacterium tuberculosis. P. Carroll, C.A. Pashley and T. Parish. J. Bacteriol. 2008. 190: 4894–4902.
• Fosmidomycin resistance in Mycobacterium tuberculosis is due to a lack of uptake. A.C. Brown and T. Parish. BMC Microbiology. 2008. 8:78.
• EmbC plays a critical role in Mycobacterium tuberculosis. R. Goude, A.G. Amin, D. Chatterjee and T. Parish. J. Bacteriol. 2008. 190:4335-4341.
• E. Sacco, A.S. Covarrubias, H.M. O'Hare, P. Carroll, N. Eynard, T.A. Jones, T. Parish , M. Daffé, K. Bäckbro, A. Quémard. 2007. The missing piece of the type II fatty acid synthase system from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA. 104: 14628-14633.
• T. Parish , G. Roberts, F. Laval, M. Schaeffer, M. Daffé, and K. Duncan. 2007. Functional complementation of the essential gene fabG1 of Mycobacterium tuberculosis by Mycobacterium smegmatis fabG, but not Escherichia coli fabG. J. Bacteriol. 189: 3721-3728.
• P. Carroll, D.G.N. Muttucumuaru and T. Parish. Use of a tetracycline-inducible system for conditional expression in Mycbacterium tuberculosis and Mycobacterium smegmatis. 2005. Appl. Env. Microbiol. 71: 3077 -3084.
