UNIVERSITY OF MIAMI, Miami, FL; Ph.D. in Microbiology and Immunology 2005.
ST. LOUIS UNIVERSITY, St. Louis, MO; M.S. in (Research) Biology 2000.
ST. LOUIS UNIVERSITY, St, Louis, MO; B.S. Biology 1998.
Current Research: Salmonella Translocated Effectors
My research focuses on the SPI-2 effectors SseJ and SifA. SifA is a SPI-2 effector that is critical for intracellular survival in macrophages and for mouse virulence. Crystal structure analysis reveals that SifA has two domains. The amino terminal domain is known to bind the eukaryotic protein SKIP (SifA and kinesin interacting protein). SifA recruits SKIP to the SCV and SKIP in turn interacts with the motor protein kinesin linking SifA to the microtubular network. The carboxyl terminal domain of SifA has a guanine nucleotide exchange factor fold (GEF) similar to the SPI-1 effector SopE and binds RhoA-GDP. We have shown that the GEF domain is critical for intracellular replication. The focus of my research is to discover the GTPase targeted by SifA and further investigate the role of the GEF-like domain during intracellular infection.
SseJ is a SPI-2 effector that has glycerophospholipid :cholesterol acyltransferase (GCAT), phospholipase A1 and deacylase activity. A deletion of SseJ results in attenuation of virulence in mice and peritoneal macrophages. The eukaryotic signaling protein RhoA stimulates SseJ’s enzymatic activity resulting in an increase of intracellular cholesterol ester. My current research is to further investigate the role of SseJ during Salmonella infection.
Christen M.*, Coye LH.*, Hontz JS., LaRock D., Pfuetzner R., Megha, Miller SI. Activation of a bacterial virulence protein by the GTPase RhoA. Science Signaling. 2009 Nov: 2(95):ra71.* Co-first author
Coye LH. and Collins CM. Identification of SpyA, a novel ADP-ribosyltransferase from Streptococcus pyogenes. Mol Microbiology. 2004 Oct: 54(1):89-98
Picking WL, Coye L, Osiecki JC, Barnoski Serfis A., Schaper E., and Picking WD. Identification of functional regions within invasion plasmid antigen C (IpaC) of Shigella flexneri. Mol Microbiol. 2001 Jan: 39 (1):100-11
Tran N., Serfis AB., Osiecki JC., Picking WL., Coye L, Davis R., Picking WD. Interaction of Shigella flexneri IpaC with model membranes correlates with effects on cultured cells. Infect. Immun. 2000 Jun: 68(6):3710-5