Zhao-Qing Luo

PULSe Contributor - not currently hosting students for laboratory rotations or recruiting students in the laboratory

Current Research Interests:

Our laboratory is interested in understanding the mechanisms that allow microbial pathogens to survive and multiply within the hostile host cells and how host cells respond to infection. We use Legionella pneumophila, the causative agent of Legionnaires disease as a model organism. One essential pathogenic factor of this bacterium is the Dot/Icm type IV secretion system that injects approximately 300 virulence proteins (effectors) into host cells to create a niche permissive for bacterial replication. One focus of our research is to determine the function of these proteins and their roles in bacterial infection. The second focus is to examine the mechanism of the detection and response of immune cells to intracellular pathogens, particularly the signaling pathway involved in the detection of the bacterial ribosomal protein RpsL that triggers lysosomal cell death.  Finally, we are interested in study the function of Fic proteins found in diverse bacteria. The long term goal of these studies is to elucidate the signal transduction pathways important for bacterial virulence, immune detection and other events important for the establishment of successful infection, such information will be invaluable not only in combating infectious diseases but also in our understanding of cell signaling in both prokaryotic and eukaryotic cells. 

Selected Publications:

Zhu W.†, Tao L.†, Quick M.L,. Joyce J.A., Qu J.M., Luo Z.-Q. 2015. Sensing cytosolic RpsL by macrophages induces lysosomal cell death and termination of bacterial infection. PLoS Pathogens. 11(3):e1004704. doi: 10.1371/journal.ppat.1004704. eCollection 2015 Mar. †,equal contribution authors. PMID: 25738962

Hsu F†., Luo X†., Qiu J†., Teng Y.B., Jin J., Smolka M.B., Luo Z.-Q*., Mao Y*. 2014. The Legionella effector SidC defines a unique family of ubiquitin ligases important for bacterial phagosomal remodeling. Proc. Natl. Acad. Sci. USA. 111(29):10538-43. doi: 10.1073/pnas.1402605111. Epub 2014 Jul 8. †,equal contribution authors. PMID: 25006264

Hsu F., Zhu W., Brennan L., Tao L, Luo ZQ, Mao Y. 2012. Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase. Proc. Natl. Acad. Sci. USA.  109:13567-72. PMID:23150405

Hsu F., Zhu W., Brennan L., Tao L, Luo ZQ, Mao Y. 2012. Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase. Proc. Natl. Acad. Sci. USA.  109:13567-72. PMID:23150405

Tan Y. Arnold A. J. and Luo Z.-Q. 2011. Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination. Proc. Natl. Acad. Sci. USA. 108:21212-7 PMID: 22158903

Tan Y. and Luo Z.-Q. 2011. Legionella pneumophila SidD is a deAMPylase that modifies Rab1. Nature. 475:506-509. PMID: 21734656.

Fontana M. F., Banga S., Barry K. C., Shen X., Tan, Y., Luo Z.-Q*. and Vance E.V*.  2011. Secreted bacterial effectors that inhibit host protein synthesis are critical for induction of the innate immune response to virulent Legionella pneumophila.  PLoS Pathogens. 7: e1001289. PMID: 21390206  

Xu L†., Shen X†., Bryan A., Banga S., Swanson M. and Luo ZQ. 2010. Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector. PLoS Pathogens 19;6(3):e1000822. †, equal contribution authors, PMID: 20333253

Liu Y., Gao P. Banga S. and Luo Z.-Q.  2008. An in vivo gene deletion system for determining temporal requirement of bacterial virulence factors. Proc. Natl. Acad. Sci USA. 105:9385-90. PMID: 18599442

Banga, S., Gao, P., Shen X., Fiscus V., Zong W-X., Chen L. and Luo Z.-Q. 2007. Legionella pneumophila inhibits macrophage apoptosis by targeting pro-death members of the Bcl2 protein family. Proc. Natl. Acad. Sci. USA. 104: 5121-5126. PMID: 17360363