TTU Biology: Faculty

Zhang, Kai

Office Phone: 1(806)834-0550

Associate Professor
  • Postdoc: Molecular parasitology, Washington University School of Medicine, St. Louis, MO (2000-2006).
  • Ph.D., Cellular and Microbial Biology, The Catholic University of America, Washington, DC. (2000)
  • BSc., Biochemistry and Molecular Biology, Peking University, Beijing, China (1996)


    • MBIO3401: Principles of Microbiology (undergraduate)
    • MBIO4367/MBIO6367: Molecular Pathogenesis of  Protozoans (undergraduate/graduate)

      Office: Biology 205

      Lab: Biology 203, 204

Research Interests

Protozoan parasites of the genus Leishmania alternate between flagellated promastigotes in sandfly vectors, and non-flagellated amastigotes residing in mammalian macrophages. They are the causative agents for a group of devastating diseases (leishmaniasis) infecting 10-12 million people worldwide. Current drugs for leishmaniasis are plagued with low efficacy and high toxicity. With resistance on the rise and no safe vaccine available, there is a pressing need to maintain a steady stream of new drugs and drug targets. Our long term goal is to decipher the molecular strategy utilized by Leishmania parasites to thrive in the harsh environments in sandflies and mammals. Understanding the fundamental mechanism of pathogenesis can lead to new and improved treatments.


Leishmania parasites are easy to culture and highly amenable to genetic manipulations. Genomes of several Leishmania species are fully sequenced and annotated, providing excellent opportunities to study various genes/pathways that are relevant to parasite virulence. My lab focuses on the role of lipid metabolism in Leishmania pathogenesis. Lipids are essential components of life. They exert important functions in membrane biology, energy conservation, protein modification, and signal transduction. The role of lipids is relatively understudied in protozoan parasites. My lab utilizes a combination of molecular biology, cell biology, animal models and lipidomic approaches to uncover the significance of sphingolipids, phospholipids, and sterols in Leishmania survival and virulence. A better understanding of lipid metabolism will not only advance our knowledge on the basic biology of Leishmania parasites,but also facilitate the development of novel drugs.

If you are interested in doing innovative research in Leishmania biology as a postdoc, graduate student, or undergraduate student, contact Dr. Kai Zhang for more ifnformation!

Selected Publications

Xu, W., Hsu, F. F., Baykal, E., Huang, J., andZhang, K*. (2014) Sterol biosynthesis is required for heat resistance but notextracellular survival in Leishmania.PLoS Pathogens in press.


Zhang, O., Hsu, F. F., Xu, W., Pawlowic, M.C., and Zhang, K*. (2013) Sphingosine kinase A is a pleiotropic and essentialenzyme for Leishmania survival and virulence. Mol. Microbiol2013Aug 28. PMCID: PMC3938578.


Pillai, A. B., Xu, W., Zhang, O., and Zhang,K.(2012) Sphingolipid Degradation in Leishmania (Leishmania) amazonensis.PLoS Negl Trop Dis. 2012 Dec;6(12):e1944. PMCID: PMC3527339.


Pawlowic, M. C., and Zhang, K. (2012) Leishmania parasitespossess a platelet-activating factor acetylhydrolase important forvirulence. Mol Biochem Parasitol. 2012 Aug 28. PMCID: PMC3492548.

Zhang, O, Xu, W., Pillai, A., and Zhang, K. (2012) Developmentally Regulated SphingolipidDegradation in Leishmania majorPLoS One.2012;7(1):e31059. PMCID: PMC3267774.  


Xu, W., Xin, L., Soong, L., and Zhang, K. (2011)Sphingolipid degradation by Leishmania is required foritsresistance to acidic pH in the mammalian host. Infect Immun. 79(8):3377-87.PMCID: PMC3147570.  


Zhang, K., and Beverley, S. M. (2010) Phospholipidand sphingolipid metabolism in Leishmania. Mol BiochemParasitol. 170(2):55-64. PMCID: PMC2815228.


Zhang, K., Bangs, J. D., and Beverley, S.M.(2010) Sphingolipids in parasitic protozoa. Adv Exp MedBiol. 688:238-48. PMCID: PMC2951629.  


Zhang, O., Wilson, M. C., Xu, W., Hsu, F.F.,Turk, J., Kuhlmann, F. M., Wang, Y., Soong, L., Key, P., Beverley, S. M.,and Zhang, K. (2009) Degradation of Host Sphingomyelin IsEssential for Leishmania Virulence. PLoS Pathogens 5(12):e1000692.doi:10.1371/journal.ppat.1000692. PMCID: PMC2784226.


Sutterwala, S. S., Hsu, F. F., Sevova, E.S.,Schwartz, K. J., Zhang, K., Key, P., Turk, J., Beverley, S. M., and Bangs,J.D. (2008) Developmentally Regulated Sphingolipid Synthesis in African Trypanosomes. Mol.Microbiol70(2):281-296. PMCID: PMC2629665.


Hsu, F. F., Turk, J., Zhang, K.,a nd  Beverley,S. M. (2007) Characterization ofInositol Phosphorylceramides from Leishmania major by TandemMass Spectrometry with Electrospray Ionization. J Am Soc MassSpectrom 18(9):1591-604. PMCID: PMC2065762.  


Zhang, K., Pompey, J. M, Hsu, F.F., Key, P.,B andBandhuvula P., Saba, J. D., Turk, J., and Beverley, S. M. (2007) Redirection ofsphingolipid  metabolism  towards de novo synthesis of ethanolaminein the protozoan parasite Leishmania majorEMBOJ 26:1094-1104.PMCID: PMC1852826.


Zhang, K., Hsu, F. F., Scott,D. A.,Docampo,R., Turk, J., and Beverley, S. M. (2005) Leishmania salvageand remodeling of host sphingolipids in amastigote survival and acidocalcisome biogenesis. Mol.Microbiol.55(5): 1566-78. PMCID: PMC3803142.


Zhang, K., Barron, T., Turco, S. J., and Beverley,S. M. (2004) The LPG1 gene family of Leishmania majorMolBiochem Parasitol.136(1):11-23. PMCID: PMC3791616. 


Zhang, K., Showalter, M., Revollo, J., Hsu,F.F., Turk, J., and Beverley, S. M. (2003) Sphingolipids are essential for differentiationbut not growth in LeishmaniaEMBOJ 22:6016-6026. PMCID: PMC275442.


Descoteaux, A., Avila, H. A.,Zhang, K.,Turco,S. J., and Beverley, S. M. (2002) Leishmania LPG3 encodesaGRP94 homolog required for phosphoglycan synthesis implicated in parasite virulencebut not viabilityEMBO J 21: 4458-69. PMCID: PMC126187.


Zhang, K., and Rathod, P. K. (2002) Divergent regulationof dihydrofolate reductase between malaria parasite and human host. Science 296:545-7. PMCID:PMC3830934.


Shallom, S., Zhang, K., Jiang, L., and Rathod,P. K. (1999) Essential protein-protein interactions between Plasmodium falciparum thymidylatesynthase and dihydrofolate reductase domains. J Biol Chem.274(53):37781-6. PMCID: PMC3791593.