Liang TAO, Ph.D.

School of Life Sciences

Laboratory of Host-Microbe Interactions

CONTACT

Email: taoliang@westlake.edu.cn

Website:

Liang TAO, Ph.D.

School of Life Sciences

Laboratory of Host-Microbe Interactions

CONTACT

Email: taoliang@westlake.edu.cn

Website:

"Release your dream, explore the future, we gather at Westlake to make our own history."

 

Biography

Liang  Tao received his bachelor’s degrees in both Life Science and Computer Science  and later Ph. D. degree in Biology at University of Science and Technology of  China in 2005 and 2010. Following a two-year postdoctoral research at Kansas  University Medical Center, he joined Dr. Min Dong's lab at New England Primate  Research Center / Harvard Medical School and later moved to Boston Children's  Hospital / Harvard Medical School. In 2017, he was promoted to the junior  faculty rank of instructor at Dept. of Surgery, Harvard Medical School. In 2018,  Dr. Tao joined the Westlake University as an assistant professor.

 

Research

Dr.  Liang Tao has been investigating human pathogens and host-bacteria interactions,  including how pathogenic bacteria cause human diseases and evade the host immune  defense, what the major bacterial virulence factors/toxins are and their  regulations, and how these virulence factors/toxins target and affect their  hosts. As an example, an investigation on Clostridium difficile toxin B  receptors interpreted how this toxin finds its entryway on the colonic  epithelia, which directly account for the initiation of C. difficile  infection. This work was highlighted by Nature Reviews  Microbiology, Science Signaling, and Faculty of 1000.  Along the lines of basic research, he is also keen on translating the insights  and knowledge of toxins toward developing new scientific tools as well as novel  therapeutics. He was awarded the Outstanding President Scholarship of CAS and  Harvard Chinese Life Science Distinguished Research Award for his work. He  published first-author papers at Nature, Science, Nature Communications,  PLoS Pathogens, etc., and held several international patents. 


The  current research areas of his lab include: (1) Basic study on molecular  mechanism of toxin actions. (2) Translational research on developing novel toxin  derivate. (3) Basic principles of host-microbiota interactions.

 

Representative  Publications

(*  Co-first author.  # Corresponding author)

1. Zhou, Y.*, Li, D.*, Luo, J. *, Chen, A., Li, X., Pan, Z., Wan, L., He, L., Li, D., Li, Y., Dong, M., Tao,L.#(2021) Sulfated glycosaminoglycans and low-density lipoprotein receptor mediate the cellular entry of Clostridium novyi alpha-toxin. Cell Res 0:1-4

2. Pan, Z. *, Zhang, Y. *, Luo, J. *, Li, D., Zhou, Y., He, L., Yang, Q., Dong, M.#, Tao,L.# (2021) Functional analyses of epidemic Clostridioides difficile toxin B variants reveal their divergence in utilizing receptors and inducing pathology. PLoS Pathog 17(1): e1009197

3. Henkel, D., Tatge, H., Schottelndreider, D., Tao,L., Dong, M., and Gerhard, R. (2020) Receptor binding domains of TcdB from Clostridioides difficile for chondroitin sulfate proteoglycan-4 and Frizzled proteins are functionally independent and additive. Toxins 12 (12), 736

4. Shen, E., Zhu, K., Li, D., Pan, Z., Luo, Y., Bian, Q., He, L., Song, X., Zhen, Y., Jin, D., and Tao,L.# (2020) Subtyping analysis reveals new variants and accelerated evolution of Clostridioides difficile toxin B. Commun Biol 3(1):347.

5. Tao, L. *#, Tian, S. *, Zhang, J.*, Liu, Z., Robinson-McCarthy, L., Miyashita, S. I., Breault, D. T., Gerhard, R., Oottamasathien, S., Whelan, S. P. J., and Dong, M.# (2019) Sulfated glycosaminoglycans and low-density lipoprotein receptor contribute to Clostridium difficile toxin A entry into cells.Nat Microbiol 4, 1760–1769.

6. Chen, P., Tao, L., Liu, Z., Dong, M. & Jin, R. (2019) Structural insight into Wnt signaling inhibition by Clostridium difficile toxin B. FEBS J286, 874-881.

7. Tian, S., Muneeruddin, K., Choi, M.Y., Tao, L., Bhuiyan, RH., Ohmi, Y., Furukawa, K., Boland, S., Shaffer, SA., Adam, RM., Dong, M. (2018) Genome-wide CRISPR screens for Shiga toxins and ricin reveal Golgi proteins critical for glycosylation. PLoS Biol16, e2006951.

8. Chen, P.*, Tao, L.*, Wang, T., Zhang, J., He, A., Lam, K., Liu, Z., He, X., Perry, K., Dong, M., Jin, R., (2018) Structural basis for recognition of frizzled proteins by Clostridium difficile toxin B. Science 360: 664-669.

9. Zhang, S., Lebreton, F., Mansfield, M.J., Miyashita, S.I., Zhang, J., Schwartzman, J.A., Tao, L., Masuyer, G., Martı´nez-Carranza, M., Stenmark, P., Gilmore, M.S., Doxey, A.C., and Dong, M. (2018) Identification of a botulinum neurotoxin-like toxin in a commensal strain of Enterococcus faecium. Cell Host Microbe23:169-176 e166.

10. Tao, L.*, Peng, L.*, Berntsson, RP-A., Park, S., Yu, F., Boone, C., Stenmark, P., Krupp, J., and Dong, M., (2017) Engineered botulinum neurotoxin B with improved efficacy for targeting human receptors. Nat Commun 8, 53.

11. Zhang, S., Berntsson, RP-A., Tepp, W., Tao, L., Johnson, E., Stenmark, P., and Dong, M., (2017) Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC.Nat Commun 8, 1637.

12. Tao, L., Zhang, J., Meraner, P., Tovaglieri, A., Wu, X., Gerhard, R., Zhang, X., Stallcup, B.W., Miao, J., He, X., Hurdle, G.J., Breault, T.D., Brass, A.L., and Dong, M., (2016) Frizzled proteins are colonic epithelial receptors for C. difficile toxin B. Nature 538:350-355.

13. Jana, B., Tao, L.,Biswas, I., (2016) Strain-Dependent Recognition of a Unique Degradation Motif by ClpXP in Streptococcus mutansMSphere1 (6), e00287-16.

14. Tao, L., and Biswas, I., (2015) Degradation of SsrA-tagged proteins in streptococci. Microbiol161:884-894.

15. Peng, L., Adler, M., Demogines, A., Borrell, A., Liu, H., Tao, L., Tepp, W.H., Zhang, S.C., Johnson, E.A., Sawyer, S.L., and Dong, M., (2014) Widespread sequence variations in VAMP1 across vertebrates suggest a potential selective pressure from botulinum neurotoxins. PLoS Pathog 10: e1004177.

16. Tao, L., and Biswas, I., (2013) ClpL is required for folding of CtsR in Streptococcus mutans. J Bacteriol 195:576-584

17.Tao, L., Chattoraj, P., and Biswas, I., (2012) CtsR regulation in mcsAB deficient gram-positive bacteria. J Bacteriol194:1361-1368.

18. Wu, X., Wang, Y., and Tao, L.# (2011) Sulfhydryl compounds reduce Staphylococcus aureus biofilm formation by inhibiting PIA biosynthesis. FEMS Microbiol Lett316:44-50

19.Tao, L.*, Wu, X.*, and Sun, B. (2010) Alternative sigma factor σH modulates prophage integration and excision in Staphylococcus aureus. PLoS Pathog 6(5): e1000888