- Pingwei Li
- Associate Professor
- ILSB / Room 2155
- Graduate Education
- M.Sc. Peking University, Beijing, P. R. China (1992)
- Ph.D. Peking University, Beijing, P. R. China (1996)
- Postdoc. Fred Hutchinson Cancer Research Center, Seattle, Washington (1998-2001)
- Postdoc. Princeton University, Princeton, New Jersey (2001-2003)
- Postdoc. California Institute of Technology, Pasadena, California (2003-2005)
- Joined Texas A&M in 2005
X-ray crystallography/Structural Immunology
The innate immune response is the first line of defense against invading pathogens. It relies on the body’s ability to recognize conserved features of pathogens that are not present in uninfected cells. Innate immunity is regulated by a broad range of germline-encoded receptors, such as toll-like receptors (TLR) and NK cell receptors. These immunoreceptors detect molecules associated with infection and cellular distress, and initiate specific immune responses.
Our laboratory is interested in the structural and functional basis of protein-protein interactions mediating innate immunity. We use x-ray crystallography, surface plasmon resonance (SPR), and site directed mutagenesis, to study the molecular structures of imunoreceptor/ligand complexes and subsequent molecular event in the signaling pathway. The aim of our research is to understand the molecular mechanism of how the immune system recognizes pathogens or cellular stress and how it responds to infections. We are also interested in the structural characterization of several immunoglobulin superfamily (IgSF) proteins, which are involved in cell adhesion and membrane fusion.
Zhang, Z, Hu, F, Sung, MW, Shu, C, Castillo-González, C, Koiwa, H et al.. RISC-interacting clearing 3'- 5' exoribonucleases (RICEs) degrade uridylated cleavage fragments to maintain functional RISC in Arabidopsis thaliana. Elife. 2017;6 :.
Shen, Q, Zeng, D, Zhao, B, Bhatt, VS, Li, P, Cho, JH et al.. The Molecular Mechanisms Underlying the Hijack of Host Proteins by the 1918 Spanish Influenza Virus. ACS Chem. Biol. 2017;12 (5):1199-1203.
Zhao, B, Yi, G, Du, F, Chuang, YC, Vaughan, RC, Sankaran, B et al.. Structure and function of the Zika virus full-length NS5 protein. Nat Commun. 2017;8 :14762.
Zhao, B, Shu, C, Gao, X, Sankaran, B, Du, F, Shelton, CL et al.. Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins. Proc. Natl. Acad. Sci. U.S.A. 2016;113 (24):E3403-12.
Li, T, Cheng, H, Yuan, H, Xu, Q, Shu, C, Zhang, Y et al.. Antitumor Activity of cGAMP via Stimulation of cGAS-cGAMP-STING-IRF3 Mediated Innate Immune Response. Sci Rep. 2016;6 :19049.
Yi, G, Wen, Y, Shu, C, Han, Q, Konan, KV, Li, P et al.. Hepatitis C Virus NS4B Can Suppress STING Accumulation To Evade Innate Immune Responses. J. Virol. 2015;90 (1):254-65.
Weaver, J, Watts, T, Li, P, Rye, HS. Structural basis of substrate selectivity of E. coli prolidase. PLoS ONE. 2014;9 (10):e111531.
Shu, C, Li, X, Li, P. The mechanism of double-stranded DNA sensing through the cGAS-STING pathway. Cytokine Growth Factor Rev. 2014;25 (6):641-8.
Li, X, Shu, C, Yi, G, Chaton, CT, Shelton, CL, Diao, J et al.. Cyclic GMP-AMP synthase is activated by double-stranded DNA-induced oligomerization. Immunity. 2013;39 (6):1019-31.
Morales, KA, Yang, Y, Long, Z, Li, P, Taylor, AB, Hart, PJ et al.. Cd2+ as a Ca2+ surrogate in protein-membrane interactions: isostructural but not isofunctional. J. Am. Chem. Soc. 2013;135 (35):12980-3.