Liang Tang

Associate Professor
Primary office:
(785) 864-5838
8041 Haworth


Structure, assembly, and dynamics of molecular complexes in viruses and bacteria.

Many biological processes are carried out by complex, multi-component macromolecular assemblies. The assembly and dynamics of these molecular machines has been central to structural and cell biology, and has imposed tremendous challenges owing to their unusual complexity. The research in this lab combines the powers of X-ray crystallography and electron cryo-microscopy to understand the structure, function, and dynamics of large molecular assemblies from a variety of viruses and pathogenic bacteria. These microbial pathogens cause diseases ranging from pneumonia, meningitis and shigellosis to mucocutaneous lesions, encephalitis and several forms of cancer. We aim to understand lifecycles of these pathogeic microorganisms at atomic or near atomic detail in order to find novel, more efficient and more economic ways for prevention, treatment and cure.  Currently, the lab is focused on the DNA-packaging nano-machines in dsDNA bacterial viruses and herpesviruses, and the type III secretion systems in Gram-gegative pathogenic bacteria.

Representative Publications
  • Haiyan Zhao, Yvonne Kamau, Theodore Christensen and Liang Tang (2012) Structural and functional studies of the bacteriophage Sf6 terminase small subunit reveal a DNA-spooling device facilitated by structural plasticity. J. Mol. Biol. In press.
  • Haiyan Zhao, Reuben D. Sequeira, Nadezhda A. Galeva and Liang Tang (2011) The host outer membrane proteins OmpA and OmpC are associated with the Shigella phage Sf6 virion. Virology. 409, 319-27. PMID: 21071053. [Featured on the cover]
  • Haiyan Zhao, Casey J. Finch, Reuben D. Sequeira, Brian A. Johnson, John E. Johnson, Sherwood R. Casjens and Liang Tang (2010) Crystal structure of the DNA-recognition component of the bacterial virus Sf6 genome-packaging machine. Proc. Natl. Acad. Sci. USA. 107, 1971-1976.
  • H Zhao and L Tang (2009) Crystallographic characterization of the histidine protein kinase from an essential two-component regulatory system YycFG. Acta Crystallogr Sect F Struct Biol Cryst Commun. 65, 346-349.
  • Liang Tang, Eddie B. Gilcrease, Sherwood Casjens, John E. Johnson (2006) Highly discriminatory binding of capsid cementing proteins in bacteriophage L. Structure 14, 837–45.
  • Gabriel C. Lander, Liang Tang, Sherwood R. Casjens, Eddie B. Gilcrease, Peter Prevelige, Anton Poliakov, Clinton S. Potter, Bridget Carragher and John E. Johnson. (2006) The structure of an infectious p22 virion shows the signal for headful DNA packaging. Science 312, 1791–5. Epub 2006 May 18. [Featured on the cover]
  • Reza Khayat, Liang Tang, Mark Young, John E. Johnson (2005) Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses. Proc. Natl. Acad. Sci. USA. 102, 18944–9.
  • L. Tang, W. Marion, G. Cingolani, P.E. Prevelige & J.E. Johnson (2005) The three-dimensional structure of the bacteriophage P22 tail machine. EMBO J. 24, 2087–95. [cover story]
  • G. Rice, L. Tang, K. Stedman, F. Roberto, J. Spuhler, E. Gillitzer, J.E. Johnson, T. Douglas, and M.J. Young (2004) The structure of a thermophilic archaeal virus shows a dsDNA viral capsid type that spans all domains of life. Proc. Natl. Acad. Sci. USA 101, 7716–7720.
  • L. Tang, C.-S. Lin, N.K. Krishna, M. Yeager, A. Schneemann & J.E. Johnson (2002) Virus-like particles of a fish nodavirus display a capsid subunit domain organization different from that of insect nodaviruses. Journal of Virology 76, 6370–6375.
  • L. Tang & J.E. Johnson (2002) Structural biology of viruses by the combination of electron cryomicroscopy and X-ray crystallography. Biochemistry 41, 11517–11524.
  • L. Tang, K.N. Johnson, L.A. Ball, T. Lin, M. Yeager & J.E. Johnson (2001) The structure of Pariacoto virus reveals a dodecahedral cage of duplex RNA. Nature Structural Biology 8, 77–83.

 

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