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Faculty Detail    
Campus Address BBRB 406A Zip 2170
Phone  (205) 975-0591
E-mail  tgreen@uab.edu
Other websites

Faculty Appointment(s)
Appointment Type Department Division Rank
Primary  Microbiology  Microbiology Associate Professor
Center  Center for AIDS Research  Center for AIDS Research Associate Professor
Center  General Clinical Research Center  Ctr for Clinical & Translational Sci Associate Professor
Center  General Clinical Research Center  Nephrology Research & Training Center Associate Professor

Graduate Biomedical Sciences Affiliations
Biochemistry and Structural Biology 

Biographical Sketch 
In the beginning of my scientific training, I studied natural products as potential therapeutics against bacterial and fungal infection and various forms of cancer at the University of Alabama at Huntsville. During this time, I developed an interest in the molecular mechanisms that were affected by the small molecules from our studies. My curiosity to understand infection and combat of disease at an atomic level lead me to pursue graduate training in the field x-ray crystallography at the University of Alabama at Birmingham. This period of my training allowed me to improve my knowledge of protein chemistry and protein structure, specifically with an emphasis on viral protein targets. I have maintained my interest in virus biology and protein structure as a faculty member in the Department of Microbiology at the UAB where I study negative-strand RNA viruses. Nonsegmented negative-strand RNA viruses (NNSVs) include measles, mumps, Ebola and many other causative agents of serious human disease. In order to gain a better understanding of the replication cycle of this class of viruses, my lab is studying the molecular structure of vesicular stomatitis virus (VSV) a prototypic NNSV in the family Rhabdoviridae. NNSV encode three functionally conserved proteins (N, P, and L) that are essential to viral transcription and replication. The large polymerase subunit (L) and phosphoprotein (P) form the RNA-dependent RNA polymerase (RdRp), while the nucleocapsid protein (N) and the genomic RNA, not the naked RNA alone, form the active template for these enzymatic processes. Using state-of-the-art techniques, such as x-ray crystallography and cryo-electron microscopy, we have observed atomic-level snapshots of how the viral capsid protein encapsidates and protects the genomic RNA, how this template is accessed by the viral polymerase co-factors, how the capsid structure is affected by specific RNA sequences and the global structure of the VSV virion. We are now pursuing the structure and studying the biology of the L protein. L is a multi-functional, modular protein housing several discreet functional domains. We have known the sequences of L proteins for over 30 years yet there have been no high-resolution detail of the L protein structure until now. We have recently determined the first structure of any part of an NNSV L protein. Our structure of the N-terminal domain of the VSV L is a big advancement in the field of virus structural biology as it demonstrates a unique fold and shares predicted structural homology with the L proteins of the viral families Rhabdoviridae, Paramyxoviridae and Filoviridae, families that include select agents. Moving forward we will continue to investigate the mechanisms of viral transcription and replication including the involvement of cellular factors. Better understanding of these processes will yield new avenues for future therapeutic design against this group of viruses. My expertise in the field of virology and x-ray crystallography has lead to my collaboration with investigators locally, nationally and internationally on viral, bacterial, human and murine targets as noted in my publication record. I believe, as scientists, we can maximize discovery by surrounding ourselves with the right team locally and abroad. As I continue to study more complex subjects, I have begun to use an integrated approach featuring electron microscopy, x-ray crystallography and small angle x-ray scattering. The structural techniques that I use are, ultimately, complemented with the biological studies from my lab as well as those of my collaborators.

Research/Clinical Interest
Viral Transcription and Replication, Capsid Structure
My current research interests include crystallographic studies of proteins involved in polynucleotide synthesis for negative strand RNA viruses. These efforts have included: structure determination of the nucleocapsid of VSV encapsidated with various sequences of RNA, as well as complexes of the nucleocapsid with the polymerase co-factor, P.

Selected Publications 
Publication PUBMEDID
Signature motifs of GDP polyribonucleotidyltransferase, a non-segmented negative strand RNA viral mRNA capping enzyme, domain in the L protein are required for covalent enzyme-pRNA intermediate formation. Neubauer J, Ogino M, Green TJ, Ogino T. Nucleic Acids Res 2016. 44:330-341.   26602696 
Structure and function of the N-terminal domain of the vesicular stomatitis virus RNA polymerase. Qiu S, Ogino M, Luo M, Ogino T, Green TJ. J Virol. 2015. 90:715-724.  26512087 
Structure of the vesicular stomatitis virus nucleoprotein-RNA complex.Green TJ, Zhang X, Wertz GW, Luo M. Science. 2006 Jul 21;313(5785):357-60. Epub 2006 Jun 15.  16778022 
Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P. Green TJ, Luo M. Proc Natl Acad Sci U S A. 2009 Jul 14;106(28):11713-8. doi: 10.1073/pnas.0903228106. Epub 2009 Jul 1.  19571006 
Cryo-EM model of the bullet-shaped vesicular stomatitis virus. Ge P, Tsao J, Schein S, Green TJ, Luo M, Zhou ZH. Science. 2010 Feb 5;327(5966):689-93. doi: 10.1126/science.1181766.  20133572 
Access to RNA encapsidated in the nucleocapsid of vesicular stomatitis virus. Green TJ, Rowse M, Tsao J, Kang J, Ge P, Zhou ZH, Luo M. J Virol. 2011 Mar;85(6):2714-22. doi: 10.1128/JVI.01927-10. Epub 2010 Dec 22.  21177817 
Structure of human stabilin-1 interacting chitinase-like protein (SI-CLP) reveals a saccharide-binding cleft with lower sugar-binding selectivity. Meng G, Zhao Y, Bai X, Liu Y, Green TJ, Luo M, Zheng X. J Biol Chem. 2010 Dec 17;285(51):39898-904. doi: 10.1074/jbc.M110.130781. Epub 2010 Aug 19.  20724479 
Characterization of a mumps virus nucleocapsidlike particle. Cox R, Green TJ, Qiu S, Kang J, Tsao J, Prevelige PE, He B, Luo M. J Virol. 2009 Nov;83(21):11402-6. doi: 10.1128/JVI.00504-09. Epub 2009 Aug 19.  19692473 
1.55Å X-ray Crystal Structure of Rv3902c from M. tuberculosis. Reddy BG, Moates D, Green TJ, Delucas L, Kim C, Terwilliger T. 2014 Acta Cryst. F70:414-417.  24699730 
Nucleocapsid protein structures from orthobunyaviruses reveal insight into ribonucleoprotein architecture and RNA polymerization. Ariza A, Tanner SJ, Walter CT, Dent KC, Shepherd DA, Wu W, Matthews SV, Hiscox JA, Green TJ, Luo M, Elliott RM, Fooks AR, Ashcroft AE, Stonehouse NJ, Ranson NA, Barr JN, Edwards TA. 2013 Nucleic Acids Res. 41(11):5912-26.  23595147 
Common mechanism for RNA encapsidation by negative-strand RNA viruses. Green TJ, Cox R, Tsao J, Rowse M, Qiu S, Luo M. J Virol. 2014 Apr;88(7):3766-75. doi: 10.1128/JVI.03483-13. Epub 2014 Jan 15.  24429372 

virology, structure, crystallography