Biochemistry and Structural Biology  Back to Main

Faculty Detail    
Campus Address BBRB 406A Zip 2170
Phone  (205) 975-0591
Other websites

Undergraduate  University of Alabama at Huntsville    1994  BS 
Graduate  University of Alabama at Birmingham    2002  PhD 
Fellowship  University of Alabama at Birmingham    2005  Post Doc 

Faculty Appointment(s)
Appointment Type Department Division Rank
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
Primary  Microbiology  Microbiology Associate Professor

Graduate Biomedical Sciences Affiliations
Biochemistry and Structural Biology 

Biographical Sketch 
My lab aims to understand the structure-function relationships involved in the processes of viral replication, virus-host interactions, capsid structure, polynucleotide synthesis and antibody-antigen complex formation. Toward this goal, we have used structural techniques (cryo-electron microscopy, x-ray crystallography and small angle x-ray scattering) and biochemistry to study: viral proteins from negative strand RNA viruses (NSV: influenza A, mumps, rabies virus, VSV), retroviruses (HIV), coronaviruses (SARS-CoV-2), human antibodies (associated with IgA nephropathy), and bacteria (IgA1 proteases). This dual approach has been successful in producing near atomic-level snapshots of many complex protein assemblies as well as enabling a fast-track to novel biological discovery and new experimental design. Professionally, my expertise in structural biology has led to my collaboration with investigators locally, nationally and internationally on viral, bacterial, human and murine targets.

Research/Clinical Interest
My funded interests include: 1) Understanding of the processes of polynucleotide synthesis used by NSV. We are studying the complex mechanism of VSV transcription and replication from the view of the template (a complex between the viral genome and the nucleocapsid), as well as, the polymerase machinery (a complex between the L protein, P protein and potentially host factors); 2) Discovering the role of aberrant glycosylation patterns on the hinge region of IgA1 and recognition of these elements by IgG autoantibodies. The hallmark of the disease, IgA nephropathy (IgAN), is the accumulation of IgA1-containing immune complexes in the kidneys, which drive progressive renal injury in IgAN patients. Our UAB research groups have shown that the pathogenic immune complexes in IgAN consist of IgA1 with hinge-region O-glycans deficient in galactose (Gd-IgA1) and IgG autoantibodies that bind Gd-IgA1. We are characterizing IgG autoantibodies from IgAN patients and defining structural features of these autoantibodies that lead to pathogenic immune complex formation. 3) Understanding antibody recognition and neutralization of CoV spike (S) protein. Through a collaboration with University of Alabama at Birmingham researchers, my group has produced an array of CoV proteins to enable structural studies of viral antigen-antibody complexes; 4) Defining the role of N-linked glycans and microdomain clustering of glycans on GP120 of HIV. Here, we are using protein modeling to interpret glycan function and mutagenesis in the context of HIV infection. All of my projects involve proteins and/or human antibodies with each project having carbohydrates as a common element, including: ribose moieties as substrates, to RNA encapsidation, to more complex sugars adorning the surfaces of viral or host proteins, and finally to glycosylated peptides that are recognized by antibodies.

Selected Publications 
Publication PUBMEDID
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 
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 
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 
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 
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 
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 
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 
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 
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 

virology, immunology, antibodies, kidney disease, nephropathy, protein structure, crystallography