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Faculty Detail    
Campus Address BBRB 311 Zip 2170
Phone  205-996-4502
Other websites

Undergraduate  University of Oslo, Norway    1988  BS, MS 
Graduate  European Molecular Biology Laboratory, Heidelberg, Germany    1993  Ph.D. 

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  Center for Biophysical Sciences/Engineering  Center for Biophysical Sciences/Engineering Associate Professor

Graduate Biomedical Sciences Affiliations
Biochemistry and Structural Biology 
Pathobiology and Molecular Medicine 

Biographical Sketch 
Terje Dokland, Associate Professor of Microbiology, received his Ph.D. from the University of Oslo, Norway on a joint program with the European Molecular Biology Laboratory in Heidelberg, in 1993. His Ph.D. work involved cryo-electron microscopy and 3D reconstruction on the bacteriophages P2, P4 and lambda, and was done with Dr. Stephen D. Fuller at EMBL and Björn H. Lindqvist at the University of Oslo. From 1994-1998 he carried out postdoctoral studies with Dr. Michael G. Rossmann at Purdue University where he continued his studies on bacteriophage assembly using X-ray crystallographic methods. In 1998, Dr. Dokland took up a position as senior scientist at the Institute of Molecular and Cell Biology (formerly Insitute of Molecular Agrobiology) in Singapore, where he set up a structural biology laboratory, including facilities for X-ray crystallography and electron microscopy. He remained in Singapore until April 2004, when he joined the faculty in the Department of Microbiology at UAB. His outside interests include music (bass player in the band "Burning Vinyl"), songwriting, oil painting, hiking, mountain biking, wine and international cooking.

Society Memberships
Organization Name Position Held Org Link
American Society for Microbiology  member 
Microscopy Society of America  member 

Research/Clinical Interest
Structural biology of viral assembly and bacterial pathogenicity
My lab uses a hybrid approach combining electron microscopy (especially cryo-EM), three-dimensional reconstruction, X-ray crystallography, NMR and other biochemical and biophysical approaches to study the structures of viruses, bacteria and proteins involved in viral and bacterial pathogenicity. One of our main projects is on the role of bacteriophages in the mobilization of pathogenicity islands (SaPIs) in Staphylococcus aureus. S. aureus is a ubiquitous commensal on human skin and mucosal epithelia, but is also an opportunistic pathogen that is associated with a range of pathogenic conditions in humans and animals. The emergence of virulent strains of S. aureus that are resistant to a range of antibiotics has become a significant public health problem. Many virulence determinants in S. aureus are carried on mobile genetic elements, such as SaPIs, which are 10-20 kb genomic islands that often carry genes for superantigen toxins. Normally stably integrated into the host genome, the SaPIs are mobilized upon infection with certain “helper” bacteriophages, leading to the packaging of the SaPI genome into phage-like transducing particles using structural proteins encoded by the helper phage. Mobilization is a multi-step process that involves derepression, excision and replication of the SaPI element, followed by assembly, DNA packaging and release of the transducing particles. We study the factors involved in the various steps of this mobilization process using a combination of genetics, biochemistry and structural approaches, including cryo-electron microscopy and 3D reconstruction, X-ray crystallography and NMR. We are also working on the P2-like bacteriophages found in many virulent E. coli strains, including E. coli O157:H7, and on the ultrastructure of bacterial pathogens, such as B. anthracis.

Selected Publications 
Publication PUBMEDID
Dokland T, McKenna R, Ilag LL, Bowman BR, Incardona NL, Fane BA, Rossmann MG. Structure of a viral procapsid with molecular scaffolding. Nature. 1997 Sep 18;389(6648):308-13.
Christie GE, Dokland T. Pirates of the Caudovirales
Virology. 2012, 434:210-21 
Dearborn AD, Dokland T. Mobilization of pathogenicity islands by Staphylococcus aureus strain Newman bacteriophages. Bacteriophage. 2012 Apr 1;2(2):70-78.  23050217 
Damle PK, Wall EA, Spilman MS, Dearborn AD, Ram G, Novick RP, Dokland T, Christie GE. The roles of SaPI1 proteins gp7 (CpmA) and gp6 (CpmB) in capsid size determination and helper phage interference. Virology. 2012 Oct 25;432(2):277-82.  22709958 
Dearborn AD, Laurinmaki P, Chandramouli P, Rodenburg CM, Wang S, Butcher SJ, Dokland T. Structure and size determination of bacteriophage P2 and P4 procapsids: function of size responsiveness mutations. J Struct Biol. 2012 178, 215-224  22508104 
Dearborn AD, Spilman MS, Damle PK, Chang JR, Monroe EB, Saad JS, Christie GE, Dokland T. The Staphylococcus aureus Pathogenicity Island 1 Protein gp6 Functions as an Internal Scaffold during Capsid Size Determination. J Mol Biol. 2011, 412, 210-722.  21821042 
Spilman MS, Dearborn AD, Chang JR, Damle PK, Christie GE, Dokland T. A conformational switch involved in maturation of Staphylococcus aureus bacteriophage 80α capsids. J Mol Biol. 2011, 405(3):863-76.  21129380 
Dokland T. The structural biology of PRRSV.
Virus Res. 2010 Aug 6.  
Spilman MS, Welbon C, Nelson E, Dokland T. Cryo-electron tomography of porcine reproductive and respiratory syndrome virus: organization of the nucleocapsid.
J Gen Virol. 2009 Mar;90(Pt 3):527-35.
Poliakov A, Chang JR, Spilman MS, Damle PK, Christie GE, Mobley JA, Dokland T. Capsid size determination by Staphylococcus aureus pathogenicity island SaPI1 involves specific incorporation of SaPI1 proteins into procapsids. J Mol Biol. 2008 Jul 11;380(3):465-75.  18565341 
Dokland T, Walsh M, Mackenzie JM, Khromykh AA, Ee KH, Wang S. West nile virus core protein; tetramer structure and ribbon formation.
Structure (Camb). 2004 Jul;12(7):1157-63. 
Prasad BV, Hardy ME, Dokland T, Bella J, Rossmann MG, Estes MK. X-ray crystallographic structure of the Norwalk virus capsid. Science. 1999 Oct 8;286(5438):287-90.  10514371 

Staphylococcus, pathogenicity, virus, assembly, bacteriophages, electron microscopy, crystallography, 3D reconstruction