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Faculty Detail    
Name TERJE DOKLAND
  
Campus Address BBRB 311 Zip 2170
Phone  (205) 996-4502
E-mail  dokland@uab.edu
Other websites
     

Education
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 Professor
Center  Center for Biophysical Sciences/Engineering  Center for Biophysical Sciences/Engineering Professor
Center  Comprehensive Cancer Center  Comprehensive Cancer Center Professor

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

Biographical Sketch 
Terje Dokland,Professor of Microbiology, received his Ph.D. in 1993 from the University of Oslo, Norway on a joint program with the European Molecular Biology Laboratory in Heidelberg. His Ph.D. work involved cryo-electron microscopy (EM) 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, one of the earliest applications of cryo-EM methods to bacteriophages. From 1994-1998 he did postdoctoral studies with Dr. Michael G. Rossmann at Purdue University where he solved X-ray crystal structures of bacteriophage phiX174 and Norwalk virus. In 1998, Dr. Dokland took up a position as senior scientist at the Institute of Molecular Agrobiology (later to merge with the Institute of Molecular and Cell Biology) in Singapore, where he initiated a structural biology program. He remained in Singapore until April 2004, when he joined the faculty in the Department of Microbiology at UAB. Dr. Dokland is also director of the UAB cryo-EM facility and teaches courses in cryo-EM, structural biology and virology. His outside interests include music (bass player in the band "Burning Vinyl"), oil painting, hiking, kayaking, craft beer and international cooking.

Society Memberships
Organization Name Position Held Org Link
American Society for Microbiology  member  http://asm.org 
Microscopy Society of America  member  http://www.microscopy.org 
 



Research/Clinical Interest
Title
Structural biology of viral assembly and bacterial pathogenicity
Description
My lab uses a hybrid approach combining cryo-EM and three-dimensional reconstruction with other biochemical and biophysical approaches to study the structures of viruses, bacteria and proteins involved in viral and bacterial pathogenicity. Cryo-EM allows imaging and structure determination of macromolecules from proteins to entire cells in their native state. With recent developments in cryo-EM technology, it is now possible to reach near-atomic (<4A) resolution for many types of specimens. As director of the UAB cryo-EM facility, I assist many users across UAB with their EM needs. Our main project is on the bacteriophage-mediated mobilization of Staphylococcus aureus pathogenicity islands (SaPIs). S. aureus is a ubiquitous commensal on human skin and mucosal epithelia, but is also an important 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-EM and 3D reconstruction, X-ray crystallography and NMR. We also apply cryo-EM methods to a range of other collaborative projects on a variety of proteins, viruses, exosomes and prokaryotic cells.

Selected Publications 
Publication PUBMEDID
Kizziah, J.L., Manning, K.A., Dearborn, A.D., Dokland, T. Structure of the host cell recognition and penetration machinery of a Staphylococcus aureus bacteriophage. PLoS Pathog. 2020 Feb 18;16(2):e1008314  32069326 
Manning, KA, Dokland, T. The gp44 ejection protein of Staphylococcus aureus bacteriophage 80a binds to the ends of the genome and protects it from degradation. Viruses. 2020 May 20;12(5):563  32443723 
Manning KA, Quiles-Puchalt N, Penades JR, Dokland T. A novel ejection protein from bacteriophage 80alpha that promotes lytic growth. Virology. 2018 Dec;525:237-247  30308422 
Kizziah JL, Manning KA, Dearborn AD, Wall EA, Klenow L, Hill RLL, Spilman MS, Stagg SM, Christie GE, Dokland T. Cleavage and Structural Transitions during Maturation of Staphylococcus aureus Bacteriophage 80alpha and SaPI1 Capsids. Viruses. 2017 Dec 16;9(12). pii: E384.  29258203 
Dearborn AD, Wall EA, Kizziah JL, Klenow L, Parker LK, Manning KA, Spilman MS, Spear JM, Christie GE, Dokland T. Competing scaffolding proteins determine capsid size during mobilization of Staphylococcus aureus pathogenicity islands. eLife. 2017; e30822.  28984245 
Hill RL, Dokland T. The Type 2 dUTPase of Bacteriophage phiNM1 Initiates Mobilization of Staphylococcus aureus Bovine Pathogenicity Island 1. J Mol Biol. 2016 Jan 16;428(1):142-52.  26585401 
Carpena N, Manning KA, Dokland T, Marina A, Penadés JR. Convergent evolution of pathogenicity islands in helper cos phage interference. Philos Trans R Soc Lond B Biol Sci. 2016 Nov 5;371(1707).  27672154 
Wall EA, Caufield JH, Lyons CE, Manning KA, Dokland T, Christie GE. Specific N-terminal cleavage of ribosomal protein L27 in Staphylococcus aureus and related bacteria. Mol Microbiol. 2015 Jan;95(2):258-69  25388641 
Rodenburg CM, McPherson SA, Turnbough CL Jr, Dokland T. Cryo-EM analysis of the organization of BclA and BxpB in the Bacillus anthracis exosporium. J Struct Biol. 2014 Apr;186(1):181-7  24607412 
Cox R, Pickar A, Qiu S, Tsao J, Rodenburg C, Dokland T, Elson A, He B, Luo M. Structural studies on the authentic mumps virus nucleocapsid showing uncoiling by the phosphoprotein. Proc Natl Acad Sci U S A. 2014 Oct 21;111(42):15208-13  25288750 
Christie GE, Dokland T. Pirates of the Caudovirales
Virology. 2012, 434:210-21 		 23131350 
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 80&#945; capsids. J Mol Biol. 2011, 405(3):863-76.  21129380 
Dokland T. The structural biology of PRRSV.
Virus Res. 2010 Aug 6.  		 20692304 
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.
 		 19218197 
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. 		 15242592 
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 
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.
 		 9305849 
 

Keywords
Staphylococcus, pathogenicity, virus, assembly, bacteriophages, electron microscopy, cryo-EM, crystallography, 3D reconstruction