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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 Associate Professor Center  Center for AIDS Research  Center for AIDS Research Associate Professor

Graduate Biomedical Sciences Affiliations Biochemistry and Structural Biology  Microbiology

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  http://asm.org  American Society for Virology  Full member  http://www.mcw.edu/asv/

Research/Clinical Interest Title Structural biology of viral assembly and bacterial pathogenicity Description My lab uses a hybrid approach combining electron microscopy (EM), especially cryo-EM, three-dimensional reconstruction, X-ray crystallography, NMR and other biochemical and biophysical approaches to study the structures of viruses and proteins involved in 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.

Selected Publications  Publication PUBMEDID 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, Epub Jul 29.   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.   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  Chang JR, Spilman MS, Rodenburg CM, Dokland T. Functional domains of the bacteriophage P2 scaffolding protein: identification of residues involved in assembly and protease activity. Virology. 2009 Feb 5;384(1):144-50.  19064277  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  Doan DN, Dokland T. Structure of the nucleocapsid protein of porcine reproductive and respiratory syndrome virus. Structure (Camb). 2003 Nov;11(11):1445-51.   14604534  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  First Prev   1 2 of  2  Next Last

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

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