Lukas K. Tamm, PhD
Graduate School: University of Basel, Switzerland
Primary Appointment: Professor, Molecular Physiology and Biological Physics
Biomembrane Structure and Function; Membrane Fusion in Viral Cell Entry and Exocytosis; Lipid-Protein Interactions
Email Address: firstname.lastname@example.org
Our lab studies the structure and function of several membrane proteins of clinical importance in their natural membrane environment. We are also interested in the roles that membrane lipids play in the regulation of these proteins. Membrane proteins that play key roles in infectious and neurological diseases are of particular interest in our laboratory.
Membrane Fusion in Viral Infection
We investigate the entry of several viruses into cells, including:
- Influenza virus
- Human immunodeficiency virus
- Ebola virus
Membrane Fusion in Neurotransmitter Release
We study the mechanism of neurotransmitter release at the synapse and its regulation by calcium.
- Synaptic exocytosis by SNARE-mediated membrane fusion
- Calcium control by synaptotagmin
- Ultrafast single particle tracking by live-cell microscopy
- Relation to neurological and neurodegenerative diseases
Structure-Function-Dynamics-Antibiotic Interactions of Membrane Channels from Pathogenic Bacteria
Gram-negative bacteria like E. coli and Pseudomonas are enveloped by two membranes. We study channels of the outer membranes of these bacteria and their contribution to antibiotic resistance.
- Gating of OmpA and OmpG from E. coli
- Structure, lipid, and drug interactions of Opr’s from Ps. aeruginosa
- NMR spectroscopy and drug screening
Hong, H., Szabo, G., and Tamm, L.K. (2006) Electrostatic side-chain couplings in the gating of the OmpA ion channel suggest a mechanism for pore opening. Nature Chem. Biol. 11:627-635.
Liang, B. and Tamm, L.K. (2007) Structure of outer membrane protein G by solution NMR. Proc. Natl. Acad. Sci. USA 104:16140-16145.
Ellena, J., Liang, B., Wiktor, M. Cafiso, D.S., Jahn, R., and Tamm, L.K. (2009) Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. Proc. Natl. Acad. Sci. USA 106:20306-20311.
Kiessling, V., Domanska, M.K., and Tamm, L.K. (2010) Single SNARE-mediated vesicle fusion observed in vitro by polarized TIRFM. Biophys. J. 99:4047-4055.
Gregory, S.M., Harada,E., Liang, B., Delos, S.E., Judith M. White, J.M. and Tamm, L.K. (2011) Structure and function of the complete internal fusion loop from Ebolavirus GP2. Proc. Natl. Acad. Sci. USA 108, 11211-11216.
Edrington, T.C., Kintz, E., Goldberg, J.B., and Tamm, L.K. (2011) Structural basis for the interaction of lipopolysaccharide with the outer membrane protein OprH from Pseudomonas aeruginosa. J. Biol. Chem. 286, 39211-39223.
Lai, A.L. Moorthy, A,E., Li, Y, and Tamm, L.K. (2012) Fusion activity of HIV gp41 fusion domain is related to its secondary structure and depth of membrane insertion in a cholesterol-dependent fashion. J. Mol. Biol. 418, 3-15 (on cover).
|Office Address:||PO Box 800886 Snyder Building, Room 355 480 Ray C. Hunt Dr|
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