Lukas K. Tamm
- Grad Res, Cornell University
- Dipl Biol II, University of Basel
- PhD, University of Basel
- Postdoc-Res, Stanford University
- Professor, Molecular Physiology and Biological Physics
- Phone: 434-982-3578; 434-982-3281
- Email: firstname.lastname@example.org
- Website: https://med.virginia.edu/tamm-lab/
Biomembrane Structure and Function; Cell Entry of Enveloped Viruses; Neurosecretion by Exocytosis; Structure of Bacterial Pathogen Membrane Proteins; Lipid-Protein Interactions
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.
We investigate the entry of several enveloped viruses into cells, including influenza virus, human immunodeficiency virus, and Ebola virus. The mechanism of membrane fusion in this process is of particular interest.
We study the mechanism of neurotransmitter release at the synapse and its regulation by calcium. We are interested in elucidating the mechanism of synaptic exocytosis by SNARE-mediated membrane fusion and the calcium control of this process by synaptotagmin. To this end, we use life-cell microscopy and ultrafast single particle tracking. The outcomes of these studies help to better understand neurological and neurodegenerative diseases.
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. Of particular interest is to understand and control the gating of the nanopores of OmpA from E. coli. Studies on the structure, lipid, and drug interactions OprG and OprH from Pseudomonas aeruginosa will help to understand the high antibiotic resistance of this serious human pathogen.
- Liang B, Tamm L. NMR as a tool to investigate the structure, dynamics and function of membrane proteins. Nature structural & molecular biology. 2016;23(6): 468-74. PMID: 27273629
- Yang S, Kiessling V, Tamm L. Line tension at lipid phase boundaries as driving force for HIV fusion peptide-mediated fusion. Nature communications. 2016;7 11401. PMID: 27113279 | PMCID: PMC4853434
- Kucharska I, Seelheim P, Edrington T, Liang B, Tamm L. OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa. Structure (London, England : 1993). 2015;23(12): 2234-45. PMID: 26655471 | PMCID: PMC4699568
- Yang S, Kiessling V, Simmons J, White J, Tamm L. HIV gp41-mediated membrane fusion occurs at edges of cholesterol-rich lipid domains. Nature chemical biology. 2015;11(6): 424-31. PMID: 25915200 | PMCID: PMC4433777
- Liang B, Kiessling V, Tamm L. Prefusion structure of syntaxin-1A suggests pathway for folding into neuronal trans-SNARE complex fusion intermediate. Proceedings of the National Academy of Sciences of the United States of America. 2013;110(48): 19384-9. PMID: 24218570 | PMCID: PMC3845119
- Gregory S, Harada E, Liang B, Delos S, White J, Tamm L. Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2. Proceedings of the National Academy of Sciences of the United States of America. 2011;108(27): 11211-6. PMID: 21690393 | PMCID: PMC3131375