Clarissa Durie, PhD

Assistant Professor

Biochemistry

Contact Information

Email Clarissa.durie@missouri.edu
Phone 573-882-5377
Address 117 Schweitzer

Education

  • BBA, Marketing, College of William and Mary, Williamsburg, Virginia
  • BS, Chemistry, University of Alabama at Birmingham, Birmingham, Alabama
  • PhD, Chemistry, University of Alabama at Birmingham, Birmingham, Alabama

Research Area

Protein complex structure & function in bacterial pathogenesis: Cryo-EM, protein translocation, enzyme kinetics

Research Description

Cells must interface with and adapt to the outside world, and one critical way they achieve this is through the dynamic and specific action of secretion systems that transport molecules in and out of cells. Over the last several decades, scientists have identified numerous cellular secretion systems from bacteria to human. However, there are still many unanswered questions about precisely how and when they function. The goal of my research program is to integrate biochemical, biophysical, and genetic approaches to understand the structure, regulation, and function of bacterial secretion systems in their physiological contexts.

Bacterial pathogens represent a significant threat to global health, exacerbated by growing drug resistance. Although pathogens use diverse strategies to infect hosts, one common obstacle that all pathogenic bacteria must overcome is moving virulence factors across multiple membrane barriers: their own and the host cell’s. For example, many bacterial pathogens secrete diverse molecules into hosts or the extracellular space to promote growth and survival through the type IV secretion system (T4SS).

The components used by bacteria to move virulence factors across membrane have been thoroughly catalogued, but our mechanistic understanding of how these components physically work lags behind. One major focus of my research program will be to advance our fundamental mechanistic understanding of how secretion systems couple chemical energy to mechanical work, allowing us to identify and target the “Achilles heel” of these molecular machines with an ultimate goal of blocking pathogenesis. Furthermore, the delivery of diverse molecules can be differentially regulated by the environment or according to bacterial lifecycle stage, implicating secretion as a key way for bacteria to broadly and quickly tune their interactions with the outside world. Thus, a second major question my research program will address is: how do bacteria regulate secretion to adapt to changing needs over their lifecycle?

My research group will investigate complex cellular machinery by integrating biochemical, biophysical (including state of the art cryo-electron microscopy), and genetic approaches to shed new light on our understanding of the fundamental process of translocation across membrane, a necessary process for all cells, as well as how we think about bacterial pathogenesis.

Notable Honors and Service

  • 2020 University of Michigan, Cell & Developmental Biology, Bradley M. Patten Award for Excellence in Postdoctoral Research
  • 2020 Fellow, HHMI Leading Edge Symposium
  • 2019 University of Michigan, Life Sciences Institute, Outreach Award
  • 2018 – 2020 STEM in Color; Executive Board Member & Communications Chair

Selected Publications

  • Sheedlo, M. J.*; Durie, C. L.*; Chung, J. M.; Chang, L.; Roberts, J.; Swanson, M. S.; Lacy, B. D.; Ohi, M. D., Cryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS. eLife, 2021; 10:e70427
  • Williamson, L. E.; Gilliland, T.; Yadav, P.; Binshtein, E.; Bombardi, R.; Kose, N.; Nargi, R.S.; Sutton, M. S.; Durie, C. L.; Armstrong, E.; Carnahan, R. H.; Walker, L. M.;Kim, A. S.; Fox, J. M.; Diamond, M. S.; Ohi, M. D.; Klimstra, W. B.; Crowe, J. E., Human antibodies protect against aerosolized eastern equine encephalitis virus infection. Cell. 2020, 183 1-17
  • Durie, C. L.*; Sheedlo, M. J.*; Chung, J. M.; Byrne, B. G.; Su, M.; Knight, T.; Swanson, M. S.; Lacy, B. D.; Ohi, M. D., Structural analysis of the Legionella pneumophila Dot/Icm type IV secretion system core complex. eLife, 2020; 9:e59530
  • Sheedlo, M. J.*; Chung, J. M.*; Sawhney, N.; Durie, C. L.; Cover, T. L.; Ohi, M. D.; Lacy, B. D., Cryo-EM reveals species-specific components within the Helicobacter pylori Cag type IV secretion system core complex. eLife, 2020; 9:e59495
  • Durie, C. L.; Lin, J.; Scull, N., Mack, K. L.; Jackrel, M. E.; Sweeny, E.; Castellano, L.; Shorter, J.; Lucius, A. L., Hsp104 and Potentiated Variants Can Operate as Distinct Non-processive Translocases. Biophysical Journal. 2019, 116 (10),1856-1872.
  • Durie, C. L., Duran, E. C., Lucius, A. L., Eschericichia coli DnaK Allosterically Modulates ClpB between High- and Low-Peptide Affinity States. Biochemistry. 2018, 57 (26), 3665-3675.
  • Duran, E. C.; Weaver, C. L.; Lucius, A. L., Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104. Front Mol Biosci. 2017 4:54
  • Weaver, C. L.; Duran, E. C.; Mack, K. L.; Lin, J.; Jackrel, M. E.; Shorter, J.; Lucius, A. L., Avidity for polypeptide binding by nucleotide-bound Hsp104 structures. Biochemistry 2017, 56 (15), 2071-2075.
  • Wang, P.; Li, J.; Weaver, C.; Lucius, A; Sha, B., Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 dissolving prions. Acta Crystallography 2017, D73, 365-3472.
  • Li, T.; Weaver, C. L.; Lin, J.; Duran, E. C.; Miller, J. M.; Lucius, A. L., Escherichia coli ClpB is a non-processive polypeptide translocase. The Biochemical Journal 2015, 470 (1), 39-52.
  • Weaver, L., Duran, E. C., Nikles, J. A., An Integrated Approach for Development of Scientific Writing Skills in Undergraduate Organic Lab. In Addressing the Millennial Student in Undergraduate Chemistry, American Chemical Society: 2014; Vol. 1180, pp 105-123.