Faculty / Research
Membrane biosynthesis, structure & behavior in bacterial pathogenesis
Lipid membranes define the boundaries of life. Membranes thus determine how a cell communicates with its environment. The integrity and surface properties of membranes are particularly important in hostile environments such as those experienced by bacterial pathogens inside their hosts. While eukaryotic lipid membranes have been extensively studied and modeled, comparatively little is understood about the membranes of pathogens such as Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis.
Mtb generates many structurally complex and unusual lipids that have received little molecular-level scrutiny in the membrane context. The JSeeliger group will pursue two major questions that address these issues:
How are bacterial lipid membranes synthesized and
How do unique bacterial lipids affect membrane properties?
This research will include the synthesis of chemical biological probes; the investigation of protein-protein interactions and enzyme mechanism; screens for proteins with novel function; and biophysical characterization of novel model membrane systems. These studies will provide a new perspective on how Mtb exploits its membrane structure and composition to interact with its human host environment. The results could impact how we design antibiotic therapies against Mtb and other bacterial pathogens.
Jessica received her A. B. in Chemistry from Harvard University in 2000, her MPhil in Chemistry from the University of Cambridge in 2001, and her Ph. D. in Chemistry from Stanford University in 2007. She moved to the University of California, Berkeley, in 2007 as a postdoctoral fellow with Carolyn Bertozzi and in Fall 2010 started her lab in the Department of Pharmacological Sciences at Stony Brook University.
For the most current list, see this PubMed search.
Selected publications (also under
Seeliger, J. C., Topp, S., Sogi, K. M., Previti, M. L., Gallivan, J. P., Bertozzi, C. R. A Riboswitch-Based Inducible Gene Expression Platform for Mycobacteria. PLoS One, in press.
Seeliger, J. C., Holsclaw, C. M., Schelle, M. W., Botyzanszki, Z., Gilmore, S. A., Tully, S. E., Niederweis, M., Cravatt, B. F., Leary, J. A., Bertozzi, C. R. Elucidation and Chemical Modulation of Sulfolipid-1 Biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem., in press.
Topp, S., Reynoso, C. M. K., Seeliger, J. C., Goldlust, I. S., Desai, S. K., Murat, D., Shen, A., Puri, A. W., Komeili, A., Bertozzi, C. R., Scott, J. R., Gallivan, J. P. (2010) Synthetic Riboswitches that Induce Gene Expression in Diverse Bacterial Species. Appl. Environ. Microbiol. 76, 7881-7884.
Chuang, J. I., Boxer, S. G., Holten, D., Kirmaier, C. (2008) Temperature Dependence of Electron Transfer to the M-side Bacteriopheophytin in Rhodobacter capsulatus Reaction Centers. J. Phys. Chem. B. 112, 5487-5499.
Fafarman, A., Webb, L. J., Chuang J. I., Boxer S. G. (2006) Site-Specific Conversion of Cysteine Thiols into Thiocyanate Creates an IR Probe for Electric Fields in Proteins. J. Amer. Chem. Soc. 128, 13356-13357.
Chuang, J. I., Boxer, S. G., Holten, D., Kirmaier, C. (2006) High Yield of M-side Electron Transfer in Mutants of Rhodobacter capsulatus Reaction Centers Lacking the Initial Electron Acceptor Bacteriopheophytin. Biochemistry 45, 3845-3851.
Khan, F., Chuang, J. I., Gianni, S., Fersht, A. R. (2003) The kinetic pathway of folding of barnase. J. Mol. Biol. 333, 169-86.
|Megan Himmler||Graduate Student, Chemistry/Chemical Biologyfirstname.lastname@example.org|
|Mary Lou Previti||Research Support Specialistemail@example.com|
Office location: 448 Centers for Molecular Medicine
Lab location: 435 Centers for Molecular Medicine
Lab phone: 631-632-4144