Gram-positive bacteria are causative agents of serious and often fatal infections in both hospital and community settings, however many fundamental aspects of their physiology and pathogenesis remain poorly studied in comparison to their Gram-negative counterparts. The fundamental process of Gram-positive protein secretion, critical for the delivery of virulence factors, is one of these largely understudied physiological facets. My research has focused on post-translocation secretion chaperones in the human Gram-positive pathogens Listeria monocytogenes and Streptococcus pneumoniae so as to better understand the processes underlying protein secretion, folding, and activity following membrane translocation. Defining paradigms of Gram-positive protein secretion will ultimately enable the design of therapeutic strategies that both inhibit virulence factor secretion and increase antibiotic susceptibility by targeting essential exposed components of the bacterial cell surface.
- Assistant Professor
- Host-pathogen Interactions
Light SH, Cahoon LA, Mahasenan KV, Lee M, Boggess B, Halavaty AS, Mobashery S, Freitag NE, Anderson WF. 2017. Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity. Structure 2017 25(2):295-304
Light SH, Cahoon LA, Halavaty AS, Freitag NE, Anderson WF. 2016. Structure to function of an α-glucan metabolic pathway that promotes Listeria monocytogenes pathogenesis, Nature Microbiology 2:16202
Cahoon LA, Freitag NE, Prehna G. 2016. A structural comparison of Listeria monocytogenes protein chaperones PrsA1 and PrsA2 reveals molecular features required for virulence, Molecular Microbiology 101(1):42-61
Cahoon LA, Freitag NE. 2015. Identification of Conserved and Species-Specific Functions of the Listeria monocytogenes PrsA2 Secretion Chaperone, Infection and Immunity 83(10):4028-41
Cahoon LA, Freitag NE. 2014. Listeria monocytogenes virulence factor secretion: don’t leave the cell without a chaperone, Frontiers in Cellular and Infection Microbiology 4(13):1-10
Cahoon LA, Manthei KA, Rotman E, Keck JL, Seifert HS. 2013. The Neisseria gonorrhoeae RecQ helicase HRDC domains are essential for efficient binding and unwinding of the pilE guanine quartet structure required for pilin Av. Journal of Bacteriology195(10):2255-61
Dr. Cahoon received her Ph.D. in 2012 with Hank Seifert at Northwestern University, performed her postdoctoral studies with Nancy Freitag at the University of Illinois at Chicago, and joined the Department in 2020.