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DTSTART;TZID=America/Chicago:20260526T121500
DTEND;TZID=America/Chicago:20260526T131500
DTSTAMP:20260513T145320Z
SUMMARY:Microbiology-Immunology Seminar Series: Dr. Laty Cahoon
UID:642094@northwestern.edu
TZID:America/Chicago
DESCRIPTION:Title:  The intrinsically disordered region of the Listeria monocytogenes secretion chaperone PrsA2 is critical for bacterial virulence and client interactions  Decription: While 30-40% of eukaryotic proteins contain at least one intrinsically disordered region (IDR)\, only 4% of bacterial proteins contain IDRs\, therefore investigating these disordered regions is critical for understanding protein function in bacteria. Here\, we use the food-borne pathogen Listeria monocytogenes (Lm) to characterize an IDR within a critical peptidyl-prolyl isomerase (PPIase) chaperone\, PrsA2. Highlighting some of the most important aspects of this work\, we demonstrate that the PrsA2 C-tail IDR is critical for Lm virulence and for the function (interaction and folding) of the major virulence factor and pore forming toxin\, listeriolysin O (LLO). Since the intrinsically disordered nature of this C-tail IDR is conserved in many PrsA homologs; our results may be widely applicable to other important Gram-positive pathogens and adds to the newly expanding characterization of IDRs within bacterial proteomes.
LOCATION:Robert H Lurie Medical Research Center\, Lurie Baldwin Auditorium\, 303 E. Superior\, Chicago\, IL 60611
TRANSP:OPAQUE
URL:https://planitpurple.northwestern.edu/event/642094
CREATED:20260505T050000Z
STATUS:CONFIRMED
LAST-MODIFIED:20260505T050000Z
PRIORITY:0
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