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.
Amelia Crowe
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