Poster abstracts

Poster number 14 submitted by Kiley Dare

Physiological roles of lipid remodeling by multiple peptide resistance factor (MprF) in Bacillus subtilis 1A100

Kiley Dare (Microbiology, The Ohio State University), Herve Roy (Microbiology, The Ohio State University), Michael Ibba

Abstract:
Multiple peptide resistance factor (MprF) is a membrane bound protein which aminoacylates phophatidylglycerol using an elongator Lys-tRNA^Lys. This lipid modification results in cellular permeability changes that confer resistance to cationic antibiotics and hence constitute a virulence factor in several pathogenic bacteria such as Listeria monocytogenes and Staphylococcus aureus. Previous studies have shown this method of membrane alteration plays an important role in the ability of L. monocytogenes to infect macrophages and epithelial cells. Many aspects of MprF involving pathogen fitness in infection have been studied however the importance of the protein in other physiological processes within the pathogen itself has been overlooked. Recently with the development of Phenotype MicroArrays by Biolog it is possible to perform a high-throughput screen for thousands of phenotypes conferred by a gene. Growth conditions testing phenotypes ranging from cell surface structure and transport functions to stress and repair functions are present in the wells of a microtiter plate that makes it effortless to determine significant effects of a gene on cellular processes. This study employs a Bacillus subtilis 1A100 with a marker-less deletion of mprF to compare to the wild type strain in a Biolog Phenotype MicroArray. Data obtained from this comparison sheds light on other roles of lipid remodeling in general cellular physiology in B. subtilis.

Keywords: MprF, lipid remodeling, tRNA