title: LysPGS formation in Listeria monocytogenes has broad roles in maintaining membrane integrity beyond antimicrobial peptide resistance.
abstract: Listeria monocytogenes is an intracellular, foodborne gastrointestinal pathogen that is primarily responsible for causing listeriosis or food poisoning in otherwise healthy individuals. Infections that arise during pregnancy or within immune compromised individuals are much more serious resulting in the risk of fetal termination or fetal fatality postpartum in the former and septicemia or meningitis with a 20% fatality rate in the latter. While the roles of internalin proteins and listeriolysin-O in the infection process are well characterized, the specific roles of lysine-modified phospholipids in the membrane of L. monocytogenes are not. Investigation into the lipid bilayer composition of L. monocytogenes indicated that the overall proportions of lipids, including lysylcardiolipin and lysylphosphatidylglycerol (LysPG), vary with growth temperature and growth phase. In addition, we demonstrate that LysPG formation is essential for L. monocytogenes survival in the presence of increased osmolytic stress but has no effect on bacterial adherence, invasion or survival in the presence of physiologically relevant concentrations of human neutrophil peptide (HNP-1). In the absence of LysPG synthesis, L. monocytogenes unexpectedly retained flagellum-mediated motility at 37 °C. Taken together, these findings show that LysPG formation in L. monocytogenes has broader functions in virulence and survival beyond its known role in the modification of membrane potential previously observed in other bacteria.
authors.affiliation: Department of Microbiology; The Ohio State University; Columbus, OH USA.
authors.forename: Kiley
authors.initials: K
authors.lastname: Dare
authors.affiliation: Department of Microbiology; The Ohio State University; Columbus, OH USA.
authors.forename: Jennifer
authors.initials: J
authors.lastname: Shepherd
authors.affiliation: Department of Microbiology; The Ohio State University; Columbus, OH USA.
authors.forename: Hervé
authors.initials: H
authors.lastname: Roy
authors.affiliation: Department of Microbiology; The Ohio State University; Columbus, OH USA.
authors.forename: Stephanie
authors.initials: S
authors.lastname: Seveau
authors.affiliation: Department of Microbiology; The Ohio State University; Columbus, OH USA; Ohio State Biochemistry Program; Center for RNA Biology; The Ohio State University; Columbus, OH USA.
authors.forename: Michael
authors.initials: M
authors.lastname: Ibba
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D024881:Drug Resistance, Bacterial; D006801:Humans; D008089:Listeria monocytogenes / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism* / Q000472:pathogenicity; D008088:Listeriosis / Q000382:microbiology*; D008239:Lysine / Q000378:metabolism*; D010715:Phosphatidylglycerols / Q000378:metabolism*; D014774:Virulence
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins; D010715:Phosphatidylglycerols; C002285:lysylphosphatidylglycerol; D008239:Lysine
keywords: Listeria; aminoacyl-tRNA; lipid; membrane; multiple peptide resistance factor; phosphatidylglycerol