J Bacteriol 2002, 184:2857–2862.CrossRefPubMed 45. Carattoli A, Bertini A, Villa L, Falbo V, Hopkins KL, Threlfall EJ: Identification of plasmids by PCR-based replicon typing. J Microbiol Methods 2005, 63:219–228.CrossRefPubMed Authors’ contributions CC designed, instructed and supervised most aspects of this project. CSC did PFGE analysis and prepared the manuscript. JML and SWC performed the experiments and data analysis. CHC, BCW and JGT assisted in the design of the study and helped to prepare the manuscript. CLC, CHC, and CHL gave useful comments and critically read the manuscript. YFC edited and revised the manuscript. All authors read and approved the final manuscript.”
“Background

Serratia marcescens Akt inhibitor is widely distributed in natural environments and has emerged in the last two decades as an important nosocomial pathogen, mainly in immunocompromised patients [1, 2]. Although S. marcescens pathogenicity is poorly understood, Berzosertib chemical structure its extracellular secreted enzymes, including several types of proteases, are candidates for virulence factors [2]. Other factors (e.g., fimbria for adhesion, lipopolysaccharide (LPS), and ShlA hemolysin) have also been suggested as virulence factors [2, 3]. Hemolysins are produced

by various pathogenic bacteria and have been proposed to be responsible for their pathogenesis [4–6]. These hemolysins, including S. marcescens ShlA, also have cytolytic activity [7]. One type of hemolysin/cytolysin is a group of pore-forming toxins. This type of toxin typically forms a homo-10058-F4 datasheet oligomer integrated into its target cell Urease membrane, thereby changing the cell permeability and leading to cell death. ShlA has been shown to increase cell membrane permeability, but not to form an oligomer [3]. Another type of hemolysin

has phospholipase C (PLC) activity. The α-toxin produced by Clostridium perfringens is the most thoroughly investigated PLC, but the molecular mechanism for its disruption of red blood cells (RBC) is not fully understood [8]. The pathogenic effects of other types of phospholipases, such as phospholipase A (PLA), have been studied in various bacteria, including Helicobacter pylori (PldA) [9], Legionella pneumophila (PlaA) [10], Campylobacter coli (PldA) [11], and Yersinia enterocolitica (YplA) [12]. Two extracellular PLAs, PhlA and PlaA, have been described previously in Serratia species [13, 14]. PlaA is produced in Serratia sp. strain MK1 isolated from Korean soil [14]. The amino acid sequence of PlaA was found to have significant similarity (80%) to PhlA from S. marcescens MG1, which was originally classified as S. liquefaciens [13–15]. However, the cytotoxic and hemolytic activities of these enzymes have remained unclear, and the importance of PLA in bacterial virulence is not well understood. S.