title: Protease treatment affects both invasion ability and biofilm formation in Listeria monocytogenes.
abstract: Listeria monocytogenes is a notably invasive bacterium associated with life-threatening food-borne disease in humans. Several surface proteins have been shown to be essential in the adhesion of L. monocytogenes, and in the subsequent invasion of phagocytes. Because the control of the invasion of host cells by Listeria could potentially hinder its spread in the infected host, we have examined the effects of a protease treatment on the ability of L. monocytogenes to form biofilms and to invade tissues. We have chosen serratiopeptidase (SPEP), an extracellular metalloprotease produced by Serratia marcescens that is already widely used as an anti-inflammatory agent, and has been shown to modulate adhesin expression and to induce antibiotic sensitivity in other bacteria. Treatment of L. monocytogenes with sublethal concentrations of SPEP reduced their ability to form biofilms and to invade host cells. Zymograms of the treated cells revealed that Ami4b autolysin, internalinB, and ActA were sharply reduced. These cell-surface proteins are known to function as ligands in the interaction between these bacteria and their host cells, and our data suggest that treatment with this natural enzyme may provide a useful tool in the prevention of the initial adhesion of L. monocytogenes to the human gut.
authors.affiliation: Department of Public Health Sciences, University La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy.
authors.forename: Catia
authors.initials: C
authors.lastname: Longhi
authors.forename: Gian Luca
authors.initials: GL
authors.lastname: Scoarughi
authors.forename: Federica
authors.initials: F
authors.lastname: Poggiali
authors.forename: Andrea
authors.initials: A
authors.lastname: Cellini
authors.forename: Andrea
authors.initials: A
authors.lastname: Carpentieri
authors.forename: Lucilla
authors.initials: L
authors.lastname: Seganti
authors.forename: Pietro
authors.initials: P
authors.lastname: Pucci
authors.forename: Angela
authors.initials: A
authors.lastname: Amoresano
authors.forename: Pier Sandro
authors.initials: PS
authors.lastname: Cocconcelli
authors.forename: Marco
authors.initials: M
authors.lastname: Artini
authors.forename: John W
authors.initials: JW
authors.lastname: Costerton
authors.forename: Laura
authors.initials: L
authors.lastname: Selan
mesh_terms: D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000494:pharmacology*; D001422:Bacterial Adhesion / Q000187:drug effects; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001427:Bacterial Toxins / Q000378:metabolism; D018441:Biofilms / Q000187:drug effects* / Q000254:growth & development; D045744:Cell Line, Tumor; D006360:Heat-Shock Proteins / Q000378:metabolism; D006460:Hemolysin Proteins / Q000378:metabolism; D006801:Humans; D008089:Listeria monocytogenes / Q000737:chemistry / Q000187:drug effects* / Q000235:genetics / Q000502:physiology; D008088:Listeriosis / Q000188:drug therapy / Q000382:microbiology*; D050296:Microbial Viability / Q000187:drug effects; D010447:Peptide Hydrolases / Q000494:pharmacology*; D012706:Serratia marcescens / Q000201:enzymology
chemical_list: D000894:Anti-Inflammatory Agents, Non-Steroidal; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D006360:Heat-Shock Proteins; D006460:Hemolysin Proteins; D010447:Peptide Hydrolases; C022640:serratiopeptidase; C038705:hlyA protein, Listeria monocytogenes