BOSÁK, Juraj, Petra LAIBLOVÁ, Daniela DĚDIČOVÁ, Jan ŠMARDA and David ŠMAJS. Colicin FY – a bacteriocin specifically killing pathogenic strains of Y. enterocolitica. In 22nd European Congress of Clinical Microbiology and Infectious Diseases. 2012.
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Basic information
Original name Colicin FY – a bacteriocin specifically killing pathogenic strains of Y. enterocolitica
Authors BOSÁK, Juraj, Petra LAIBLOVÁ, Daniela DĚDIČOVÁ, Jan ŠMARDA and David ŠMAJS.
Edition 22nd European Congress of Clinical Microbiology and Infectious Diseases, 2012.
Other information
Original language English
Type of outcome Presentations at conferences
Field of Study 10600 1.6 Biological sciences
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
Organization unit Faculty of Medicine
Changed by Changed by: Mgr. Juraj Bosák, Ph.D., učo 106498. Changed: 14/12/2012 11:47.
Abstract
Objectives: Three Yersinia species (out of 17) are important human pathogens - Y. pestis, Y. enterocolitica and Y. pseudotuberculosis. Out of yersiniae, only one bacteriocin, pesticin I, was characterized on a molecular level so far. In this study, we have mapped the production of antimicrobial agents by 53 environmental yersiniae. Results: In the set of yersiniae strains, we have identified 6 bacteriocin producers - Y. frederiksenii (1 strain), Y. intermedia (1 strain) and Y. ruckerii (4 strains). Bacteriocin produced by Y. frederiksenii 27601 was further analyzed. This bacteriocin seems to specifically target yersinia strains, as it does not act against any other tested Enterobacteriaceae (20 strains out of 5 enterobacterial genera have been tested so far). Interestingly, this bacteriocin specifically kills Y. enterocolitica (98%, 45 out of 46 strains tested) in contrast to strains of Y. pseudotuberculosis (0%, 15 strains tested). Among the 53 environmental yersiniae, this bacteriocin was active on 14 strains (24%). Genes encoding the colicin (1317 bp) and immunity protein (338 bp) have been identified on a plasmid. Functional tests revealed its pore forming activity. Moreover, receptor binding domain interacting with yersinia-specific outer membrane protein YiuR was identified together with TonB-system responsible for its translocation. Conclusion: We have described a novel colicin FY, isolated from a strain of Yersinia frederiksenii, its complete plasmid sequence (pYF27601), mechanism of its toxicity, corresponding receptor (YiuR), and translocation routes into a susceptible bacterium. This is the first colicin characterized in detail, active mainly against pathogenic species of Y. enterocolitica.
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