k 2012

Colicin FY – a bacteriocin specifically killing pathogenic strains of Y. enterocolitica

BOSÁK, Juraj, Petra LAIBLOVÁ, Daniela DĚDIČOVÁ, Jan ŠMARDA, David ŠMAJS et. al.

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

Language

English

Type of outcome

Prezentace na konferencích

Field of Study

10600 1.6 Biological sciences

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

Organization unit

Faculty of Medicine
Změněno: 14/12/2012 11:47, Mgr. Juraj Bosák, Ph.D.

Abstract

V originále

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.