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Novel pore-forming colicin FY identified in the genus Yersinia

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BOSÁK Juraj FIŠER Radovan KONOPÁSEK Ivo ŠMAJS David

Rok publikování 2012
Druh Konferenční abstrakty
Fakulta / Pracoviště MU

Lékařská fakulta

Citace
Popis In the set of yersinia strains, a novel bacteriocin, produced by Y. frederiksenii 27601, was identified. Its activity spectrum comprises strains of the genus Yersinia, especially strains of Y. enterocolitica. The colicinogenic plasmid pYF27601 (5574 bp) was sequenced and two colicin genes were identified: the colicin FY activity gene (cfyA) and the immunity gene (cfyI). The deduced amino acid sequence of immunity protein and C-terminal sequence of colicin FY revealed high similarity to immunity protein and pore-forming domain of colicin Ib. Colicin FY (54 kDa) was purified and was shown to form a distinct voltage-dependent pore, which is activated by Ca2+ ions. Transposon mutagenesis of susceptible strain Y. kristensenii Y276 revealed the yiuR gene (ykris001_4440) encoding outer membrane protein with siderophore binding function as the colicin FY receptor molecule. Cloning of the gene yiuR to resistant strain Y. kristensenii Y104 resulted in sensitivity to colicin FY. YiuR is similar to Cir protein of Escherichia coli, which is a receptor for colicin Ib. Naturally FY-resistant strains of E. coli acquired susceptibility to colicin FY, when genes yiuR and tonB from the FY-sensitive Y. kristensenii Y276 were introduced. Colicin FY thus belongs to colicin-group B, a group using TonB, ExbB and ExbD proteins to translocate through the bacterial envelope.