Characterization of Serracin P, a Phage-Tail-Like Bacteriocin, and Its Activity against
            <i>Erwinia amylovora</i>
            , the Fire Blight Pathogen

Jabrane, A.; Sabri, Ahmed; Compère, Philippe; Jacques, Philippe; Vandenberghe, Isabel; Beeumen, Jozef Van; Thonart, Philippe

doi:10.1128/aem.68.11.5704-5710.2002

Cited by 81 publications

(52 citation statements)

References 42 publications

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“…This raises the possibility that R2 pyocin might restrict the conditions under which P. aeruginosa can grow because the expression of B-band O-antigen synthesis genes must be maintained to resist R2 pyocin-mediated killing. Many bacteria produce HMW or phage tail-like bacteriocins (44)(45)(46)(47)(48)(49)(50)(51)(52), and it is likely that the genes that confer resistance and synthesize the HMW bacteriocin are not genetically linked. These species may also have to balance the benefits of producing HMW bacteriocins with the risks that may pose under certain conditions.…”

Section: Discussionmentioning

confidence: 99%

Biological Cost of Pyocin Production during the SOS Response in Pseudomonas aeruginosa

2014

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bLexA and two structurally related regulators, PrtR and PA0906, coordinate the Pseudomonas aeruginosa SOS response. RecAmediated autocleavage of LexA induces the expression of a protective set of genes that increase DNA damage repair and tolerance. In contrast, RecA-mediated autocleavage of PrtR induces antimicrobial pyocin production and a program that lyses cells to release the newly synthesized pyocin. Recently, PrtR-regulated genes were shown to sensitize P. aeruginosa to quinolones, antibiotics that elicit a strong SOS response. Here, we investigated the mechanisms by which PrtR-regulated genes determine antimicrobial resistance and genotoxic stress survival. We found that induction of PrtR-regulated genes lowers resistance to clinically important antibiotics and impairs the survival of bacteria exposed to one of several genotoxic agents. Two distinct mechanisms mediated these effects. Cell lysis genes that are induced following PrtR autocleavage reduced resistance to bactericidal levels of ciprofloxacin, and production of extracellular R2 pyocin was lethal to cells that initially survived UV light treatment. Although typically resistant to R2 pyocin, P. aeruginosa becomes transiently sensitive to R2 pyocin following UV light treatment, likely because of the strong downregulation of lipopolysaccharide synthesis genes that are required for resistance to R2 pyocin. Our results demonstrate that pyocin production during the P. aeruginosa SOS response carries both expected and unexpected costs.

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Section: Discussionmentioning

confidence: 99%

Biological Cost of Pyocin Production during the SOS Response in Pseudomonas aeruginosa

2014

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“…R-type pyocins present a rodlike structure resembling contractile bacteriophage tails, whereas S-type pyocins are more related to colicins for domain organization (255,317,476,619). The phage-tail-like structure of R-type pyocins is not unique, since other genera produce similar bacteriocins (for example, serracin P from Serratia plymithicum) (293). R-type pyocins adsorb to LPS molecules at the cell surface (287,454) and then penetrate through the outer membrane by a process resembling phage contraction (232) before killing the target bacteria by membrane depolarization (635).…”

Section: Pyocinsmentioning

confidence: 99%

Colicin Biology

Cascales

Buchanan

Duché

et al. 2007

Microbiol Mol Biol Rev

985

1,324

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SUMMARY Colicins are proteins produced by and toxic for some strains of Escherichia coli. They are produced by strains of E. coli carrying a colicinogenic plasmid that bears the genetic determinants for colicin synthesis, immunity, and release. Insights gained into each fundamental aspect of their biology are presented: their synthesis, which is under SOS regulation; their release into the extracellular medium, which involves the colicin lysis protein; and their uptake mechanisms and modes of action. Colicins are organized into three domains, each one involved in a different step of the process of killing sensitive bacteria. The structures of some colicins are known at the atomic level and are discussed. Colicins exert their lethal action by first binding to specific receptors, which are outer membrane proteins used for the entry of specific nutrients. They are then translocated through the outer membrane and transit through the periplasm by either the Tol or the TonB system. The components of each system are known, and their implication in the functioning of the system is described. Colicins then reach their lethal target and act either by forming a voltage-dependent channel into the inner membrane or by using their endonuclease activity on DNA, rRNA, or tRNA. The mechanisms of inhibition by specific and cognate immunity proteins are presented. Finally, the use of colicins as laboratory or biotechnological tools and their mode of evolution are discussed.

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“…Another potentially specific approach for interfering with growth of Erw. amylovora has been the proposed use of Serracin P, a phage-tail-like bacteriocin (Jabrane et al, 2002). In orchards, successful control of fire blight with bacteriophages or bacteriocins has not yet been reported.…”

Section: Introductionmentioning

confidence: 99%

Expression of bacteriophage ϕEa1h lysozyme in Escherichia coli and its activity in growth inhibition of Erwinia amylovora

2004

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A 3·3 kb fragment from Erwinia amylovora phage ϕEa1h in plasmid pJH94 was previously characterized and found to contain an exopolysaccharide depolymerase (dpo) gene and two additional ORFs encoding 178 and 119 amino acids. ORF178 (lyz) and ORF119 (hol) were found to overlap by 19 bp and they resembled genes encoding lysozymes and holins. In nucleotide sequence alignments, lyz had structurally conserved regions with residues important for lysozyme function. The lyz gene was cloned into an expression vector and expressed in Escherichia coli. Active lysozyme was detected only when E. coli cells with the lyz gene and a kanamycin-resistance cassette were grown in the presence of kanamycin. Growth of Erw. amylovora was inhibited after addition of enzyme exceeding a threshold for lysozyme to target cells. When immature pears were soaked in lysates of induced cells, symptoms such as ooze formation and necrosis were retarded or inhibited after inoculation with Erw. amylovora.

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Characterization of Serracin P, a Phage-Tail-Like Bacteriocin, and Its Activity against Erwinia amylovora , the Fire Blight Pathogen

Cited by 81 publications

References 42 publications

Biological Cost of Pyocin Production during the SOS Response in Pseudomonas aeruginosa

Biological Cost of Pyocin Production during the SOS Response in Pseudomonas aeruginosa

Colicin Biology

Expression of bacteriophage ϕEa1h lysozyme in Escherichia coli and its activity in growth inhibition of Erwinia amylovora

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