Bacteriocin production by <i>Pseudomonas syringae</i> PsW-1 in plant tissue

Smidt, Mary L.; Vidaver, Anne K.

doi:10.1139/m82-089

Cited by 18 publications

(12 citation statements)

References 16 publications

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“…Our results indicate that toxin production by that organism does not necessarily lead to the production of symptoms. An alternative to the direct role of toxins in disease is the suggestion that toxins are produced by phytopathogenic bacteria to prevent coinfection of a plant by related bacteria (37,47). PTBR 4.000 penetrates and multiplies in intercellular spaces of tobacco leaf tissue to approximately the same level as PTBR 2.024 does, but in contrast to the parent, it does not survive (Fig.…”

Section: (7)mentioning

confidence: 99%

Isolation and characterization of pathogenicity genes of Pseudomonas syringae pv. tabaci

Salch

Shaw

1988

J Bacteriol

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Pseudomonas syringae pv. tabaci BR2 produces tabtoxin and causes wildfire disease on tobacco and bean plants. Approximately 2,700 TnS insertion mutants of a plasmid-free strain, PTBR 2.024, were generated by using suicide plasmid pGS9. Of these Tn5 mutants, 8 were no longer pathogenic on tobacco plants and 10 showed reduced symptoms. All of the eight nonpathogenic mutants caused typical wildfire disease symptoms on bean plants. Two of the nonpathogenic mutants failed to produce tabtoxin. The eight nonpathogenic mutants have TnS insertions into different EcoRI and SailI restriction fragments. The EcoRI fragments containing Tn5 from the eight nonpathogenic mutants were cloned into vector pTZ18R or pLAFR3. A genomic library of the parent strain was constructed in the broad-host-range cosmid pLAFR3. Three different cosmid clones that hybridized to the cloned Tn5-containing fragment from one of the nonpathogenic mutants, PTBR 4.000, were isolated from the genomic library. These clones contained six contiguous EcoRI fragments (a total of 57 kilobases [kb] (29,31).The development of Tn5 mutagenesis and recombinant DNA procedures has provided tools for the isolation and characterization of large numbers of mutant derivatives of phytopathogenic bacteria, defective in various aspects of the pathogenic process (6,28). A number of genes involved in the plant-pathogen interactions have been cloned; examples are pathogenicity genes from P. syringae pv. phaseolicola (25), avirulence genes of P. syringae pv. glycinea (38), and toxin-production genes of P. syringae pv. phaseolicola (30).Little is known about the molecular genetics of pathogenicity mechanisms of P. syringae pv. tabaci, even though the structure of tabtoxin is well established and its inhibition mechanism is well understood (41). Turner and Taha (44) suggested that tabtoxin production is significant in pathogenicity, since their spontaneous nontoxigenic mutants of P. syringae pv. tabaci 11528 were nonpathogenic on tobacco leaves of Nicotiana tabacum cv. White Burley. However, other P. syringae pv. tabaci strains incapable of producing tabtoxin were still pathogenic on tobacco plants (11). Also, nontoxigenic strains of P. syringae pv. phaseolicola were still pathogenic on host plants (30).In this study, a plasmid-free BR2 strain was selected for * Corresponding author.the investigation of pathogenicity traits by using Tn5 mutagenesis and recombinant DNA techniques.(A preliminary report of this study was presented at the Third International Symposium on the Molecular Genetics of Plant-Microbe Interactions, Montreal, Quebec, Canada, 27 to 31 July 1986.) MATERIALS AND METHODS Bacterial strains, plasmids, and culture conditions. The bacterial strains and plasmids used are listed in Table 1. Bacteria were grown in Luria-Bertani broth (LB) (24), King B medium (KB) (23), Vogel-Bonner minimal medium (VB) (49), or M9 medium (5) at 26 or 37°C. Filter-sterilized antibiotics (Sigma Chemical Co.) were added to media at the following concentrations (in micrograms per milliliter...

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Section: (7)mentioning

confidence: 99%

Isolation and characterization of pathogenicity genes of Pseudomonas syringae pv. tabaci

Salch

Shaw

1988

J Bacteriol

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“…Bacteriocin production has also been reported for Halobacteriaceae, a family of extremely halophilic Archaea (36). Bacteriocins constitute a structurally and functionally diverse group within the antimicrobials, ranging from small peptides, such as microcins of Enterobacteriaceae and antibiotics secreted by low-GC-content gram-positive bacteria (23,31), to middle-sized polypeptides, such as colicins of Escherichia coli (34) and their counterparts in Pseudomonas aeruginosa (S pyocins) (39), to large phage tail-like multiprotein complexes, such as syringacin produced by Pseudomonas syringae (58) and R-and F-type pyocins of P. aeruginosa (39). Bacteriocin mode of killing can be either by membrane pore formation, nonspecific degradation of cellular DNA, cleavage of 16S rRNA or tRNA, or inhibition of peptidoglycan synthesis resulting in cell lysis (51).…”

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Novel Lectin-Like Bacteriocins of Biocontrol Strain Pseudomonas fluorescens Pf-5

Parret

Temmerman

Mot

2005

Appl Environ Microbiol

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Bacteria living in a competitive environment are able to secrete proteinaceous toxins, known as bacteriocins, which can kill closely related bacterial competitors while causing little harm to the bacteriocinogenic cells. These bacterial inhibitors are produced by all major groups of Bacteria (53). Bacteriocin production has also been reported for Halobacteriaceae, a family of extremely halophilic Archaea (36). Bacteriocins constitute a structurally and functionally diverse group within the antimicrobials, ranging from small peptides, such as microcins of Enterobacteriaceae and antibiotics secreted by low-GC-content gram-positive bacteria (23, 31), to middle-sized polypeptides, such as colicins of Escherichia coli (34) and their counterparts in Pseudomonas aeruginosa (S pyocins) (39), to large phage tail-like multiprotein complexes, such as syringacin produced by Pseudomonas syringae (58) and R-and F-type pyocins of P. aeruginosa (39). Bacteriocin mode of killing can be either by membrane pore formation, nonspecific degradation of cellular DNA, cleavage of 16S rRNA or tRNA, or inhibition of peptidoglycan synthesis resulting in cell lysis (51).Bacteriocins from lactic acid bacteria, such as nisin, have received considerable attention, given their potential as food preservatives (41, 42). Among bacteriocins of gram-negative bacteria, colicins are the most intensively studied. Colicins are produced by, and attack, strains of E. coli. These proteins, as well as the S pyocins, are organized in functional domains, namely, regions for cell attachment, translocation, and bactericidal activity. Colicins and S pyocins parasitize specific membrane-bound receptors on target cells, resulting in a rather narrow spectrum of activity. The host strain is protected from its own bacteriocin through the action of a cognate immunity protein that is coproduced with the bacteriocin (39, 51).It has been proposed that bacteriocins may play a key role in bacterial population dynamics (52,53). In a recent study, Kirkup and Riley demonstrated that the production of colicins by E. coli colonizing the mouse colon gives the colicinogenic strains a competitive advantage by killing colicin-sensitive E. coli sharing the same ecological niche (33). Possible applications of bacteriocinogenic strains in agriculture include their use in biological control of soilborne or phyllosphere-inhabiting bacterial plant pathogens. In this way, heterologous production of the peptide bacteriocin trifolitoxin by an avirulent Agrobacterium strain effectively enhances biological control of Agrobacterium vitis crown gall (24). Expression of the trifolitoxin genes from Rhizobium leguminosarum bv. trifolii T24 in Rhizobium etli CE3 increases bean nodulation competitiveness of the recombinant strain in the presence of indigenous rhizobia under agricultural conditions (54). A phage tail-like bacteriocin (serracin P) produced by Serratia plymithicum may be used for biological control of fire blight caused by Erwinia amylovora (30), while Xanthomonas campestris pv. glycin...

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“…Because of their wide distribution, pyocins are useful tools for epidemiological studies (54), and because of their chimeric nature, colicins and S-type pyocins are of particular interest for investigating the evolutionary mechanisms involved in bacteriocin diversification (45,49). For plant-associated pseudomonads, research has been focused mainly on plant-pathogenic Pseudomonas syringae strains (24,29,53). In this respect, bacteriocins have potential as biological control agents that can be used against bacterial pathogens (34).…”

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Plant Lectin-Like Bacteriocin from a Rhizosphere-Colonizing Pseudomonas Isolate

et al. 2003

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Rhizosphere isolate Pseudomonas sp. strain BW11M1, which belongs to the Pseudomonas putida cluster, secretes a heat-and protease-sensitive bacteriocin which kills P. putida GR12-2R3. The production of this bacteriocin is enhanced by DNA-damaging treatment of producer cells. We isolated a TnMod mutant of strain BW11M1 that had lost the capacity to inhibit the growth of strain GR12-2R3. A wild-type genomic fragment encompassing the transposon insertion site was shown to confer the bacteriocin phenotype when it was introduced into Escherichia coli cells. The bacteriocin structural gene was identified by defining the minimal region required for expression in E. coli. This gene was designated llpA (lectin-like putidacin) on the basis of significant homology of its 276-amino-acid product with mannose-binding lectins from monocotyledonous plants. LlpA is composed of two monocot mannose-binding lectin (MMBL) domains. Several uncharacterized bacterial genes encoding diverse proteins containing one or two MMBL domains were identified. A phylogenetic analysis of the MMBL domains present in eukaryotic and prokaryotic proteins assigned the putidacin domains to a new bacterial clade within the MMBL-containing protein family. Heterologous expression of the llpA gene also conveyed bacteriocin production to several Pseudomonas fluorescens strains. In addition, we demonstrated that strain BW11M1 and heterologous hosts secrete LlpA into the growth medium without requiring a cleavable signal sequence. Most likely, the mode of action of this lectin-like bacteriocin is different from the modes of action of previously described Pseudomonas bacteriocins.

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Bacteriocin production by Pseudomonas syringae PsW-1 in plant tissue

Cited by 18 publications

References 16 publications

Isolation and characterization of pathogenicity genes of Pseudomonas syringae pv. tabaci

Isolation and characterization of pathogenicity genes of Pseudomonas syringae pv. tabaci

Novel Lectin-Like Bacteriocins of Biocontrol Strain Pseudomonas fluorescens Pf-5

Plant Lectin-Like Bacteriocin from a Rhizosphere-Colonizing Pseudomonas Isolate

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