Isolation and characterization of syringacin W-1, a bacteriocin produced by <i>Pseudomonas syringae</i> pv. <i>syringae</i>

Smidt, Mary L.; Vidaver, Anne K.

doi:10.1139/m86-046

Cited by 19 publications

(17 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Weil-diffusion assays conducted in the presence of iron-supplemented media showed inhibitory activity similar to that determined without integration (data not shown), excluding the role of siderophores in the antimicrobial activity of Pfluorescens ATCC 948. An antagonism linked to bacterial viruses contained in the extracellular culture filtrate has been shown in pseudomonads (Vidaver, 1983;Smidt and Vidaver, 1986) and other microbial species (De Klerk and Coetzee 1961;Betz and Anderson, 1964;Hamada and Ooshima, 1975). Dilutions of the antimicrobial preparation from P fluorescens ATCC 948 produced smaller zones of inhibition and did not increase plaque formation (data not shown), thus also excluding the presence of viruses in the culture supernatant.…”

Section: Discussionmentioning

confidence: 71%

“…The proteinaceous nature of the antimicrobial compound purified in this study, together with the high molecular mass and the absence of carbohydrate and lipid moities (treatments with acetone and nbutanol did not modify the inhibitory activity of P fluorescens ATCC 948 supematant) (Iacobellis et al, 1992) seem to exclude the compound from this category. Bacteriocins with features quite similar to those determined for the antimicrobial compound produced by P fluorescens ATCC 948 (active protein moiety, molecular mass of -60 kDa, optimal production at 20 "C and a certain degree ofthermostability) have been shown in P syringae pv syringae (Smidt and Vidaver, 1986), P syringae susbp savastanoi (lacobellis et al, 1995), P solanacearum (Cuppels et al, 1978), P phaseolicola and P glycinea (Vidaver et al, 1972). By comparing these studies, the main difference lies in a narrower spectrum of activity, in sorne cases species-specific, which characterizes the isolated bacteriocins.…”

Section: Discussionmentioning

confidence: 79%

“…Siderophores, pterines, indoles, phenazynes, lipids, peptides and bacteriocins are produced by Pseudomonas spp strains and have been extensively studied for their antimicrobial activity in the biocontrol of plant diseases (Dowling and 0' Gara, 1994). Bacteriocins from P glycinea, P phaseolicola (Vidaver et al, 1972), P syringae pv syringae (Smidt and Vidaver, 1986), P syring ae subsp savastanoi (Iacobellis et al, 1995), P solanacearum (Cuppels et al, 1978) and P fluorescens (Reeves, 1965) have been isolated and characterized. A narrow spectrum of activity, in particular shown against important plant pathogens, is a corn mon feature of pseudomonad bacteriocins: several studies (Cuppels et al, 1978;Iacobellis et al, 1995) have shown a species-specific inhibition.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Purification and characterization of a proteinaceous compound from Pseudomonas fluorescens ATCC 948 with inhibitory activity against some Gram-positive and Gram-negative bacteria of dairy interest

Gobbetti¹,

Corsetti²,

Smacchi³

et al. 1997

Lait

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 71%

Section: Discussionmentioning

confidence: 79%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Purification and characterization of a proteinaceous compound from Pseudomonas fluorescens ATCC 948 with inhibitory activity against some Gram-positive and Gram-negative bacteria of dairy interest

Gobbetti¹,

Corsetti²,

Smacchi³

et al. 1997

Lait

View full text Add to dashboard Cite

“…Syringacins 4-A and W-1 are high-molecular-weight and heatsensitive bacteriocins identified and purified from two strains of Pseudomonas syringae pv. syringae isolated from corn and beans, respectively (5,17). Applicative studies on disease control using bacteriocin-producing bacteria have also been reported (1,13).…”

mentioning

confidence: 99%

Reduction of Olive Knot Disease by a Bacteriocin from Pseudomonas syringae pv. ciccaronei

Lavermicocca¹,

Lonigro²,

Valerio³

et al. 2002

Appl Environ Microbiol

View full text Add to dashboard Cite

A bacteriocin produced by Pseudomonas syringae pv. ciccaronei, used at different purification levels and concentrations in culture and in planta, inhibited the multiplication of P. syringae subsp. savastanoi, the causal agent of olive knot disease, and affected the epiphytic survival of the pathogen on the leaves and twigs of treated olive plants. Treatments with bacteriocin from P. syringae pv. ciccaronei inhibited the formation of overgrowths on olive plants caused by P. syringae subsp. savastanoi strains PVBa229 and PVBa304 inoculated on V-shaped slits and on leaf scars at concentrations of 10 5 and 10 8 CFU ml ؊1 , respectively. In particular, the application of 6,000 arbitrary units (AU) of crude bacteriocin (dialyzed ammonium sulfate precipitate of culture supernatant) ml ؊1 at the inoculated V-shaped slits and leaf scars resulted in the formation of knots with weight values reduced by 81 and 51%, respectively, compared to the control, depending on the strains and inoculation method used. Crude bacteriocin (6,000 AU ml ؊1 ) was also effective in controlling the multiplication of epiphytic populations of the pathogen. In particular, the bacterial populations recovered after 30 days were at least 350 and 20 times lower than the control populations on twigs and on leaves, respectively. These results suggest that bacteriocin from P. syringae pv. ciccaronei can be used effectively to control the survival of the causal agent of olive knot disease and to prevent its multiplication at inoculation sites.

show abstract

“…glycines was first reported by Fett et al (5), who chose the term glycinecin to differentiate the X. campestris bacteriocin from the glycin produced by P. syringae pv. glycinea (21). Previously, X. campestris pv.…”

mentioning

confidence: 99%

gly Gene Cloning and Expression and Purification of Glycinecin A, a Bacteriocin Produced by Xanthomonas campestris pv. glycines 8ra

Heu¹,

Kang

et al. 2001

Appl Environ Microbiol

View full text Add to dashboard Cite

Glycinecin A, a bacteriocin produced by Xanthomonas campestris pv. glycines, inhibits the growth of X. campestris pv. vesicatoria. We have cloned and expressed the genes encoding glycinecin A in Escherichia coli. Recombinant glycinecin A was purified from cell extracts by ammonium sulfate precipitation followed by chromatography on Q-Sepharose, Mono Q (ion exchange), and size exclusion columns. Purified glycinecin A is composed of two polypeptides, is active over a wide pH range (6 to 9), and is stable at temperatures up to 60°C. Glycinecin A is a heterodimer consisting of 39-and 14-kDa subunits, as revealed through size exclusion chromatography and cross-linking analysis. Two genes, glyA and glyB, encoding the 39-and 14-kDa subunits, respectively, were identified based on the N-terminal sequences of the subunits. From the nucleotide sequences of glyA and glyB, we conclude that both genes are translated as bacteriocin precursors that include N-terminal leader sequences. When expressed in E. coli, recombinant glycinecin A was found primarily in cell extracts. In contrast, most glycinecin A from Xanthomonas was found in the culture media. E. coli transformed with either glyA or glyB separately did not show the bacteriocin activity.Bacteriocins are bactericidal compounds, usually proteinaceous, whose activities are often restricted to bacterial strains that are closely related to the producing bacterium (6, 23). Bacteriocins are produced in all major groups of Eubacteria and Archaebacteria (22). Some bacteriocins, the halocins from Halobacteria, have no protein sequence homology to any known bacteriocins (20), whereas others, such as the S-type pyocins of Pseudomonas aeruginosa, some of the colicins of Escherichia coli, and a cloacin of Enterobacter cloacae, reveal protein sequence homologies (16,17,19).Despite their diversity, the bacteriocins share several characteristics (6, 23). They are generally high-molecular-weight proteins that gain entry into target cells by binding to cell surface receptors. Their bactericidal mechanisms vary and include pore formation, degradation of cellular DNA, disruption of specific cleavage of 16S rRNA, and inhibition of peptidoglycan synthesis.Many phytopathogenic bacteria, including members of the corynebacteria, erwinias, pseudomonads, and xanthomonads, produce proteinaceous bacteriocins (1, 2, 4, 5, 21, 24, 25). Since these bacteriocins are highly specific, can be produced at low cost, and are likely to be safe for both users and the environment, they appear to be excellent candidates for agricultural use in controlling plant pathogens. However, little is known about the chemical compositions, structures, modes of action, and genetics of most bacteriocins. Only a few isolated and/or purified bacteriocins have been reported from Agrobacterium radiobacter (18), Corynebacterium ulcerans (1), Erwinia carotovora subsp. carotovora (4), and Pseudomonas syringae pv. syringae (21).Thus far, bacteriocin production by xanthomonads has received little attention. Bacteriocin production by X...

show abstract

Isolation and characterization of syringacin W-1, a bacteriocin produced by Pseudomonas syringae pv. syringae

Cited by 19 publications

References 0 publications

Purification and characterization of a proteinaceous compound from Pseudomonas fluorescens ATCC 948 with inhibitory activity against some Gram-positive and Gram-negative bacteria of dairy interest

Purification and characterization of a proteinaceous compound from Pseudomonas fluorescens ATCC 948 with inhibitory activity against some Gram-positive and Gram-negative bacteria of dairy interest

Reduction of Olive Knot Disease by a Bacteriocin from Pseudomonas syringae pv. ciccaronei

gly Gene Cloning and Expression and Purification of Glycinecin A, a Bacteriocin Produced by Xanthomonas campestris pv. glycines 8ra

Contact Info

Product

Resources

About