Bacteriocins and Bacteriocin-Like Substances

Ivánovics, G.

doi:10.1128/mmbr.26.2_pt_1-2.108-118.1962

Cited by 55 publications

(30 citation statements)

References 20 publications

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“…Other Gram-positive bacteria, such as Staphylococcus aureus (Jung and Sahl 1991), Carnobacterium piscicola (Stoffels et al 1992), Streptococcus pyogenes (Jack et al 1994) and Enterococcus faecalis (Maisnier-Patin et al 1996), also produce antibacterial peptides. Within the genus Bacillus, bacteriocins or bacteriocin-like inhibitory substances (BLIS) have been reported from Bacillus subtilis (Jansen and Hirschmann 1944), B. thuringiensis (De Borjac et al 1974), B. stearothermophilus (Shafia et al 1966), B. licheniformis (Bradley 1967), B. megaterium (Ivanovics 1962), B. thermoleovorans (Novotny et al 1992) and B. cereus (Naclerio et al 1993). Spore-forming micro-organisms are responsible for food spoilage, especially Bacillus species.…”

Section: Introductionmentioning

confidence: 99%

Coagulin, a bacteriocin-like inhibitory substance produced by Bacillus coagulans I4

Hyronimus

Marrec²,

Urdaci

1998

Journal of Applied Microbiology

159

106

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A protease‐sensitive antibacterial substance produced by Bacillus coagulans I4 strain, isolated from cattle faeces, was classified as a bacteriocin‐like inhibitory substance and named coagulin. The inhibitory spectrum included B. coagulans and unrelated bacteria such as Enterococcus, Leuconostoc, Oenococcus, Listeria and Pediococcus. Coagulin was stable at 60 °C for 90 min, at a pH ranging from 4 to 8 and appeared to be unaffected by α‐amylase, lipase or organic solvents (10% v/v). Coagulin exhibited a bactericidal and a bacteriolytic mode of action against indicator cells. The apparent molecular mass was estimated to be about 3–4 kDa by SDS‐PAGE. The B. coagulans I4 strain harbours a plasmid, pI4, approximately 14 kb in size. Novobiocin curing experiments yielded two derivatives that no longer produced the bacteriocin‐like inhibitory substance. Plasmid content of these two derivatives showed that one had lost pI4,whereas the second harboured a deleted form of this plasmid, thus suggesting a plasmid location for the genes for coagulin production.

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Section: Introductionmentioning

confidence: 99%

Coagulin, a bacteriocin-like inhibitory substance produced by Bacillus coagulans I4

Hyronimus

Marrec²,

Urdaci

1998

Journal of Applied Microbiology

159

106

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“…Since the initial report, we have detected (unpublished data) bacteriocin activity against C. botulinum type E in filtrates of C. perfringens and C. botulinum types A, B, and E strains as well. Interference of these bacteriocin-producing organisms with methods for the detection or recovery (or both) of toxin-producing type E has been demonstrated (25).The status of our knowledge regarding the bacteriocins has been reviewed frequently (3,9,10,17,21,30,34); the recent reviews of Reeves (34) and Bradley (3) are especially pertinent. Bradley's broad definition of bacteriocins as "bactericidal particles which are unable to multiply in a sensitive indicator" is applied in this report.Many bacteriocinogenic organisms elaborate maximal quantities of bacteriocins only after induction with ultraviolet light, metabolic inhibitors such as mitomycin C, or other agents known to induce lysogenic phages (2,10,13,18,20,24,34,37).…”

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confidence: 99%

“…Bradley's broad definition of bacteriocins as "bactericidal particles which are unable to multiply in a sensitive indicator" is applied in this report.Many bacteriocinogenic organisms elaborate maximal quantities of bacteriocins only after induction with ultraviolet light, metabolic inhibitors such as mitomycin C, or other agents known to induce lysogenic phages (2,10,13,18,20,24,34,37). Some organisms release bacteriocin continuously (11,26); in other cases, an abrupt release of bacteriocin coincides with partial or complete lysis of the culture (11,14,17,20,24).As Bradley (3) pointed out, the bacteriocins studied to date fall into two distinct categories. One group consists of bacteriocins of small molecular size, which are usually thermostable and cannot be sedimented by ultracentrifugation; bacteriocins of very large size, which are usually thermolabile and can be sedimented easily, make up the second group.…”

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confidence: 99%

Purification and Some Properties of Two Boticins

Ellison

Kautter

1970

J Bacteriol

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Two bacteriocins (boticins) were elaborated without induction by strain S5, a nontoxigenic variant of Clostridium botulinum type E. After separation of the two active entities by gel filtration on Sephadex G-50, a large particle with boticin activity was isolated by density gradient ultracentrifugation, and a small soluble boticin was purified by continuous curtain electrophoresis and chromatography on sulfoethyl-Sephadex. Large and small boticins were purified 200-and 3,000-fold, respectively, with yields of 50% or more. The small boticin, a basic substance with molecular weight under 30,000, was the predominant species; the large boticin, a negatively charged particle with particle weight greater than 40 x 106, represented less than 20% of the total activity. Both purified boticins were resistant to heat and were attacked by proteolytic enzymes, but the large boticin was less thermostable and less sensitive to proteolytic enzymes than was the smaller variety. The activity of the large boticin was not reduced by treatment with urea or deoxyribonuclease. Both boticins exhibited sporostatic and bactericidal activities for C. botulinum type E, strain 070. A suspension of type E strain 070 vegetative cells was rendered nonviable within 9 min by the small boticin. The lethal action of this bacteriocin was not reversed by trypsin.The production of bacteriocins (boticins) active against toxigenic Clostridium botulinum type E strains by several closely related but nontoxigenic organisms was described in an earlier report from this laboratory (25). Since the initial report, we have detected (unpublished data) bacteriocin activity against C. botulinum type E in filtrates of C. perfringens and C. botulinum types A, B, and E strains as well. Interference of these bacteriocin-producing organisms with methods for the detection or recovery (or both) of toxin-producing type E has been demonstrated (25).The status of our knowledge regarding the bacteriocins has been reviewed frequently (3,9,10,17,21,30,34); the recent reviews of Reeves (34) and Bradley (3) are especially pertinent. Bradley's broad definition of bacteriocins as "bactericidal particles which are unable to multiply in a sensitive indicator" is applied in this report.Many bacteriocinogenic organisms elaborate maximal quantities of bacteriocins only after induction with ultraviolet light, metabolic inhibitors such as mitomycin C, or other agents known to induce lysogenic phages (2,10,13,18,20,24,34,37). Some organisms release bacteriocin continuously (11,26); in other cases, an abrupt release of bacteriocin coincides with partial or complete lysis of the culture (11,14,17,20,24).As Bradley (3) pointed out, the bacteriocins studied to date fall into two distinct categories. One group consists of bacteriocins of small molecular size, which are usually thermostable and cannot be sedimented by ultracentrifugation; bacteriocins of very large size, which are usually thermolabile and can be sedimented easily, make up the second group. The production of a bacteriocin of each...

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“…Killer strains of certain microorganisms such as bacteria and yeasts that kill other sensitive strains have been reported (8,13,15). Killer strains of yeasts each produce a particular toxin, such as K,, K2 or K3, that kills sensitive strains specifically.…”

Section: Introductionmentioning

confidence: 99%

Cell‐division inhibitor produced by a killer strain of cellular slime mold Polysphondylium pallidum

Mizutani

Yanagisawa

1990

Dev Growth Differ

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The killer strain CK-8 of cellular slime mold Polysphondylium pallidum produces a cell-division inhibitor, in addition to a killer factor. This inhibitor represses cell division of many strains and species of cellular slime molds, except CK-8 itself and its complementary mating-type strain. It is sensitive to both heat and trypsin, and capable of binding to Con A. Its apparent molecular mass is more than 100 kDa. Repression of cell division by this inhibitor is reversed by trypsin treatment of the cells.

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Bacteriocins and Bacteriocin-Like Substances

Cited by 55 publications

References 20 publications

Coagulin, a bacteriocin-like inhibitory substance produced by Bacillus coagulans I4

Coagulin, a bacteriocin-like inhibitory substance produced by Bacillus coagulans I4

Purification and Some Properties of Two Boticins

Cell‐division inhibitor produced by a killer strain of cellular slime mold Polysphondylium pallidum

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