The biology of colicin M

Harkness, R

doi:10.1016/0378-1097(91)90694-6

Cited by 8 publications

(8 citation statements)

References 62 publications

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“…As these cells were in TSBYE, i.e., a nonhypertonic medium, it was not surprising that they were prone to lysis. Linenscin OC2 seems to have a mode of action similar to that of certain bacteriocins produced by gram-negative bacteria such as colicin M and pesticin (10,19) and some antibiotics such as cycloserine and bacitracin (25), whose effect is to inhibit peptidoglycan formation.…”

Section: Resultsmentioning

confidence: 99%

Activity and purification of linenscin OC2, an antibacterial substance produced by Brevibacterium linens OC2, an orange cheese coryneform bacterium

Maisnier‐Patin

Richard

1995

Appl Environ Microbiol

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An orange cheese coryneform bacterium isolated from the surface of Gruyère of Comté and identified as Brevibacterium linens produces an antimicrobial substance designated linenscin OC2. This compound inhibits gram-positive food-borne pathogens including Staphylococcus aureus and Listeria monocytogenes but is not active against gram-negative bacteria. Linenscin OC2 caused viability loss and lysis of the test organism, Listeria innocua. Electron microscopy showed that linenscin OC2 induces protoplast formation and cell lysis. The native substance is resistant to proteolytic enzymes, heat, and organic solvents and stable over a wide range of pH. The molecular weight of the native linenscin OC2 was estimated by gel chromatography to be over 285,000. Linenscin OC2 was purified by ammonium sulfate precipitation, 2-propanol extraction, and reversephase chromatography. Direct detection of antimicrobial activity on a sodium dodecyl sulfate-polyacrylamide gel suggested an apparent molecular mass under 2,412 Da. Molecular mass was determined to be 1,196.7 Da by mass spectrometry. Amino acid composition analysis indicated that linenscin OC2 may contain 12 residues. Listeria monocytogenes has been recognized as a major foodborne pathogen since the outbreaks in California and Switzerland (5) involving cheeses. L. monocytogenes has the ability to withstand various environmental conditions, such as low pH (7, 26) and salt concentration of up to 10% (24). It is, therefore, not surprising that Listeria organisms can survive in various kinds of fermented products such as cheeses (32). Moreover, they can resume growth during the ripening of surface-ripened soft and semihard cheeses as a result of a pH rise (30, 31). Thus, any studies on antagonistic systems that could prevent growth of this organism in cheese are of great interest. Lactic acid bacteria produce several antagonistic systems such as hydrogen peroxide, diacetyl, organic acids, and bacteriocins (27). Only the latter substances seem to have a real practical interest. However, a few of them are active against food-borne pathogens such as Listeria organisms: nisin produced by Lactococcus lactis (15), mesenterocins or leucocins produced by Leuconostoc mesenteroides (9, 11-13), and pediocins produced by Pediococcus acidilactici (28). To date, nisin is the only one that has found practical applications in cheese technology, mostly for preventing growth of clostridia in processed cheese and cheese spreads (35). Recently, nisin was shown to substantially reduce the level of L. monocytogenes in Camembert cheese made with artificially contaminated milk but was unable to prevent the growth of this organism during ripening (22), presumably because nisin was degraded by proteolytic enzymes produced by lactic acid bacteria and mould and/or was bound on some cheese components. Thus, there are still no antagonistic systems which remain active during cheese ripening. In particular, there is a strong need for cheese surface flora exhibiting inhibitory properties against L. monocytogenes.

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Section: Resultsmentioning

confidence: 99%

Activity and purification of linenscin OC2, an antibacterial substance produced by Brevibacterium linens OC2, an orange cheese coryneform bacterium

Maisnier‐Patin

Richard

1995

Appl Environ Microbiol

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“…Active transport of colicins is a remarkable example of protein import into Escherichia coli. Those colicins which kill ceils by forming pores in the cytoplasmic membrane, or colicin M which interferes with murein and lipopolysaccharide biosynthesis, have only to be translocated across the outer membrane, while those which inhibit protein synthesis or degrade the DNA are taken up across the cytoplasmic membrane into the cytoplasm [1][2][3][4]. All colicins bind to specific receptors in the outer membrane.…”

Section: Introductionmentioning

confidence: 99%

Energy-coupled colicin transport through the outer membrane of Escherichia coli K-12: mutated TonB proteins alter receptor activities and colicin uptake

Traub¹

1994

FEMS Microbiology Letters

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The current model of TonB‐dependent colicin transport through the outer membrane of Escherichia coli proposes initial binding to receptor proteins, vectorial release from the receptors and uptake into the periplasm from where the colicins, according to their action, insert into the cytoplasmic membrane or enter the cytoplasm. The uptake is energy‐dependent and the TonB protein interacts with the receptors as well as with the colicins. In this paper we have studied the uptake of colicins B and Ia, both pore‐forming colicins, into various tonB point mutants. Colicin Ia resistance of the tonB mutant (G186D, R204H) was consistent with a defective Cir receptor‐TonB interaction while colicin Ia resistance of E. coli expressing TonB of Serratia marcescens, or TonB of E. coli carrying a C‐terminal fragment of the S. marcescens TonB, seemed to be caused by an impaired colicin Ia‐TonB interaction. In contrast, E. coli tonB (G174R, V178I) was sensitive to colicin Ia and resistant to colicin B unless TonB, ExbB and ExbD were overproduced which resulted in colicin B sensitivity. The differential effects of tonB mutations indicate differences in the interaction of TonB with receptors and colicins.

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“…Given this, I sought to develop another method to achieve constitutive production without mutating native regulatory pathways. The colicin M operon is a perfect test case, since the native operon for this colicin is dysfunctional as is (Harkness and Olschliiger, 1991). The colicin M operon is a known anomaly among colicin operons, as it lacks a lysis gene.…”

Section: Resultsmentioning

confidence: 99%

A New Paradigm of Developing Therapeutics to Infectious Diseases by Combining Insights from Nature and Engineering

Kim

2020

Preprint

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Broad host-spectrum antibiotics not only kill pathogens, but also beneficial commensal bacteria of the host microbiome that play crucial roles for health. In Nature, bacteria kill other bacteria much more selectively than antibiotics do. Because there is metabolic cost involved in producing molecules to inhibit others, evolution endowed bacteria with bacteriocins to kill those who are similar enough to compete for the same niche, while leaving more distantly related bacteria, intact. The presence of such narrow host-spectrum antibacterial molecules suggests that by engineering and reprogramming what is found in nature, it may be possible to develop highly effective yet selective therapeutics to infectious diseases, either as purified drugs, or as live bacterial therapeutics. Here, I propose a new paradigm of developing highly selective therapeutics by combining insights from Nature and engineering and applied this against foodborne pathogens, one of the most common causes of bacterial infections for humans.

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The biology of colicin M

Cited by 8 publications

References 62 publications

Activity and purification of linenscin OC2, an antibacterial substance produced by Brevibacterium linens OC2, an orange cheese coryneform bacterium

Activity and purification of linenscin OC2, an antibacterial substance produced by Brevibacterium linens OC2, an orange cheese coryneform bacterium

Energy-coupled colicin transport through the outer membrane of Escherichia coli K-12: mutated TonB proteins alter receptor activities and colicin uptake

A New Paradigm of Developing Therapeutics to Infectious Diseases by Combining Insights from Nature and Engineering

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