The bacteriocin lactococcin A specifically increases permeability of lactococcal cytoplasmic membranes in a voltage-independent, protein-mediated manner

Belkum, Marco J. van; Kok, Jan; Venema, Gerhardus; Holo, Helge; Nes, Ingolf F.; Konings, Wn; Abee, Tjakko

doi:10.1128/jb.173.24.7934-7941.1991

Cited by 165 publications

(133 citation statements)

References 36 publications

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“…Although other LAB-produced bacteriocins that have been sequenced do not appear to have such a marked amphiphilic distribution of amino acids as a1 and 13, such a distribution is seen in the C-terminal parts of lactococcin A (10) and lactocin S (16). There is evidence that lactococcin A permeabilizes target cell membranes (28), as also appears to be the case for nisin (22).…”

Section: Resultsmentioning

confidence: 99%

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A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides

Nissen‐Meyer¹,

Holo²,

Håvarstein³

et al. 1992

J Bacteriol

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216

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A lactococcal bacteriocin, termed lactococcin G, was purified to homogeneity by a simple four-step purification procedure that includes ammonium sulfate precipitation, binding to a cation exchanger and octyl-Sepharose CL4B, and reverse-phase chromatography. The final yield was about 20%k, and nearty a 7,000-fold increase in the specific activity was obtained. The bacteriocin activity was associated with three peptides, termed al, a2, and 13, which were separated by reverse-phase chromatography. Judging from their amino acid sequences, al and a2 were the same gene product. Differences in their configurations presumably resulted in a2 having a slightly lower affinity for the reverse-phase column than al and a reduced bacteriocin activity when combined with 13. Bacteriocin activity required the complementary action of both the a and the 1 peptides. When neither al nor 1 was in excess, about 0.3 nM al and 0.04 nM 13 induced 50%1 growth inhibition, suggesting that they might interact in a 7:1 or 8:1 ratio. As judged by the amino acid sequence, a1has an isoelectric point of 10.9, an extinction coefficient of 1.3 x 104 M-1 cm-', and a molecular weight of 4,346 (39 amino acid residues long). Similarly, 13 has an isoelectric point of 10.4, an extinction coefficient of 2.4x 104 M-1 cm'1, and a molecular weight of 4110 (35 amino acid residues long). Molecular weights of 4,376 and 4,109 for al and (, respectively, were obtained by mass spectrometry. The N-terminal halves of both the a and the 13 peptides may form amphiphilic a-helices, suggesting that the peptides are pore-forming toxins that create cell membrane channels through a "barrel-stave" mechanism. The C-terminal halves of both peptides consist largely of polar amino acids.Bacteriocins are proteins that show bactericidal activity towards bacteria that are closely related to the bacteriocinproducing species (25). Because of their potential use as antibacterial agents, bacteriocins have been the subject of much research. In recent years, there has been considerable interest especially in bacteriocins from lactic acid bacteria (LAB), because of their potential as food and feed additives.The LAB bacteriocins appear to be structurally quite different from the colicins of Escherichia coli (7,14). LAB bacteriocins are usually small peptides, seldom containing more than 60 amino acids, while colicins are proteins of 300 to 800 amino acids. On the basis of their structure, LAB bacteriocins may be divided into two groups. The first group contains the so-called lantibiotics, which have been known for a long time (6, 11). Lantibiotics consist of a polypeptide chain that has been posttranslationally modified. The modified amino acids are lanthionine and methyllanthionine and their precursors dehydroalanine and dehydrobutyrine. Among the lantibiotics, nisin is by far the most studied (1, 4, 12), although three new LAB lantibiotics recently have been purified and characterized (15,16,21,24 which does not show any apparent amino acid sequence homology to other isolated LAB bacteri...

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Section: Resultsmentioning

confidence: 99%

“…Lactococcin A, * Corresponding author. which does not show any apparent amino acid sequence homology to other isolated LAB bacteriocins, has been shown to induce cell death by permeabilizing the membrane of susceptible cells (28).…”

mentioning

confidence: 99%

A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides

Nissen‐Meyer¹,

Holo²,

Håvarstein³

et al. 1992

J Bacteriol

Self Cite

301

216

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show abstract

“…In addition to dissipation of PMF, bacteriocins are reported to deplete intracellular adenosine triphosphate (ATP), either through leakage or hydrolysis, and to cause efflux of intracellular inorganic phosphate (P i ) (Abee et al 1994a;Abee et al 1994b;Winkowski et al 1994;Chen and Montville 1995). Some bacteriocins also inhibit uptake and induce efflux of nutrients such as amino acids and sugars (van Belkum et al 1991;Venema et al 1993;Christensen and Hutkins 1994).…”

confidence: 99%

Bacteriocin inhibition of two glucose transport systems in Listeria monocytogenes

Waite

Siragusa²,

Hutkins³

1998

J Appl Microbiol

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Listeria monocytogenes transports glucose by proton motive force-mediated and phosphoenolpyruvate-dependent phosphotransferase systems (PEP-dependent PTS). Inhibition of both systems by nisin, pediocin JD and leuconosin S is reported here for four strains of L. monocytogenes. Intracellular and extracellular adenosine triphosphate (ATP) and extracellular inorganic phosphate were measured in energized L. monocytogenes Scott A cells to determine whether inhibition of the PEP-dependent PTS might occur as a result of bacteriocin-induced leakage of intracellular components. Addition of nisin resulted in a decrease in intracellular ATP with an increase in extracellular ATP. Leuconosin S and pediocin JD induced a depletion of intracellular ATP. ATP efflux was low for the leuconosin S-treated cells and barely detectable for pediocin JD-treated cells. Addition of nisin, leuconosin S and pediocin JD induced efflux of inorganic phosphate. It appears that bacteriocin-mediated inhibition of the glucose PEP-dependent PTS occurs as a result of hydrolysis or efflux of ATP, PEP and other essential molecules from L. monocytogenes cells.

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“…Είναι ένα μικρό υδρόφοβο πεπτίδιο που αποτελείται από 54 αμινοξέα και εμποδίζει την ανάπτυξη των στελεχών των λακτοκόκκων. Από πειράματα που έγιναν 23 αποδείχτηκε ότι η βακτηριοσίνη αυξάνει τη διαπερατότητα της κυττα ροπλασματικής μεμβράνης των ευαίσθητων λακτοκόκκων. Σε αντίθεση με τις βακτηριοσίνες της πρώτης κατηγορίας, οι οποίες προκαλούν διαταραχή της δομικής ακεραιότητας της μεμβράνης, αυτές της κλάσης II διαταράσσουν τη λει τουργία της ανεξάρτητα από τη διαφορά δυναμικού (Δψ) που επικρατεί.…”

Section: τρόπος δράσης των βακτηριοσινώνunclassified

Bacteriocins: Classification, properties, production and mode of action. (I)

Metaxopoulos

Mataragas

Drosinos

2018

J Hellenic Vet Med Soc

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Bacteriocins are antimicrobial compounds synthesized by ribosomes. In the last years a variety of bacteriocins, produced by lactic acid bacteria, has been identified and characterized. As a result of these studies is that new knowledge regarding the biosynthesis, structure, production and mode of action of these proteinaceous compounds has been gained. The present review attempts to refer some of the available data with reference to the bacteriocins, which are important for the understanding of the whole mechanism of the production of bacteriocins. Additionally, some features and recent biology and biochemistry findings concerning these substances will be reported, in order to provide a general overview of the production and action of the bacteriocins.

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The bacteriocin lactococcin A specifically increases permeability of lactococcal cytoplasmic membranes in a voltage-independent, protein-mediated manner

Abstract: Lactococcin A is a bacteriocin produced by Lactococcus lactis. Its structural gene has recently been cloned and sequenced (M. J. van Belkum, B. J. Hayema, R. E. Jeeningaf J. Kok, and G. Venema, Appl. Environ. Microbiol. 57:492-498, 1991

Cited by 165 publications

References 36 publications

A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides

A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides

Bacteriocin inhibition of two glucose transport systems in Listeria monocytogenes

Bacteriocins: Classification, properties, production and mode of action. (I)

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