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Role of transmembrane pH gradient and membrane binding in nisin pore formation

Publikováno v: Journal of Bacteriology. 179(1):135-140

Nisin is a cationic antimicrobial peptide that belongs to the group of lantibiotics. It is thought to form oligomeric pores in the target membrane by a mechanism that requires the transmembrane electrical potential (Delta psi) and that involves local

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dris___01423::5ce0e40e9285ea37e24b192255b4ae9f
https://research.rug.nl/en/publications/2e5319eb-be52-4332-8710-4265f61d78cf

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Bactericidal mode of action of plantaricin C

Publikováno v: Applied Environmental Microbiology. 62(8):2701-2709

Plantaricin C is a bacteriocin produced by Lactobacillus plantarum LL441 that kills sensitive cells by acting on the cytoplasmic membrane. In contrast to its lack of impact on immune cells, plantaricin C dissipates the proton motive force and inhibit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dris___01423::6e09674d456192ec0c6f3efe7e63426a
https://research.rug.nl/en/publications/7a016620-df92-4237-97e5-119a3c91a16f

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Bactericidal mode of action of plantaricin C

Autor: Wil N. Konings, Edmund R.S. Kunji, Arnold J. M. Driessen, Beatriz González, Juan E. Suárez, Erwin Glaasker

Publikováno v: Applied and environmental microbiology, 62(8), 2701-2709. AMER SOC MICROBIOLOGY

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4df86cbb933a5bcc6df6c0d62871153
https://doi.org/10.1128/aem.62.8.2701-2709.1996

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The Bacteriocin Lactococcin A Specifically Increases Permeability of Lactococcal Cytoplasmic Membranes in a Voltage-Independent, Protein-Mediated Manner

Publikováno v: Journal of Bacteriology. 173(24):7934-7941

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. Jeeninga, J. Kok, and G. Venema, Appl. Environ. Microbiol. 57:492-498, 1991). Purified la

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dris___01423::901e0ed9ea6c33ea276a0e494c5227b9
https://research.rug.nl/en/publications/5cf536cd-b0a0-4ad4-9725-e0a27915c21b

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MECHANISM OF ACTION OF THE PEPTIDE ANTIBIOTIC NISIN IN LIPOSOMES AND CYTOCHROME-C OXIDASE-CONTAINING PROTEOLIPOSOMES

Publikováno v: Applied and environmental microbiology. 57(8):2164-2170

The interaction of the peptide antibiotic nisin with liposomes has been studied. The effect of this interaction was analyzed on the membrane potential (inside negative) and the pH gradient (inside alkaline) in liposomes made from Escherichia coli pho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dris___00893::6ea30cb01dd07bacc950105fb12edb99
https://hdl.handle.net/11370/197772da-0a1e-4c18-a3cd-2d8845e3cccb

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Mutational analysis and chemical modification of Cys24 of lactococcin B, a bacteriocin produced by Lactococcus lactis

Autor: Venema, K, Dost, MHR, Kok, J, Dost, Michiel H.R., Venema, Gerhardus

Publikováno v: Microbiology-Uk, 142(10), 2825-2830. MAIK NAUKA/INTERPERIODICA/SPRINGER

Using site-directed mutagenesis the single cysteine residue at position 24 of lactococcin B was replaced by all other possible amino acids. Most of these mutant molecules retained bacteriocin activity, with the exception of those in which cysteine wa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::733e23bb1029ba8979e9588077fe111f
https://pubmed.ncbi.nlm.nih.gov/8885398

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Mechanism of lantibiotic-induced pore-formation

Autor: Gordon C. K. Roberts, Gert N. Moll, Arnold J. M. Driessen, Wil N. Konings

Publikováno v: Antonie Van Leeuwenhoek: International Journal of General and Molecular Microbiology, 69(2). SPRINGER

Nisin and other lantibiotics have a bacteriocidal effect against Gram-positive bacteria, and also inhibit the outgrowth of bacterial spores. The bacteriocidal effect appears to be due to the formation of pores in the bacterial membrane. In the absenc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9c2911555022a7a326f3373a31d5b07
https://pubmed.ncbi.nlm.nih.gov/8775978

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In vitro pore-forming activity of the lantibiotic nisin. Role of protonmotive force and lipid composition

Autor: Marieke G. L. Elferink, Wil N. Konings, Maria J. García Garcerá, Arnold J. M. Driessen

Publikováno v: European Journal of Biochemistry, 212(2), 417-422. Blackwell Publishing Ltd

Nisin is a lantibiotic produced by some strains of Lactococcus lactis subsp. lactis. The target for nisin action is the cytoplasmic membrane of Gram-positive bacteria. Nisin dissipates the membrane potential (DELTApsi) and induces efflux of low-molec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03837363d18cff6c2fd6a13ff149a9a7
https://pubmed.ncbi.nlm.nih.gov/8444179

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

Autor: Jan Kok, Ingolf F. Nes, Wn Konings, T Abee, H Holo, M J van Belkum, Gerhardus Venema

Publikováno v: Journal of Bacteriology, 173(24), 7934-7941. AMER SOC MICROBIOLOGY

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. Jeeninga, J. Kok, and G. Venema, Appl. Environ. Microbiol. 57:492-498, 1991). Purified la

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b84414191c8f1a8adbbaa47181df0fa
https://europepmc.org/articles/PMC212587/

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