Gert N. Moll

Distinct Contributions of the Nisin Biosynthesis Enzymes NisB and NisC and Transporter NisT to Prenisin Production by Lactococcus lactis (2008)

Bakkes, Patrick J., Moll, Gert N., Driessen, Arnold J.M.

Several Lactococcus lactis strains produce the lantibiotic nisin. The dedicated enzymes NisB and NisC and the transporter NisT modify and secrete the ribosomally synthesized nisin precursor peptide....

Influence of Shifting Positions of Ser, Thr, and Cys Residues in Prenisin on the Efficiency of Modification Reactions and on the Antimicrobial Activities of the Modified Prepeptides (2008)

Lubelski, Jacek, Overkamp, Wout, Kluskens, Leon D., Moll, Gert N., Kuipers, Oscar P.

Since the recent discovery that the nisin modification and transport machinery can be used to produce and modify peptides unrelated to nisin, specific questions arose concerning the specificity of...

Production of Dehydroamino Acid-Containing Peptides by Lactococcus lactis (2007)

Rink, Rick, Wierenga, Jenny, Kuipers, Anneke, Kluskens, Leon D., Driessen, Arnold J.M., Kuipers, Oscar P., ...

Nisin is a pentacyclic peptide antibiotic produced by some Lactococcus lactis strains. Nisin contains dehydroresidues and thioether rings that are posttranslationally introduced by a...

Dissection and Modulation of the Four Distinct Activities of Nisin by Mutagenesis of Rings A and B and by C-Terminal Truncation (2007)

Rink, Rick, Wierenga, Jenny, Kuipers, Anneke, Kluskens, Leon D., Driessen, Arnold J.M., Kuipers, Oscar P., ...

Nisin A is a pentacyclic antibiotic peptide produced by various Lactococcus lactis strains. Nisin displays four different activities: (i) it autoinduces its own synthesis; (ii) it inhibits the growth...

NisC, the Cyclase of the Lantibiotic Nisin, Can Catalyze Cyclization of Designed Nonlantibiotic Peptides (2007)

Rink, Rick, Kluskens, Leon D., Kuipers, Anneke, Driessen, Arnold J.M., Kuipers, Oscar P., Moll, Gert N.

Nisin is a pentacyclic peptide antibiotic active against Gram-positive bacteria. Its thioether rings are formed by two enzymatic steps: nisin dehydratase (NisB)-mediated dehydration of serines and...

Sec-Mediated Transport of Posttranslationally Dehydrated Peptides in Lactococcus lactis (2006)

Kuipers, Anneke, Wierenga, Jenny, Rink, Rick, Kluskens, Leon D., Driessen, Arnold J.M., Kuipers, Oscar P., ...

Nisin is a lanthionine-containing antimicrobial peptide produced by Lactococcus lactis. Its (methyl)lanthionines are introduced by two posttranslational enzymatic steps involving the dehydratase...

Post-translational Modification of Therapeutic Peptides By NisB, the Dehydratase of the Lantibiotic Nisin (2005)

Kluskens, Leon D., Kuipers, Anneke, Rink, Rick, Boef, Esther De, Fekken, Susan, Driessen, Arnold J.M., ...

Post-translationally introduced dehydroamino acids often play an important role in the activity and receptor specificity of biologically active peptides. In addition, a dehydroamino acid can be...

Lantibiotic Structures as Guidelines for the Design of Peptides That Can Be Modified by Lantibiotic Enzymes (2005)

Rink, Rick, Kuipers, Anneke, Boef, Esther De, Leenhouts, Kees J., Driessen, Arnold J.M., Moll, Gert N., ...

Lantibiotics are (methyl)lanthionine-containing bacterial peptides. (Methyl)lanthionines are posttranslationally introduced into the prepropeptides by biosynthetic enzymes that dehydrate serines and...

NisT, the Transporter of the Lantibiotic Nisin, Can Transport Fully Modified, Dehydrated, and Unmodified Prenisin and Fusions of the Leader Peptide with Non-lantibiotic Peptides (2004)

Kuipers, Anneke, Boef, Esther De, Rink, Rick, Fekken, Susan, Kluskens, Leon D., Driessen, Arnold J.M., ...

Lantibiotics are lanthionine-containing peptide antibiotics. Nisin, encoded by nisA, is a pentacyclic lantibiotic produced by some Lactococcus lactis strains. Its thioether rings are...

Enterocin P Causes Potassium Ion Efflux from Enterococcus faecium T136 Cells (2001)

Herranz, Carmen, Cintas, Luis M., Hernández, Pablo E., Moll, Gert N., Driessen, Arnold J.M.

Enterocin P is a bacteriocin produced by Enterococcus faecium P13. We studied the mechanism of its bactericidal action using enterocin-P-sensitive E. faecium T136 cells. The bacteriocin is incapable...

Comparison of the Membrane Interaction and Permeabilization by the Designed Peptide Ac-MB21-NH2 and Truncated Dermaseptin S3 (2000)

Moll, Gert N., Brul, Stanley, Konings, Wil N., Driessen, Arnold J.M.

Ac-MB21-NH2 (Ac-FASLLGKALKALAKQ-NH2) and dermaseptin S3(1-16)-NH2 (ALWKNMLKGIGKLAGK-NH2) are cationic amphipathic peptides with antimicrobial activity against a broad spectrum of microorganisms...

Complementary and Overlapping Selectivity of the Two-Peptide Bacteriocins Plantaricin EF and JK (1999)

Moll, Gert N., Akker, Emile Van Den, Hauge, Håvard H., Nissen-Meyer, Jon, Nes, Ingolf F., Konings, Wil N., ...

Plantaricin EF and JK are both two-peptide bacteriocins produced by Lactobacillus plantarum C11. The mechanism of plantaricin EF and JK action was studied on L. plantarum 965 cells. Both plantaricins...

Bacteriocins: mechanism of membrane insertion and pore formation (1999)

Moll, Gert N., Konings, Wil N., Driessen, Arnold J.M.

Lactic acid bacteria produce several types of pore forming peptides. Class I bacteriocins are lantibiotics that contain (methyl)lanthionine residues that may form intramolecular thioether rings....

Plantaricin A Is an Amphiphilic α-Helical Bacteriocin-like Pheromone Which Exerts Antimicrobial and Pheromone Activities through Different Mechanisms (1998)

Hauge, Håvard Hildeng, Mantzilas, Dimitris, Moll, Gert N., Konings, Wil N., Driessen, Arnold J.M., Eijsink, Vincent G.H., ...

Production of bacteriocins by lactic acid bacteria is in some cases regulated by a quorum sensing mechanism that involves a secreted bacteriocin-like peptide pheromone. In the case of Lactobacillus...

The Lantibiotic Nisin Induces Transmembrane Movement of a Fluorescent Phospholipid (1998)

Moll, Gert N., Konings, Wil N., Driessen, Arnold J.M.

Nisin is a pore-forming antimicrobial peptide. The capacity of nisin to induce transmembrane movement of a fluorescent phospholipid in lipid vesicles was investigated. Unilamellar phospholipid...

Role of Transmembrane pH Gradient and Membrane Binding in Nisin Pore Formation (1997)

Moll, Gert N., Clark, Jonathan, Chan, Weng C., Bycroft, Barrie W., Roberts, Gordon C.K., Konings, Wil N., ...

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...

Mechanism of lantibiotic-induced pore-formation (1996)

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

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...

Enterocin P Causes Potassium Ion Efflux from Enterococcus faecium T136 Cells

Herranz, Carmen, Cintas, Luis M., Hernández, Pablo E., Moll, Gert N., Driessen, Arnold J. M.

Enterocin P is a bacteriocin produced by Enterococcus faecium P13. We studied the mechanism of its bactericidal action using enterocin-P-sensitive E. faecium T136 cells. The bacteriocin is incapable...

Complementary and Overlapping Selectivity of the Two-Peptide Bacteriocins Plantaricin EF and JK

Moll, Gert N., Van Den Akker, Emile, Hauge, Håvard H., Nissen-Meyer, Jon, Nes, Ingolf F., Konings, Wil N., ...

Plantaricin EF and JK are both two-peptide bacteriocins produced by Lactobacillus plantarum C11. The mechanism of plantaricin EF and JK action was studied on L. plantarum 965 cells. Both plantaricins...

The Lantibiotic Nisin Induces Transmembrane Movement of a Fluorescent Phospholipid

Moll, Gert N., Konings, Wil N., Driessen, Arnold J. M.

Nisin is a pore-forming antimicrobial peptide. The capacity of nisin to induce transmembrane movement of a fluorescent phospholipid in lipid vesicles was investigated. Unilamellar phospholipid...

Enterocin P Causes Potassium Ion Efflux from Enterococcus faecium T136 Cells

Herranz, Carmen, Cintas, Luis M., Hernández, Pablo E., Moll, Gert N., Driessen, Arnold J. M.

Enterocin P is a bacteriocin produced by Enterococcus faecium P13. We studied the mechanism of its bactericidal action using enterocin-P-sensitive E. faecium T136 cells. The bacteriocin is incapable...

Complementary and Overlapping Selectivity of the Two-Peptide Bacteriocins Plantaricin EF and JK

Moll, Gert N., Van Den Akker, Emile, Hauge, Håvard H., Nissen-Meyer, Jon, Nes, Ingolf F., Konings, Wil N., ...

Plantaricin EF and JK are both two-peptide bacteriocins produced by Lactobacillus plantarum C11. The mechanism of plantaricin EF and JK action was studied on L. plantarum 965 cells. Both plantaricins...

The Lantibiotic Nisin Induces Transmembrane Movement of a Fluorescent Phospholipid

Moll, Gert N., Konings, Wil N., Driessen, Arnold J. M.

Nisin is a pore-forming antimicrobial peptide. The capacity of nisin to induce transmembrane movement of a fluorescent phospholipid in lipid vesicles was investigated. Unilamellar phospholipid...

Sec-Mediated Transport of Posttranslationally Dehydrated Peptides in Lactococcus lactis▿ †

Kuipers, Anneke, Wierenga, Jenny, Rink, Rick, Kluskens, Leon D., Driessen, Arnold J. M., Kuipers, Oscar P., ...

Nisin is a lanthionine-containing antimicrobial peptide produced by Lactococcus lactis. Its (methyl)lanthionines are introduced by two posttranslational enzymatic steps involving the dehydratase...

Production of Dehydroamino Acid-Containing Peptides by Lactococcus lactis▿

Rink, Rick, Wierenga, Jenny, Kuipers, Anneke, Kluskens, Leon D., Driessen, Arnold J. M., Kuipers, Oscar P., ...

Nisin is a pentacyclic peptide antibiotic produced by some Lactococcus lactis strains. Nisin contains dehydroresidues and thioether rings that are posttranslationally introduced by a...

Dissection and Modulation of the Four Distinct Activities of Nisin by Mutagenesis of Rings A and B and by C-Terminal Truncation▿ †

Rink, Rick, Wierenga, Jenny, Kuipers, Anneke, Kluskens, Leon D., Driessen, Arnold J. M., Kuipers, Oscar P., ...

Nisin A is a pentacyclic antibiotic peptide produced by various Lactococcus lactis strains. Nisin displays four different activities: (i) it autoinduces its own synthesis; (ii) it inhibits the growth...

Influence of Shifting Positions of Ser, Thr, and Cys Residues in Prenisin on the Efficiency of Modification Reactions and on the Antimicrobial Activities of the Modified Prepeptides▿ †

Lubelski, Jacek, Overkamp, Wout, Kluskens, Leon D., Moll, Gert N., Kuipers, Oscar P.

Since the recent discovery that the nisin modification and transport machinery can be used to produce and modify peptides unrelated to nisin, specific questions arose concerning the specificity of...

Distinct Contributions of the Nisin Biosynthesis Enzymes NisB and NisC and Transporter NisT to Prenisin Production by Lactococcus lactis▿

Bakkes, Patrick J., Moll, Gert N., Driessen, Arnold J. M.

Several Lactococcus lactis strains produce the lantibiotic nisin. The dedicated enzymes NisB and NisC and the transporter NisT modify and secrete the ribosomally synthesized nisin precursor peptide....

Mechanistic Dissection of the Enzyme Complexes Involved in Biosynthesis of Lacticin 3147 and Nisin ▿ †

Kuipers, Anneke, Meijer-Wierenga, Jenny, Rink, Rick, Kluskens, Leon D., Moll, Gert N.

The thioether rings in the lantibiotics lacticin 3147 and nisin are posttranslationally introduced by dehydration of serines and threonines, followed by coupling of these dehydrated residues to...