Hans-Georg Sahl

Transcriptome analysis of the responses of Staphylococcus aureusto antimicrobial peptides and characterization of the roles of vraDEand vraSRin antimicrobial resistance (2009)

Pietiäinen, Milla, François, Patrice, Hyyryläinen, Hanne-Leena, Tangomo, Manuela, Sass, Vera, Sahl, Hans-Georg, ...

Abstract Background Understanding how pathogens respond to antimicrobial peptides, and how this compares to currently available antibiotics, is crucial for optimizing antimicrobial therapy....

The lantibiotic mersacidin is a strong inducer of the cell wall stress response of Staphylococcus aureus (2008)

Sass, Peter, Jansen, Andrea, Szekat, Christiane, Sass, Vera, Sahl, Hans-Georg, Bierbaum, Gabriele

Abstract Background The lantibiotic mersacidin is an antimicrobial peptide of 20 amino acids that is ribosomally produced by Bacillus sp. strain HIL Y-85,54728. Mersacidin acts by complexing the...

Mersacidin eradicates methicillin-resistant Staphylococcus aureus (MRSA) in a mouse rhinitis model (2004)

Kruszewska, Danuta, Sahl, Hans-Georg, Bierbaum, Gabriele, Pag, Ulrike, Hynes, Sean O., Ljungh, Åsa

Objectives: Methicillin-resistant Staphylococcus aureus (MRSA) often colonize the anterior nares, and nasal carriage remains the main source of bacterial dissemination. The aim of this study was to...

Mersacidin eradicates methicillin-resistant Staphylococcus aureus (MRSA) in a mouse rhinitis model (2004)

Kruszewska, Danuta, Sahl, Hans-Georg, Bierbaum, Gabriele, Pag, Ulrike, Hynes, Sean O., Ljungh, Åsa

Objectives: Methicillin-resistant Staphylococcus aureus (MRSA) often colonize the anterior nares, and nasal carriage remains the main source of bacterial dissemination. The aim of this study was to...

Specific Binding of Nisin to the Peptidoglycan Precursor Lipid II Combines Pore Formation and Inhibition of Cell Wall Biosynthesis for Potent Antibiotic Activity (2001)

Wiedemann, Imke, Breukink, Eefjan, Kraaij, Cindy Van, Kuipers, Oscar P., Bierbaum, Gabriele, Kruijff, Ben De, ...

Unlike numerous pore-forming amphiphilic peptide antibiotics, the lantibiotic nisin is active in nanomolar concentrations, which results from its ability to use the lipid-bound cell wall precursor...

Protein engineering of lantibiotics (1996)

Kuipers, Oscar P., Bierbaum, Gabriele, Ottenwälder, Birgit, Dodd, Helen M., Horn, Nicky, Metzger, Jörg, ...

Whereas protein engineering of enzymes and structural proteins nowadays is an established research tool for studying structure-function relationships of polypeptides and for improving their...

Mechanistic Studies of Lantibiotic-Induced Permeabilization of Phospholipid Vesicles (1995)

Driessen, Arnold J.M., Kuiper, Wieny, Kamp, Mart Van De, Sahl, Hans-Georg, Konings, Ruud N.H., ...

Nisin is a cationic polycyclic bacteriocin secreted by some lactic acid bacteria. Nisin has previously been shown to permeabilize liposomes. The interaction of nisin was analyzed with liposomes...

Elucidation of the primary structure of the lantibiotic epilancin K7 from Staphylococcus epidermidis K7. Cloning and characterisation of the epilancin-K7-encoding gene and NMR analysis of mature epilancin K7 (1995)

Kamp, Mart Van De, Konings, Ruud N.H., Bierbaum, Gabriele, Sahl, Hans-Georg, Kuipers, Oscar P., ...

Lantibiotics are bacteriocins that contain unusual amino acids such as lanthionines and α,β-didehydro residues generated by posttranslational modification of a ribosomally synthesized precursor...

Two-Component Anti-Staphylococcus aureus Lantibiotic Activity Produced by Staphylococcus aureus C55

Sahl, Hans-Georg, Tagg, John R.

Staphylococcus aureus C55 was shown to produce bacteriocin activity comprising three distinct peptide components, termed staphylococcins C55α, C55β, and C55γ. The three peptides were purified to...

Molecular Analysis of Expression of the Lantibiotic Pep5 Immunity Phenotype

Pag, Ulrike, Heidrich, Christoph, Bierbaum, Gabriele, Sahl, Hans-Georg

The lantibiotic Pep5 is produced by Staphylococcus epidermidis 5. Within its biosynthetic gene cluster, the immunity gene pepI, providing producer self-protection, is localized upstream of the...

Identification of Genes Encoding Two-Component Lantibiotic Production in Staphylococcus aureus C55 and Other Phage Group II S. aureus Strains and Demonstration of an Association with the Exfoliative Toxin B Gene

Sahl, Hans-Georg, Tagg, John R.

The production of exfoliative toxin B (ET-B), but not ET-A, was shown to be specifically associated with production of a highly conserved two-component lantibiotic peptide system in phage group II...

The Lantibiotic Mersacidin Inhibits Peptidoglycan Synthesis by Targeting Lipid II

Brötz, Heike, Bierbaum, Gabriele, Leopold, Klaus, Reynolds, Peter E., Sahl, Hans-Georg

The lantibiotic mersacidin exerts its bactericidal action by inhibition of peptidoglycan biosynthesis. It interferes with the membrane-associated transglycosylation reaction; during this step the...

Isolation, Characterization, and Heterologous Expression of the Novel Lantibiotic Epicidin 280 and Analysis of Its Biosynthetic Gene Cluster

Heidrich, Christoph, Pag, Ulrike, Josten, Michaele, Metzger, Jörg, Jack, Ralph W., Bierbaum, Gabriele, ...

Epicidin 280 is a novel type A lantibiotic produced by Staphylococcus epidermidis BN 280. During C18 reverse-phase high-performance liquid chromatography two epicidin 280 peaks were obtained; the two...

Role of the Single Regulator MrsR1 and the Two-Component System MrsR2/K2 in the Regulation of Mersacidin Production and Immunity

Guder, André, Schmitter, Tim, Wiedemann, Imke, Sahl, Hans-Georg, Bierbaum, Gabriele

The lantibiotic mersacidin is an antimicrobial peptide of 20 amino acids which inhibits bacterial cell wall biosynthesis by binding to the precursor molecule lipid II and which is produced by...

Mode of Action of the Antimicrobial Peptide Aureocin A53 from Staphylococcus aureus

Netz, Daili Jacqueline Aguilar, Sahl, Hans-Georg

We investigated the mode of action of aureocin A53 on living bacterial cells and model membranes. Aureocin A53 acted bactericidally against Staphylococcus simulans 22, with >90% of the cells killed...

Lipid II-Mediated Pore Formation by the Peptide Antibiotic Nisin: a Black Lipid Membrane Study

Wiedemann, Imke, Benz, Roland, Sahl, Hans-Georg

The antibiotic peptide nisin is the first known lantibiotic that uses a docking molecule within the bacterial cytoplasmic membrane for pore formation. Through specific interaction with the cell wall...

Localization and Functional Analysis of PepI, the Immunity Peptide of Pep5-Producing Staphylococcus epidermidis Strain 5

Hoffmann, Anja, Schneider, Tanja, Pag, Ulrike, Sahl, Hans-Georg

Pep5 is a cationic pore-forming lantibiotic produced by Staphylococcus epidermidis strain 5. The producer strain protects itself from the lethal action of its own bacteriocin through the...

Controlled alteration of the shape and conformational stability of α-helical cell-lytic peptides: effect on mode of action and cell specificity

Zelezetsky, Igor, Pacor, Sabrina, Pag, Ulrike, Papo, Niv, Shai, Yechiel, Sahl, Hans-Georg, ...

A novel method, based on the rational and systematic modulation of macroscopic structural characteristics on a template originating from a large number of natural, cell-lytic, amphipathic α-helical...

Transposon Disruption of the Complex I NADH Oxidoreductase Gene (snoD) in Staphylococcus aureus Is Associated with Reduced Susceptibility to the Microbicidal Activity of Thrombin-Induced Platelet Microbicidal Protein 1

Bayer, Arnold S., McNamara, Peter, Yeaman, Michael R., Lucindo, Natalie, Jones, Tiffanny, Cheung, Ambrose L., ...

The cationic molecule thrombin-induced platelet microbicidal protein 1 (tPMP-1) exerts potent activity against Staphylococcus aureus. We previously reported that a Tn551 S. aureus transposon mutant,...

Insights into In Vivo Activities of Lantibiotics from Gallidermin and Epidermin Mode-of-Action Studies†

Bonelli, Raquel Regina, Schneider, Tanja, Sahl, Hans-Georg, Wiedemann, Imke

The activity of lanthionine-containing peptide antibiotics (lantibiotics) is based on different killing mechanisms which may be combined in one molecule. The prototype lantibiotic nisin inhibits...

Very Low Ethanol Concentrations Affect the Viability and Growth Recovery in Post-Stationary-Phase Staphylococcus aureus Populations

Chatterjee, Indranil, Somerville, Greg A., Heilmann, Christine, Sahl, Hans-Georg, Maurer, Hans H., Herrmann, Mathias

Pharmaceuticals, culture media used for in vitro diagnostics and research, human body fluids, and environments can retain very low ethanol concentrations (VLEC) (≤0.1%, vol/vol). In contrast to the...

Lipid II-Based Antimicrobial Activity of the Lantibiotic Plantaricin C

Wiedemann, Imke, Böttiger, Tim, Bonelli, Raquel Regina, Schneider, Tanja, Sahl, Hans-Georg, Martínez, Beatriz

We analyzed the mode of action of the lantibiotic plantaricin C (PlnC), produced by Lactobacillus plantarum LL441. Compared to the well-characterized type A lantibiotic nisin and type B lantibiotic...

Two-Component Anti-Staphylococcus aureus Lantibiotic Activity Produced by Staphylococcus aureus C55

Sahl, Hans-Georg, Tagg, John R.

Staphylococcus aureus C55 was shown to produce bacteriocin activity comprising three distinct peptide components, termed staphylococcins C55α, C55β, and C55γ. The three peptides were purified to...

Molecular Analysis of Expression of the Lantibiotic Pep5 Immunity Phenotype

Pag, Ulrike, Heidrich, Christoph, Bierbaum, Gabriele, Sahl, Hans-Georg

The lantibiotic Pep5 is produced by Staphylococcus epidermidis 5. Within its biosynthetic gene cluster, the immunity gene pepI, providing producer self-protection, is localized upstream of the...

Identification of Genes Encoding Two-Component Lantibiotic Production in Staphylococcus aureus C55 and Other Phage Group II S. aureus Strains and Demonstration of an Association with the Exfoliative Toxin B Gene

Sahl, Hans-Georg, Tagg, John R.

The production of exfoliative toxin B (ET-B), but not ET-A, was shown to be specifically associated with production of a highly conserved two-component lantibiotic peptide system in phage group II...

The Lantibiotic Mersacidin Inhibits Peptidoglycan Synthesis by Targeting Lipid II

Brötz, Heike, Bierbaum, Gabriele, Leopold, Klaus, Reynolds, Peter E., Sahl, Hans-Georg

The lantibiotic mersacidin exerts its bactericidal action by inhibition of peptidoglycan biosynthesis. It interferes with the membrane-associated transglycosylation reaction; during this step the...

Isolation, Characterization, and Heterologous Expression of the Novel Lantibiotic Epicidin 280 and Analysis of Its Biosynthetic Gene Cluster

Heidrich, Christoph, Pag, Ulrike, Josten, Michaele, Metzger, Jörg, Jack, Ralph W., Bierbaum, Gabriele, ...

Epicidin 280 is a novel type A lantibiotic produced by Staphylococcus epidermidis BN 280. During C18 reverse-phase high-performance liquid chromatography two epicidin 280 peaks were obtained; the two...

Role of the Single Regulator MrsR1 and the Two-Component System MrsR2/K2 in the Regulation of Mersacidin Production and Immunity

Guder, André, Schmitter, Tim, Wiedemann, Imke, Sahl, Hans-Georg, Bierbaum, Gabriele

The lantibiotic mersacidin is an antimicrobial peptide of 20 amino acids which inhibits bacterial cell wall biosynthesis by binding to the precursor molecule lipid II and which is produced by...

Mode of Action of the Antimicrobial Peptide Aureocin A53 from Staphylococcus aureus

Netz, Daili Jacqueline Aguilar, Sahl, Hans-Georg

We investigated the mode of action of aureocin A53 on living bacterial cells and model membranes. Aureocin A53 acted bactericidally against Staphylococcus simulans 22, with >90% of the cells killed...

Lipid II-Mediated Pore Formation by the Peptide Antibiotic Nisin: a Black Lipid Membrane Study

Wiedemann, Imke, Benz, Roland, Sahl, Hans-Georg

The antibiotic peptide nisin is the first known lantibiotic that uses a docking molecule within the bacterial cytoplasmic membrane for pore formation. Through specific interaction with the cell wall...

Localization and Functional Analysis of PepI, the Immunity Peptide of Pep5-Producing Staphylococcus epidermidis Strain 5

Hoffmann, Anja, Schneider, Tanja, Pag, Ulrike, Sahl, Hans-Georg

Pep5 is a cationic pore-forming lantibiotic produced by Staphylococcus epidermidis strain 5. The producer strain protects itself from the lethal action of its own bacteriocin through the...

Controlled alteration of the shape and conformational stability of α-helical cell-lytic peptides: effect on mode of action and cell specificity

Zelezetsky, Igor, Pacor, Sabrina, Pag, Ulrike, Papo, Niv, Shai, Yechiel, Sahl, Hans-Georg, ...

A novel method, based on the rational and systematic modulation of macroscopic structural characteristics on a template originating from a large number of natural, cell-lytic, amphipathic α-helical...

Transposon Disruption of the Complex I NADH Oxidoreductase Gene (snoD) in Staphylococcus aureus Is Associated with Reduced Susceptibility to the Microbicidal Activity of Thrombin-Induced Platelet Microbicidal Protein 1

Bayer, Arnold S., McNamara, Peter, Yeaman, Michael R., Lucindo, Natalie, Jones, Tiffanny, Cheung, Ambrose L., ...

The cationic molecule thrombin-induced platelet microbicidal protein 1 (tPMP-1) exerts potent activity against Staphylococcus aureus. We previously reported that a Tn551 S. aureus transposon mutant,...

Insights into In Vivo Activities of Lantibiotics from Gallidermin and Epidermin Mode-of-Action Studies†

Bonelli, Raquel Regina, Schneider, Tanja, Sahl, Hans-Georg, Wiedemann, Imke

The activity of lanthionine-containing peptide antibiotics (lantibiotics) is based on different killing mechanisms which may be combined in one molecule. The prototype lantibiotic nisin inhibits...

Very Low Ethanol Concentrations Affect the Viability and Growth Recovery in Post-Stationary-Phase Staphylococcus aureus Populations

Chatterjee, Indranil, Somerville, Greg A., Heilmann, Christine, Sahl, Hans-Georg, Maurer, Hans H., Herrmann, Mathias

Pharmaceuticals, culture media used for in vitro diagnostics and research, human body fluids, and environments can retain very low ethanol concentrations (VLEC) (≤0.1%, vol/vol). In contrast to the...

Lipid II-Based Antimicrobial Activity of the Lantibiotic Plantaricin C

Wiedemann, Imke, Böttiger, Tim, Bonelli, Raquel Regina, Schneider, Tanja, Sahl, Hans-Georg, Martínez, Beatriz

We analyzed the mode of action of the lantibiotic plantaricin C (PlnC), produced by Lactobacillus plantarum LL441. Compared to the well-characterized type A lantibiotic nisin and type B lantibiotic...

Failures in Clinical Treatment of Staphylococcus aureus Infection with Daptomycin Are Associated with Alterations in Surface Charge, Membrane Phospholipid Asymmetry, and Drug Binding▿

Jones, Tiffanny, Yeaman, Michael R., Sakoulas, George, Yang, Soo-Jin, Proctor, Richard A., Sahl, Hans-Georg, ...

Increasingly frequent reports have described the in vivo loss of daptomycin susceptibility in association with clinical treatment failures. The mechanism(s) of daptomycin resistance is not well...

Insights into the Mode of Action of Chitosan as an Antibacterial Compound▿ †

Raafat, Dina, Von Bargen, Kristine, Haas, Albert, Sahl, Hans-Georg

Chitosan is a polysaccharide biopolymer that combines a unique set of versatile physicochemical and biological characteristics which allow for a wide range of applications. Although its antimicrobial...

Specific Interaction of the Unmodified Bacteriocin Lactococcin 972 with the Cell Wall Precursor Lipid II▿

Martínez, Beatriz, Böttiger, Tim, Schneider, Tanja, Rodríguez, Ana, Sahl, Hans-Georg, Wiedemann, Imke

Lactococcin 972 (Lcn972) is a nonlantibiotic bacteriocin that inhibits septum biosynthesis in Lactococcus lactis rather than forming pores in the cytoplasmic membrane. In this study, a deeper...