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  • 1
    Electronic Resource
    Electronic Resource
    Mechanistic studies of lantibiotic-induced permeabilization of phospholipid vesicles (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 1606-1614 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00005a017
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  • 2
    Electronic Resource
    Electronic Resource
    Pep5, a new lantibiotic: structural gene isolation and prepeptide sequence (1989)
    Springer
    Archives of microbiology 152 (1989), S. 16-19 
    Details
    ISSN: 1432-072X
    Keywords: Lantibiotic ; Pep5 ; Nucleotide sequence ; Staphylococcus epidermidis 5 ; Lanthionine ; Non-proteinogenic amino acids ; Post-translational modification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A wobbled 14-mer oligonucleotide was derived from the amino acid sequence of the 34-residue propeptide of the lantibiotic Pep5 (Kellner et al. 1989). Using this hybridization probe, the structural gene of Pep5, pepA, was located on the 18.6 kbp plasmid pED503. The nucleotide sequence of pepA codes for a prepeptide with 60 residues and proves that Pep5 is ribosomally synthesized. The N-terminus of the prepeptide has a high α-helix probability and a characteristic proteolytic cleavage site precedes the C-terminal 34-residue propeptide. Our present theory is that maturation of Pep5 involves (a) enzymic conversion of Thr, Ser and Cys into dehydrated amino acids and sulfide bridges, (b) membrane translocation and cleavage of the modified prepeptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00447005
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  • 3
    Electronic Resource
    Electronic Resource
    Induction of autolysis of staphylococci by the basic peptide antibiotics Pep 5 and nisin and their influence on the activity of autolytic enzymes (1985)
    Springer
    Archives of microbiology 141 (1985), S. 249-254 
    Details
    ISSN: 1432-072X
    Keywords: Staphylococcin-like peptide Pep 5 ; Nisin ; Autolytic enzymes of Staphylococcus cohnii 22 ; Regulation of autolysis ; Cationic peptides ; Lipoteichoic acids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pep 5 and nisin are cationic bactericidal peptides which were shown to induce autolysis in Staphylococcus cohnii 22. In contrast to nisin, Pep 5 induced lysis could be stimulated in the presence of glucose. Addition of lipoteichoic acids (LTA) (d-alanine:phosphorus=0.475:1) inhibited all effects of Pep 5 on susceptible cells in a molar ratio LTA:Pep 5 of 10:1. Treatment of S. cohnii 22 with Pep 5 or nisin for 20 min and subsequent washing with 2.5 M NaCl released autolysin activity. Crude preparations of the hydrolyzing enzymes produced free amino groups as well as polysaccharide fragments from the murein backbone, suggesting the presence of a muramidase or glucosamidase, and endopeptidase or amidase. Both enzyme activities were inhibited by lipoteichoic acid; they could be fully reactivated by addition of Pep 5 in sufficient concentrations. The velocity of hydrolysis was not influenced by nisin, whereas it was doubled in presence of Pep 5. The results are discussed in view of a possible mechanism of induction of lysis by Pep 5 and nisin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408067
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  • 4
    Electronic Resource
    Electronic Resource
    Efflux of low-Mr substances from the cytoplasm of sensitive cells caused by the staphylococcin-like agent Pep 5 (1983)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 16 (1983), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1983.tb00262.x
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  • 5
    Electronic Resource
    Electronic Resource
    Cloning, sequencing and production of the lantibiotic mersacidin (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 127 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Mersacidin is a lanthionine-containing peptide antibiotic that shows a good in vivo efficiency against methicillin-resistant Staphylococcus aureus. It is excreted during early stationary phase and could be purified from culture supernatant in a one-step procedure by reversed phase HPLC. Its structural gene was cloned from chromosomal DNA of the producer strain Bacillus subtilis HIL Y-85,54728. Sequencing revealed that pre-mersacidin consists of an unusually long 48 amino acid leader sequence and a 20 amino acid propeptide part which is modified during biosynthesis to the mature lantibiotic. The comparison of the mersacidin prepeptide with those of hitherto known lantibiotics demonstrates that mersacidin is more closely related to type B lantibiotic cinnamycin than to type A lantibiotics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07460.x
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  • 6
    Electronic Resource
    Electronic Resource
    Susceptibility of bacterial, eukaryotic and artificial membranes to the disruptive action of the cationic peptides Pep 5 and nisin (1986)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 34 (1986), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The cationic bactericidal peptides Pep 5 and nisin render membranes permeable to low-Mr compounds. All Gram-positive bacteria treated with these peptides showed an immediate efflux of entrapped radioactive markers. The uptake of α-[14C]methylglucoside by the phosphoenolpyruvate-dependent phosphotransferase system was stimulated by Pep 5, supporting previous results that pep 5 abolishes the membrane potential. Oxygen consumption was inhibited, presumably due to lack of ADP. Escherichia coli became sensitive to Pep 5 and nisin when the outer membrane was bypassed by osmotic shock or by formation of cytoplasmic membrane vesicles. In contrast, Mycoplasma cells and erythrocytes were unaffected by Pep 5 and nisin in concentrations up to 1 mM. Human lung fibroblasts released only small amounts of ATP when treated with Pep 5 and nisin in μM concentrations. Eukaryotic and Mycoplasma cells were disrupted more effectively by the bee venom peptide melittin, which displays overall structural similarities to Pep 5 and nisin. Various artificial membranes were not affected by Pep 5, nisin, or melittin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1986.tb01393.x
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  • 7
    Electronic Resource
    Electronic Resource
    Lantibiotic-mediated anti-lactobacillus activity of a vaginal Staphylococcus aureus isolate (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 93 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Staphylococcus aureus strain 26 inhibited the growth of 23 of 26 lactobacilli of endocervical origin, but only two of 17 staphylococci, in deferred antagonism tests. The inhibitory agent, a bacteriocin-like inhibitory substance (BLIS) named staphylococcin Au-26, was obtained from vigorously shaken liquid cultures containing a 0.1% (v/v) supplement of Tween 80 and was purified by chromatographic fractionation on XAD-2, carboxymethyl Sephadex and reversed phase HPLC. The molecular mass of staphylococcin Au-26 was estimated by SDS-PAGE to be approx. 2700. The detection of lanthionine residues in the molecule, the high stability to heating at acidic but not alkaline pH values and inactivation by proteinases indicate that staphylococcin Au-26 is a member of the lantibiotic class of peptide antibiotics—the first reported to be produced by a S. aureus strain. Primary sequence analysis showed that the N-terminus of the molecule is isoleucine, a characteristic also displayed by the lantibiotics nisin, epidermin and gallidermin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05047.x
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  • 8
    Electronic Resource
    Electronic Resource
    Effect of leader peptide mutations on biosynthesis of the lantibiotic Pep5 (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 149 (1997), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Lantibiotics are lanthionine-containing antibiotic peptides which are synthesized from ribosomal prepeptides by post-translational modification. In order to elucidate the function of a conserved motif in the N-terminal leader sequence of lantibiotic prepeptides, three amino acids were exchanged in the leader peptide sequence of the lantibiotic Pep5. Exchanging Phe-19 for Ser and Glu-16 for Lys in the FDLEI-motif, reduced Pep5 production to 35 and 38% of the control whereas, after exchanging Asp-6 for Lys, the production was decreased only to 82%. Proteolytic fragments of Pep5 or incorrectly modified Pep5 molecules, indicative of incorrect modifications, were not found in the culture supernatant. Thus, in contrast to the biosynthesis of the lantibiotic nisin, the FDLEI-motif is not essential for biosynthesis of Pep5 and has no influence on correct ring formation or processing, but seems to be important for optimal biosynthesis rates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb10337.x
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  • 9
    Electronic Resource
    Electronic Resource
    LANTIBIOTICS: Biosynthesis and Biological Activities of Uniquely Modified Peptides from Gram-Positive Bacteria (1998)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Microbiology 52 (1998), S. 41-79 
    Details
    ISSN: 0066-4227
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract A plethora of novel gene-encoded antimicrobial peptides from animals, plants and bacteria has been described during the last decade. Many of the bacterial peptides possess modified building blocks such as thioethers and thiazoles or unsaturated and stereoinverted amino acids, which are unique among ribosomally made peptides. Genetic and biochemical studies of many of these peptides, mostly the so-called lantibiotics, have revealed the degree to which cells are capable of transforming peptides by posttranslational modification. The biosynthesis follows a general scheme: Precursor peptides are first modified and then proteolytically activated; the latter may occur prior to, concomitantly with or after export from the cell. The genes for the biosynthetic machinery are organized in clusters and include information for the antibiotic prepeptide, the modification enzymes and accessory functions such as dedicated proteases and ABC transporters as well as immunity factors and regulatory proteins. These fundamental aspects are discussed along with the biotechnological potential of the peptides and of the biosynthesis enzymes, which could be used for construction of novel, peptide-based biomedical effector molecules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.micro.52.1.41
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  • 10
    Electronic Resource
    Electronic Resource
    In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 53 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Staphylococcus aureus peptidoglycan is cross-linked via a characteristic pentaglycine interpeptide bridge. Genetic analysis had identified three peptidyltransferases, FemA, FemB and FemX, to catalyse the formation of the interpeptide bridge, using glycyl t-RNA as Gly donor. To analyse the pentaglycine bridge formation in vitro, we purified the potential substrates for FemA, FemB and FemX, UDP-MurNAc-pentapeptide, lipid I and lipid II and the staphylococcal t-RNA pool, as well as His-tagged Gly-tRNA-synthetase and His-tagged FemA, FemB and FemX. We found that FemX used lipid II exclusively as acceptor for the first Gly residue. Addition of Gly 2,3 and of Gly 4,5 was catalysed by FemA and FemB, respectively, and both enzymes were specific for lipid II-Gly1 and lipid II-Gly3 as acceptors. None of the FemABX enzymes required the presence of one or two of the other Fem proteins for activity; rather, bridge formation was delayed in the in vitro system when all three enzymes were present. The in vitro assembly system described here will enable detailed analysis of late, membrane-associated steps of S. aureus peptidoglycan biosynthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04149.x
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