In vitro synthesis of the delta-lysin of Staphylococcus aureus

Lee, K Y; Birkbeck, T. H.

doi:10.1128/iai.44.2.434-438.1984

Cited by 10 publications

(4 citation statements)

References 44 publications

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“…All features considered, the enterocin L50 system seems to have more in common with members of a small group of antimicrobial and/or hemolytic peptides secreted by staphylococci than with class II bacteriocins. These peptides, the ␦-lysin, three peptides with hemolytic activity (SLUSH A to C), and three peptides termed antigonococcal substances (AGS 1 to 3), are produced by Staphylococcus aureus (17,33) Staphylococcus lugdunensis (15), and Staphylococcus haemolyticus (57), respectively. They are ribosomally synthesized, unmodified, secreted without leader sequences or signal peptides, and do not seem to be cotranscribed with an immunity protein gene (15,17,33).…”

Section: Discussionmentioning

confidence: 99%

“…3) strongly suggests that the characteristics listed above also apply to them. The ␦-lysin, which is lytic to a wide range of eukaryotic cells, is a small peptide of only 26 amino acids which ruptures cells by forming pores selective for cations in their plasma membrane (17,33). As far as we know, the ␦-lysin has not been shown to possess antimicrobial activity.…”

Section: Discussionmentioning

confidence: 99%

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Enterocins L50A and L50B, Two Novel Bacteriocins from Enterococcus faecium L50, Are Related to Staphylococcal Hemolysins

et al. 1998

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Enterocin L50 (EntL50), initially referred to as pediocin L50 (L. M. Cintas, J. M. Rodrı́guez, M. F. Fernández, K. Sletten, I. F. Nes, P. E. Hernández, and H. Holo, Appl. Environ. Microbiol. 61:2643–2648, 1995), is a plasmid-encoded broad-spectrum bacteriocin produced by Enterococcus faecium L50. It has previously been purified from the culture supernatant and partly sequenced by Edman degradation. In the present work, the nucleotide sequence of the EntL50 locus was determined, and several putative open reading frames (ORFs) were identified. Unexpectedly, two ORFs were found to encode EntL50-like peptides. These peptides, termed enterocin L50A (EntL50A) and enterocin L50B (EntL50B), have 72% sequence identity and consist of 44 and 43 amino acids, respectively. Interestingly, a comparison of the deduced sequences of EntL50A and EntL50B with the corresponding sequences obtained by Edman degradation shows that these bacteriocins, in contrast to other peptide bacteriocins, are secreted without an N-terminal leader sequence or signal peptide. Expression in vivo and in vitro transcription/translation experiments demonstrated thatentL50A and entL50B are the only genes required to obtain antimicrobial activity, strongly indicating that their bacteriocin products are not posttranslationally modified. Both bacteriocins possess antimicrobial activity on their own, with EntL50A being the most active. In addition, when the two bacteriocins were combined, a considerable synergism was observed, especially with some indicator strains. Even though the enterocins in some respects are similar to class II bacteriocins, several conserved features common to class II bacteriocins are absent from the EntL50 system. The enterocins have more in common with members of a small group of cytolytic peptides secreted by certain staphylococci. We therefore propose that the enterocins L50A and L50B and the staphylococcal cytolysins together constitute a new family of peptide toxins, unrelated to class II bacteriocins, which possess bactericidal and/or hemolytic activity.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Enterocins L50A and L50B, Two Novel Bacteriocins from Enterococcus faecium L50, Are Related to Staphylococcal Hemolysins

et al. 1998

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“…δ-lysin is a small polypeptide of only 26 amino acids. It is secreted without a signal peptide, and it makes cation-selective channels in the phospholipid bilayers ( Lee and Birkbeck, 1984 ). δ-lysin is a virulence factor with lytic activity in a wide range of cells, such as neutrophils, macrophages, mammalian erythrocytes, and bacterial protoplasts, as well as in cellular organelles ( Julander et al, 1983 ).…”

Section: Introductionmentioning

confidence: 99%

Vancomycin modifies the expression of the agr system in multidrug-resistant Staphylococcus aureus clinical isolates

et al. 2015

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Staphylococcus aureus is an opportunistic pathogen that colonizes human hosts and causes a wide variety of diseases. Two interacting regulatory systems called agr (accessory gene regulator) and sar (staphylococcal accessory regulator) are involved in the regulation of virulence factors. The aim of this study was to evaluate the effect of vancomycin on hld and spa gene expression during the exponential and post-exponential growth phases in multidrug-resistant (MDR) S. aureus.Methods: Antibiotic susceptibility was evaluated by the standard microdilution method. The phylogenetic profile was obtained by pulsed-field gel electrophoresis (PFGE). Polymorphisms of agr and SCCmec (staphylococcal cassette chromosome mec) were analyzed by multiplex polymerase chain reaction (PCR). The expression levels of hld and spa were analyzed by reverse transcription-PCR. An enzyme-linked immunosorbent assay (ELISA) was performed to detect protein A, and biofilm formation was analyzed via crystal violet staining.Results: In total, 60.60% (20/33) of S. aureus clinical isolates were MDR. Half (10/20) of the MDR S. aureus isolates were distributed in subcluster 10, with >90% similarity among them. In the isolates of this subcluster, a high prevalence (100%) for the agrII and the cassette SCCmec II polymorphisms was found. Our data showed significant increases in hld expression during the post-exponential phase in the presence and absence of vancomycin. Significant increases in spa expression, protein A production and biofilm formation were observed during the post-exponential phase when the MDR S. aureus isolates were challenged with vancomycin.Conclusion: The polymorphism agrII, which is associated with nosocomial isolates, was the most prevalent polymorphism in MDR S. aureus. Additionally, under our study conditions, vancomycin modified hld and spa expression in these clinical isolates. Therefore, vancomycin may regulate alternative systems that jointly participate in the regulation of these virulence factors.

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“…Such a differential effect in the presence of PEA was also observed in the synthesis and assembly among both major outer membrane proteins (17) and periplasmic proteins (24) of Escherichia coli. Here, it is likely that entirely different modes of secretion of a-lysin and 8-lysin are involved, as 8-lysin does not seem to require a signal sequence (20).…”

Section: Downloaded Frommentioning

confidence: 99%

Effect of phenethyl alcohol on Staphylococcus aureus alpha-lysin production

Lee¹,

Birkbeck²

1985

Infect Immun

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Phenethyl alcohol, at the maximum concentration which did not inhibit growth (0.3% [vol/vol]), inhibited the production of a-lysin and exoproteases but not that of 8-lysin in Staphylococcus aureus Wood 46. The inhibition of aL-lysin was reversible, and transient accumulation of cell-associated a-lysin occurred in the presence of PEA. A precursor of a-lysin ca. 3,000 daltons larger than extracellular aL-lysin was immunologically detected in the sodium dodecyl sulfate extracts of membranes and whole cells of phenethyl alcohol-treated S. aureus cultures. Also, a degraded form of a-lysin was detected in membranes prepared from cells lysed by lysostaphin but not in membranes from cells lysed with an X-press.

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In vitro synthesis of the delta-lysin of Staphylococcus aureus

Cited by 10 publications

References 44 publications

Enterocins L50A and L50B, Two Novel Bacteriocins from Enterococcus faecium L50, Are Related to Staphylococcal Hemolysins

Enterocins L50A and L50B, Two Novel Bacteriocins from Enterococcus faecium L50, Are Related to Staphylococcal Hemolysins

Vancomycin modifies the expression of the agr system in multidrug-resistant Staphylococcus aureus clinical isolates

Effect of phenethyl alcohol on Staphylococcus aureus alpha-lysin production

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