Effect of carrier molecules on production and properties of extracellular hemolysin produced byStreptococcus agalactiae

Tsaihong, John Chin; Wennerstrom, D. E.

doi:10.1007/bf01588830

Cited by 22 publications

(7 citation statements)

References 14 publications

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“…Simultaneous loss of both properties was recorded in a group-B streptococcus by Lancefield (1934) and Noble et al (1 983) suggested, on epidemiological grounds, that the two properties were closely linked. Merritt and Jacobs (1976) located the pigment in the cell membrane and Tsaihong and Wennerstrom (1983) suggested that lipoteichoic acid of the cell wall is the natural carrier of haemolysin. In this present study, further parallels are established by demonstrating that pigment, like haemolysin (Marchelewicz and Duncan, 1980) is formed and released by an active process by washed cell suspensions, but retains its properties only in the presence of a suitable carrier.…”

Section: Discussionmentioning

confidence: 99%

Pigment production by Lancefield-group-B streptococci (Streptococcus agalactiae)

Tapsall

1986

Journal of Medical Microbiology

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Summary. Cells of group-B streptococci harvested in the late exponential phase of growth and suspended in starch-glucose phosphate-buffered saline extractor solution were observed to form and release pigment into solution. Filtrates of these solutions were analysed spectrophotometrically and two varieties of pigment were detected. Pigment, when freshly produced or in the presence of starch, had four absorption peaks at 520, 485, 455 and 435 nm. If albumin was substituted for starch in the extractor solution or if the starch-pigment complex was disrupted by treatment with amylase or by boiling, the four-peak pigment rapidly and irreversibly degraded to a second type with a single absorption band at 41 5 nm. The pigments formed by washed cell suspensions had absorption spectra identical to those produced by pigment formed during growth in Todd-Hewitt Broth. The formation and release of soluble pigment appeared to be an active metabolic process; a carrier molecule and an energy source were both required. Pigment yields were increased when the pH of the extractor solution was in the range 7.0-7.4 and when Mg2+, but not other divalent cations, was present. No differences in yield or type of pigment were observed when pigment was formed in anaerobic conditions. These findings support an earlier observation that group-B streptococcal pigment resembles a p carotenoid. There is some added support for the suggestion that haemolysin and pigment production by these organisms are closely linked characteristics.

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Section: Discussionmentioning

confidence: 99%

Pigment production by Lancefield-group-B streptococci (Streptococcus agalactiae)

Tapsall

1986

Journal of Medical Microbiology

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“…Haemolytic activity can be extracted from the bacterial surface using molecules such as starch, Tween or bovine serum albumin that act as stabilizer or carrier molecules (Marchlewicz & Duncan, 1980, 1981Ferrieri, 1982Dal & Monteil, 1983. As the elution profiles of the carrier molecules in gel sizeexclusion chromatography did not change in the presence of the haemolysin (Marchlewicz & Duncan, 1980;Tsaihong & Wennerstrom, 1983), it was assumed that GBS haemolysin is a small molecule. As attempts to produce specific antisera in rabbits with a haemolytic preparation obtained after gel exclusion chromatography of crude bacterial surface extracts had been unsuccessful (Dal & Monteil, 1983), the GBS haemolysin was characterized as being a nonimmunogenic substance.…”

Section: Biological Characteristicsmentioning

confidence: 99%

“…Many attempts to purify and study this elusive cytolysin have failed, raising doubts about its proteinaceous nature (Marchlewicz & Duncan, 1980, 1981Dal & Monteil, 1983;Tsaihong & Wennerstrom, 1983;Nizet et al, 1997a;). The main obstacles encountered in b-haemolysin purification include rapid loss of activity when stored at room temperature (Tapsall & Phillips, 1991), due to its high thermolability (Marchlewicz & Duncan, 1981;Dal & Monteil, 1983), and the loss of haemolytic activity upon detachment from the carrier molecule .…”

Section: Biological Characteristicsmentioning

confidence: 99%

Group B streptococcal haemolysin and pigment, a tale of twins

Rosa-Fraile¹,

Dramsi²,

Spellerberg³

2014

FEMS Microbiol Rev

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Group B streptococcus [(GBS or Streptococcus agalactiae)] is a leading cause of neonatal meningitis and septicaemia. Most clinical isolates express simultaneously a β-haemolysin/cytolysin and a red polyenic pigment, two phenotypic traits important for GBS identification in medical microbiology. The genetic determinants encoding the GBS haemolysin and pigment have been elucidated and the molecular structure of the pigment has been determined. The cyl operon involved in haemolysin and pigment production is regulated by the major two-component system CovS/R, which coordinates the expression of multiple virulence factors of GBS. Genetic analyses indicated strongly that the haemolysin activity was due to a cytolytic toxin encoded by cylE. However, the biochemical nature of the GBS haemolysin has remained elusive for almost a century because of its instability during purification procedures. Recently, it has been suggested that the haemolytic and cytolytic activity of GBS is due to the ornithine rhamnopolyenic pigment and not to the CylE protein. Here we review and summarize our current knowledge of the genetics, regulation and biochemistry of these twin GBS phenotypic traits, including their functions as GBS virulence factors.

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“…Detection of Heterocyclized ClosA Peptides via Off-line Separation and LC-MS/MS Methods-From the first reports of SLS activity in the early 1900s, structural characterization attempts have failed, and all attempts to characterize other hemolytic biotoxins from Listeria, Streptococci, or Clostridia have met the same fate (6,7,11,28,29). Therefore, any direct structural insight into a SLS-type toxin would be a major advancement.…”

Section: Closa-d Genetic Complementation Studies In Groupmentioning

confidence: 99%

Clostridiolysin S, a Post-translationally Modified Biotoxin from Clostridium botulinum

Gonzalez

Lee

Hensler

et al. 2010

Journal of Biological Chemistry

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Through elaboration of its botulinum toxins, Clostridium botulinum produces clinical syndromes of infant botulism, wound botulism, and other invasive infections. Using comparative genomic analysis, an orphan nine-gene cluster was identified in C. botulinum and the related foodborne pathogen Clostridium sporogenes that resembled the biosynthetic machinery for streptolysin S, a key virulence factor from group A Streptococcus responsible for its hallmark ␤-hemolytic phenotype. Genetic complementation, in vitro reconstitution, mass spectral analysis, and plasmid intergrational mutagenesis demonstrate that the streptolysin S-like gene cluster from Clostridium sp. is responsible for the biogenesis of a novel post-translationally modified hemolytic toxin, clostridiolysin S.Microbial virulence and survival are often defined by metabolic output. Among the many molecular species used to give a competitive advantage are hydrogen peroxide, genetically encoded small molecules, siderophores, proteins, and bacteriocins (1, 2). Streptolysin S (SLS) 2 is a well known hemolytic/ cytolytic, ribosomally encoded bacteriocin and virulence factor group A Streptococcus (GAS) (3)(4)(5). To this day, the characteristic ␤-hemolytic phenotype observed on blood agar plates is used as a clinical diagnostic tool for GAS identification. GAS is best known as the agent of acute pharyngitis (strep throat) but also may cause invasive infections, including necrotizing fasciitis and toxic shock syndrome. In the 100-year history of our knowledge of streptococcal bacteria, the precise chemical structure of this toxin has remained elusive, although the discovery of its biosynthetic gene cluster more than a decade ago (4) has guided investigations into its post-translational modification and likely heterocyclic nature (6, 7).Through recent comparative genomic analysis, an SLS-type gene cluster was identified in clostridia species including Clostridium botulinum and Clostridium sporogenes, two diseasecausing bacteria known to endanger food supplies (8 -10). Similar gene clusters were found in Staphylococcus aureus RF122, Bacillus thuringiensis, Streptococcus iniae, and Listeria monocytogenes 4b. The L. monocytogenes 4b strain is the primary serotype and causative agent for outbreaks of listeriosis (11). The S. aureus RF122 strain is responsible for bovine mastitis. S. iniae is a cytotoxic fish pathogen. This suggests that a shared metabolic output of these pathogens including SLS-like toxins may contribute to their pathogenic potential (11).Each of these SLS family gene clusters contains a similar set of genes. For instance, in C. botulinum and C. sporogenes, the closA-I genes are related by sequence to sagA-I from GAS (see Fig. 1A). Of these genes, ClosF is a protein of unknown function. ClosG, -H, and -I are ABC transporters and therefore are likely to be responsible for exporting the mature hemolytic product. ClosA is the prepropeptide (structural peptide) that is post-translationally modified to form the propeptide. ClosE has been annotated as an i...

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Effect of carrier molecules on production and properties of extracellular hemolysin produced byStreptococcus agalactiae

Cited by 22 publications

References 14 publications

Pigment production by Lancefield-group-B streptococci (Streptococcus agalactiae)

Pigment production by Lancefield-group-B streptococci (Streptococcus agalactiae)

Group B streptococcal haemolysin and pigment, a tale of twins

Clostridiolysin S, a Post-translationally Modified Biotoxin from Clostridium botulinum

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