Production and Purification of the Gamma Haemolysin of Staphylococcus aureus 'Smith 5R'

Fackrell, Hugh B.; Wiseman, G. M.

doi:10.1099/00221287-92-1-1

Cited by 13 publications

(4 citation statements)

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“…hlgCB forms one transcriptional unit and hlgA forms another, each harboring independent promoters [78]. HlgA and HlgB combine to form the classical γ-hemolysin (HlgAB) which was described in 1938 [7], though it was difficult to assign biological or biochemical functions to the toxin until reliable purification methods were developed in the late 1970s [79, 80]. HlgAB is particularly effective at lysing human RBCs [81] and exhibits cytolytic activity towards human and rabbit leukocytes [15, 78].…”

Section: Overviewmentioning

confidence: 99%

Staphylococcus aureus pore-forming toxins: The interface of pathogen and host complexity

Seilie

Wardenburg

2017

Seminars in Cell & Developmental Biology

173

136

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Staphylococcus aureus is a prominent human pathogen capable of infecting a variety of host species and tissue sites. This versatility stems from the pathogen’s ability to secrete diverse host-damaging virulence factors. Among these factors, the S. aureus pore-forming toxins (PFTs), α-toxin and the bicomponent leukocidins, have garnered much attention for their ability to lyse cells at low concentrations and modulate disease severity. Although many of these toxins were discovered nearly a century ago, their host cell specificity has only been elucidated over the past five to six years, starting with the discovery of the eukaryotic receptor for α-toxin and rapidly followed by identification of the leukocidin receptors. The identification of these receptors has revealed the species- and cell type-specificity of toxin binding, and provided insight into non-lytic effects of PFT intoxication that contribute to disease pathogenesis.

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Section: Overviewmentioning

confidence: 99%

Staphylococcus aureus pore-forming toxins: The interface of pathogen and host complexity

Seilie

Wardenburg

2017

Seminars in Cell & Developmental Biology

173

136

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“…It was not until the 1960s and 1970s that purified preparations of gamma-hemolysin were isolated and its lytic activity was demonstrated on red blood cells of diverse species (76)(77)(78)(79)(80)(81). Like PVL, gamma-hemolysin was purified as two separate protein subunits that were active only when combined (77,78,82,83). Fackrell and Wiseman determined that, in addition to red blood cells, gamma-hemolysin exhibited lytic activity on human leukocytes and lymphoblasts, and Szmigielski et al further measured lytic activity on rabbit polymorphonuclear leukocytes (81,84).…”

Section: Mid-to Late 20th Century: Identification Of Gammahemolysinmentioning

confidence: 99%

The Bicomponent Pore-Forming Leucocidins of Staphylococcus aureus

Alonzo

Torres

2014

Microbiol Mol Biol Rev

239

290

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SUMMARY The ability to produce water-soluble proteins with the capacity to oligomerize and form pores within cellular lipid bilayers is a trait conserved among nearly all forms of life, including humans, single-celled eukaryotes, and numerous bacterial species. In bacteria, some of the most notable pore-forming molecules are protein toxins that interact with mammalian cell membranes to promote lysis, deliver effectors, and modulate cellular homeostasis. Of the bacterial species capable of producing pore-forming toxic molecules, the Gram-positive pathogen Staphylococcus aureus is one of the most notorious. S. aureus can produce seven different pore-forming protein toxins, all of which are believed to play a unique role in promoting the ability of the organism to cause disease in humans and other mammals. The most diverse of these pore-forming toxins, in terms of both functional activity and global representation within S. aureus clinical isolates, are the bicomponent leucocidins. From the first description of their activity on host immune cells over 100 years ago to the detailed investigations of their biochemical function today, the leucocidins remain at the forefront of S. aureus pathogenesis research initiatives. Study of their mode of action is of immediate interest in the realm of therapeutic agent design as well as for studies of bacterial pathogenesis. This review provides an updated perspective on our understanding of the S. aureus leucocidins and their function, specificity, and potential as therapeutic targets.

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“…It is possible that they failed to separate the two components since resolution by isoelectric focussing in this high pH range is poor. Fackrell & Wiseman (1976a), using a combination of ultrafiltration, gel-filtration and ammonium sulphate fractionation, isolzted only one protein but this had markedly different physicochemical characteristics to the toxin isolated by other workers with a molecular mass of 45 kDa and a PI value of 6.0 (Fackrell & Wiseman, 1976 b). This protein also differed from the toxin isolated by other workers in that it had a very high specific activity against human erythrocytes.…”

Section: Introductionmentioning

confidence: 67%

Characterization of staphylococcal -lysin

Clyne

Birkbeck²,

Arbuthnott³

1992

Journal of General Microbiology

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y-Lysh was purifed from Stuphyfococcus aureus strains Smith 5R and PG23 (a toxic shock syndrome isolate) by a combination of heparin-agarose and hydroxylapatite chromatography. Both strains produced two haemolytic components, designated y1 and yz. Though each component was weakly haemolytic they acted synergistically to potentiate haemolysis on rabbit, sheep and human blood. Rabbit and sheep erythrocytes were more sensitive to lysis by y-lysin than human erythrocytes. The molecular mass of y1 was 32 kDa and its PI value was 9.4. y2 had a molecular mass of 36 kDa and a PI value of 9.3. While both trypsin and papain acted synergistically with y2 to induce increased haemolysis, no such synergism was seen with yl. Also, protease inhibitors acted to inhibit synergism between y1 and y2. These findings suggest that y1 could be a protease.

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Production and Purification of the Gamma Haemolysin of Staphylococcus aureus 'Smith 5R'

Cited by 13 publications

References 2 publications

Staphylococcus aureus pore-forming toxins: The interface of pathogen and host complexity

Staphylococcus aureus pore-forming toxins: The interface of pathogen and host complexity

The Bicomponent Pore-Forming Leucocidins of Staphylococcus aureus

Characterization of staphylococcal -lysin

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