Fractionation of a leucocidin from <i>Staphylococcus aureus</i>

Woodin, A. M.

doi:10.1042/bj0730225

Cited by 86 publications

(51 citation statements)

References 6 publications

(4 reference statements)

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“…It is therefore difficult to ascertain whether the leukocidal activity was strictly caused by PVL or a combination of leucocidins present within culture filtrates. We presume that it was likely the latter circumstance for most studies using S. aureus culture supernatants, prior to the purification of PVL by Woodin in the 1960s (54,55). Thus, "PVL" remained the primary toxin of study for much of the mid-20th century (1960s to 1970s).…”

Section: A Brief Historical Perspective: Identification and Early Chamentioning

confidence: 99%

The Bicomponent Pore-Forming Leucocidins of Staphylococcus aureus

Alonzo

Torres

2014

Microbiol Mol Biol Rev

236

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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Section: A Brief Historical Perspective: Identification and Early Chamentioning

confidence: 99%

The Bicomponent Pore-Forming Leucocidins of Staphylococcus aureus

Alonzo

Torres

2014

Microbiol Mol Biol Rev

236

290

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“…For quantitative estimations of enzymes, 0-3 M-ammonium acetate adjusted to the desired pH value with either 0.3 M-acetic acid or 0.3 M-NH,OH was used. For chromatography on hydroxylapatite, a stock solution of 0-5 M-phosphate buffer (pH 6.7) was prepared according to Woodin (1959 For quantitative estimations the soy bean phosphatidyl choline was homogenized in an Omnimixer blender (1600 rev./min. for 5 min.).…”

Section: Origin)mentioning

confidence: 99%

The Properties of Phospholipase Enzymes in Staphylococcal Toxins

Doery

Magnusson

Gulasekharam

et al. 1965

Journal of General Microbiology

132

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SUMMARYTwo phospholipase enzymes have been identified in toxic preparations from Staphylococcus aureus, each having a mode of action like that of phospholipase C. One enzyme hydrolysed phosphatidyl inositol and lysophosphatidyl inositol, while the other hydrolysed sphingomyelin and lysophosphatidyl choline. The latter enzyme was always associated with /I-haemolysin activity and it is concluded that P-haemolysin, sphingomyelinase and lysophospholipase are activities of one protein. A phospholipase A was also detected in a toxic preparation from an ap strain.

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“…PVL is a staphylococcal synergohymenotropic exotoxin belonging to the pore-forming toxin family (5)(6)(7). In vitro, PVL has been shown to induce lysis of host defense cells such as human polymorphonuclear neutrophils (PMNs), monocytes, and macrophages (8).…”

Section: Introductionmentioning

confidence: 99%

Staphylococcus aureus Panton-Valentine leukocidin directly targets mitochondria and induces Bax-independent apoptosis of human neutrophils

Genestier

Michallet²,

Prévost³

et al. 2005

J. Clin. Invest.

348

274

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Panton-Valentine leukocidin (PVL) is a pore-forming toxin secreted by Staphylococcus aureus that has recently been associated with necrotizing pneumonia. In the present study, we report that in vitro, PVL induces polymorphonuclear cell death by necrosis or by apoptosis, depending on the PVL concentration. PVL-induced apoptosis was associated with a rapid disruption of mitochondrial homeostasis and activation of caspase-9 and caspase-3, suggesting that PVL-induced apoptosis is preferentially mediated by the mitochondrial pathway. Polymorphonuclear cell exposure to PVL leads to mitochondrial localization of the toxin, whereas Bax, 1 of the 2 essential proapoptotic members of the Bcl-2 family, was still localized in the cytosol. Addition of PVL to isolated mitochondria induced the release of the apoptogenic proteins cytochrome c and Smac/ DIABLO. Therefore, we suggest that PVL, which belongs to the pore-forming toxin family, could act at the mitochondrion level by creating pores in the mitochondrial outer membrane. Furthermore, LukS-PV, 1 of the 2 components of PVL, was detected in lung sections of patients with necrotizing pneumonia together with DNA fragmentation, suggesting that PVL induces apoptosis in vivo and thereby is directly involved in the pathophysiology of necrotizing pneumonia.

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Fractionation of a leucocidin from Staphylococcus aureus

Cited by 86 publications

References 6 publications

The Bicomponent Pore-Forming Leucocidins of Staphylococcus aureus

The Bicomponent Pore-Forming Leucocidins of Staphylococcus aureus

The Properties of Phospholipase Enzymes in Staphylococcal Toxins

Staphylococcus aureus Panton-Valentine leukocidin directly targets mitochondria and induces Bax-independent apoptosis of human neutrophils

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