Morphological changes associated with the extrusion of protein induced in the polymorphonuclear leucocyte by staphylococcal leucocidin

Woodin, A. M.; French, John E.; Marchesi, V.

doi:10.1042/bj0870567

Cited by 35 publications

(13 citation statements)

References 8 publications

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“…Moreover, leucocidin demonstrably increases the permeability of the plasmalemma to calcium; and calcium itself (in the absence of leucocidin) releases the granule-bound leucocytic enzymes under conditions where it penetrates the cell membrane readily (Woodin & Wienecke, 1963. All this is clearly analogous to the evidence my colleagues and I obtained from the adrenal medulla and the submaxillary salivary gland; and like these glands the leucocyte apparently releases its secretory products directly from membrane-limited granules to the cell exterior (Woodin, French & Marchesi, 1963).…”

Section: The Adrenal Chromaffin Cellmentioning

confidence: 57%

“…Calcium could facilitate the approximation of granule membrane and plasmalemma by changing the physico-chemical state of the cell sap in such a way as to enhance Brownian motion. Or it could promote adhesion of the two membranes: Woodin, French & Marchesi (1963) have shown that the addition of calcium to leucocytes poisoned with leucocidin causes the enzyme-containing granules to become attached to the plasmalemma; and Banks (1966b) has speculated that calcium may act similarly in the chromaffin cell by neutralizing net negative surface charges on the granules. The attachment of the granule membrane to the plasmalemma might then lead to reorganization of the two membranes by purely physical forces acting to reduce the total energy of the system by incorporating the granule membrane into the plasmalemma-much as a small soap bubble is incorporated into a larger one contiguous with it.…”

Section: The Adrenal Chromaffin Cellmentioning

confidence: 99%

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Stimulus‐secretion coupling: the concept and clues from chromaffin and other cells

Douglas

1968

British J Pharmacology

1,365

414

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Section: The Adrenal Chromaffin Cellmentioning

confidence: 57%

Section: The Adrenal Chromaffin Cellmentioning

confidence: 99%

Stimulus‐secretion coupling: the concept and clues from chromaffin and other cells

Douglas

1968

British J Pharmacology

1,365

414

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“…Thus, "PVL" remained the primary toxin of study for much of the mid-20th century (1960s to 1970s). As such, it was the first leucocidin to be purified and served to demonstrate a number of the hallmark features of these toxins (54)(55)(56)(57)(58)(59)(60)(61)(62)(63)(64)(65)(66)(67)(68)(69)(70)(71). Of his numerous contributions to the leucocidin field, Woodin provided the first evidence that active leucocidins consist of two separate protein components, designated "S," or slow (LukS-PV), and "F," or fast (LukF-PV), based on their chromatography elution profiles (Table 1).…”

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

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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“…Because of the failure of antileucocidin to inhibit the incorporation of 32p in the leucocidin-treated cell the participation of the two components of leucocidin is not ino q cs volved. The appearance of a new exchange reaction need not be hypothesized, for the process of fusion of the surface of the vesicles with that of the cell surface (Woodin, French & Marchesi, 1963) will result in a spatial rearrangement of molecules in these surfaces and it is possible that by this means 0 + : 3. In the presence of fluoride, iodoacetate or arsenate the incorporation of 3p2 into the lipids and nucleotides of the leucocidin-treated leucocyte is partially inhibited.…”

Section: Discussionmentioning

confidence: 99%

The incorporation of radioactive phosphorus in the leucocyte during the extrusion of protein induced by staphylococcal leucocidin

Woodin¹,

Wieneke²

1963

Biochemical Journal

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It has been shown that treatment of the polymorphonuclear leucocyte with leucocidin stimulates the incorporation of radioactive phosphorus into the phospholipids of the cell (Woodin, 1962). The radioactivity of the precursors was not known and so it was uncertain if this represented an increased turnover. The present paper shows that the stimulated incorporation of radioactive phosphorus is found in the nucleotides and other acidsoluble compounds of the leucocidin-treated leucocyte. There is no evidence for a causal connexion between this stimulated incorporation and the extrusion of protein from the granules of the leucocyte. METHODSThe two components of leucocidin were crystallized as described by Woodin (1960); unless otherwise indicated they were added to cell suspensions to give 2 jig./108 cells.Polymorphonuclear leucocytes were obtained from peritoneal exudates of rabbits (Woodin, 1962) and will be referred to below as leucocytes. ATP and ADP were obtained from C. F. Boehringer und Soehne, Mannheim, Germany; GTP and GDP were obtained from the Sigma Chemical Co., St Louis, Mo., U.S.A. The solutions used for suspending the cells were Hanks (1948) Incorporation of 32p into the nucleotide& of the leucocyte.Tubes containing 5 x 109 cells in 10 ml. of Hanks solution were incubated for 10 min. at 370 and then leucocidin was added to one tube and 82p (0.05 ml. containing 107 counts/ min.) was added to both tubes. Incubation was continued for 10 min. and the tubes were cooled in ice. They were centrifuged at 0°for 5 min. at 2000 rev./min. and the supernatant was rejected. The cell pellets were extracted for 2 hr. at room temperature with 20 vol. of chloroformmethanol (2:1, v/v). The suspensions were centrifuged and the supernatants used for the preparation of the phospholipids (see below). The cell residues were washed with ether and dried in a stream of air. The powder was then extracted with 10 ml. of ice-cold HC104 (3 %, w/v), residual ether and occluded air being removed by evacuating the tubes until the cell residues no longer floated on the surface. Extraction was continued for 30 min. and then the suspensions were centrifuged at 20 000 rev./min. for 20 min. The slightly opalescent supernatant was passed down a column containing 100 mg. of Norit and 100 mg. of Celite (Threlfall, 1957), which was then washed three times with 3 ml. of water. The effluent from the column was collected; it contained the nucleotide-free, acid-soluble fraction. The nucleotides were eluted from the washed Norit-Celite column in 7 ml. of pyridine and freeze-dried. The solid was dissolved in a small volume of water and put on paper for chromatography. After separation as described below the specific activities of the nucleotides were determined.In a similar experiment, 2 x 109 leucocytes in 12 ml. of Hanks medium were incubated alone or with added leucocidin for 10 min. 32P (01 ml.; 2 x 108 counts/min.) was added and incubation at 37°continued for 20 sec. The suspensions of cells were then diluted with 75 ml. of icecold Hanks mediu...

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Morphological changes associated with the extrusion of protein induced in the polymorphonuclear leucocyte by staphylococcal leucocidin

Cited by 35 publications

References 8 publications

Stimulus‐secretion coupling: the concept and clues from chromaffin and other cells

Stimulus‐secretion coupling: the concept and clues from chromaffin and other cells

The Bicomponent Pore-Forming Leucocidins of Staphylococcus aureus

The incorporation of radioactive phosphorus in the leucocyte during the extrusion of protein induced by staphylococcal leucocidin

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