Interaction of Clostridium perfringens δ toxin with erythrocyte and liposome membranes and relation with the specific binding to the ganglioside GM2

Jolivet-Reynaud, Colette; Hauttecoeur, Bernard; Alouf, Joseph E.

doi:10.1016/0041-0101(89)90005-6

Cited by 26 publications

(26 citation statements)

References 39 publications

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“…As Delta toxin was reported to specifically bind to ganglioside G M2 [7], we tested the inhibition of Delta toxin hemolytic activity with various gangliosides. prDelta was incubated with gangliosides for 5 min and then tested for hemolytic activity with sheep red blood cells.…”

Section: Resultsmentioning

confidence: 99%

“…Indeed, the hemolytic activity of Delta toxin as well as the binding of iodinated toxin to target erythrocytes is preferentially inhibited by G M2 [2], [6]. In addition, iodinated Delta toxin was shown to specifically bind to ganglioside G M2 extracted from membrane of sensitive cells and to liposome containing G M2 [7]. Thus Delta toxin was revealed to be an excellent tool for probing G M2 on cell membranes.…”

Section: Introductionmentioning

confidence: 99%

“…In addition, Delta toxin selectively lyses malignant cells expressing G M2 , such as carcinoma Me180, melanoma A375, and neuroblastoma C1300, and in vivo administration of Delta toxin to mice bearing these tumors significantly reduces tumor growth [8]. However, the mechanism of cytotoxicity remains unclear, since Delta toxin was reported to not insert into cell membrane and to induce membrane lysis by an unknown process [6], [7].…”

Section: Introductionmentioning

confidence: 99%

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Clostridium perfringens Delta Toxin Is Sequence Related to Beta Toxin, NetB, and Staphylococcus Pore-Forming Toxins, but Shows Functional Differences

et al. 2008

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Clostridium perfringens produces numerous toxins, which are responsible for severe diseases in man and animals. Delta toxin is one of the three hemolysins released by a number of C. perfringens type C and possibly type B strains. Delta toxin was characterized to be cytotoxic for cells expressing the ganglioside GM2 in their membrane. Here we report the genetic characterization of Delta toxin and its pore forming activity in lipid bilayers. Delta toxin consists of 318 amino acids, its 28 N-terminal amino acids corresponding to a signal peptide. The secreted Delta toxin (290 amino acids; 32619 Da) is a basic protein (pI 9.1) which shows a significant homology with C. perfringens Beta toxin (43% identity), with C. perfringens NetB (40% identity) and, to a lesser extent, with Staphylococcus aureus alpha toxin and leukotoxins. Recombinant Delta toxin showed a preference for binding to GM2, in contrast to Beta toxin, which did not bind to gangliosides. It is hemolytic for sheep red blood cells and cytotoxic for HeLa cells. In artificial diphytanoyl phosphatidylcholine membranes, Delta and Beta toxin formed channels. Conductance of the channels formed by Delta toxin, with a value of about 100 pS to more than 1 nS in 1 M KCl and a membrane potential of 20 mV, was higher than those formed by Beta toxin and their distribution was broader. The results of zero-current membrane potential measurements and single channel experiments suggest that Delta toxin forms slightly anion-selective channels, whereas the Beta toxin channels showed a preference for cations under the same conditions. C. perfringens Delta toxin shows a significant sequence homolgy with C. perfringens Beta and NetB toxins, as well as with S. aureus alpha hemolysin and leukotoxins, but exhibits different channel properties in lipid bilayers. In contrast to Beta toxin, Delta toxin recognizes GM2 as receptor and forms anion-selective channels.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Clostridium perfringens Delta Toxin Is Sequence Related to Beta Toxin, NetB, and Staphylococcus Pore-Forming Toxins, but Shows Functional Differences

et al. 2008

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“…Delta toxin is an haemolysin for erythrocytes of eventoed ungulates, which also lyses other eukaryotic cells such as human monocytes, rabbit macrophages and platelets from human, rabbit, goat and guinea pigs (Jolivet-Reynaud et al, 1988, 1989.…”

Section: Heptameric β-Pfts Forming Small Pores Aerolysin and Related mentioning

confidence: 99%

Bacterial protein toxins and lipids: pore formation or toxin entry into cells

Geny

Popoff

2006

Biology of the Cell

119

104

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Lipids are hydrophobic molecules which play critical functions in cells, in particular, they are essential constituents of membranes, whereas bacterial toxins are mainly hydrophilic proteins. All bacterial toxins interact first with their target cells by recognizing a surface receptor, which is either a lipid or a lipid derivative, or another compound but in a lipid environment. Most bacterial toxins are PFTs (pore‐forming toxins) which oligomerize and insert into the lipid bilayer. A common mechanism of action involves the formation of a β‐barrel structure, resulting from the assembly of individual β‐hairpin(s) from individual monomers. An essential step for intracellular active toxins is to translocate their enzymatic part into the cytosol. Some toxins use a translocation mechanism based on pore formation similar to that of PFTs, others undergo a yet unclear ‘chaperone’ process.

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“…They participate in vital processes, such as immune or nervous systems, as molecules responsible for cell-cell and cell-ligand interactions [1,2]. In particular, a series of gangliosides, such as GM1, GM2 and GM3, are important as regulatory factors for the differentiation of the central nervous system and serve as cell-attachment receptors for some viruses, bacteria and bacterial toxins [3,4]. Moreover, many profound relationships between those gangliosides and a number of cancers and diseases have been demonstrated [5,6].…”

Section: Introductionmentioning

confidence: 99%

Design and synthesis of versatile ganglioside probes for carbohydrate microarrays

et al. 2008

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Interaction of Clostridium perfringens δ toxin with erythrocyte and liposome membranes and relation with the specific binding to the ganglioside GM2

Cited by 26 publications

References 39 publications

Clostridium perfringens Delta Toxin Is Sequence Related to Beta Toxin, NetB, and Staphylococcus Pore-Forming Toxins, but Shows Functional Differences

Clostridium perfringens Delta Toxin Is Sequence Related to Beta Toxin, NetB, and Staphylococcus Pore-Forming Toxins, but Shows Functional Differences

Bacterial protein toxins and lipids: pore formation or toxin entry into cells

Design and synthesis of versatile ganglioside probes for carbohydrate microarrays

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