The erythrocyte receptor for the channel‐forming toxin aerolysin is a novel glycosylphosphatidylinositol‐anchored protein

Cowell, Scott; Aschauer, W; Gruber, Hermann J.; Nelson, Kim L.; Buckley, J. Thomas

doi:10.1046/j.1365-2958.1997.4691828.x

Cited by 57 publications

(48 citation statements)

References 25 publications

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“…Mature aerolysin binds to its receptor on the target cell surface and then oligomerizes to form stable heptamers. The oligomers penetrate the membrane, producing well-defined channels that destroy the permeability barrier (6,26). Not only erythrocytes but also cultured cells are sensitive to aerolysin (24,26).…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Enterotoxin Produced by Aeromonas sobria

Fujii

Nomura

Kanzawa

et al. 1998

Microbiology and Immunology

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We purified the toxin of Aeromonas sobria capable of inducing a positive response in the mouse intestinal loop assay. The purified toxin showed a positive response not only in the loop assay but also in a hemolytic assay. Subsequently, we cloned the toxin gene and demonstrated that the product of this gene possessed both hemolytic and enterotoxic activities. These results showed that the enterotoxin of A. sobria possesses hemolytic activity. Nucleotide sequence determination of the toxin gene and amino acid sequence analysis of the purified toxin revealed that it is synthesized as a precursor composed of 488 amino acid residues, and that the 24 amino-terminal amino acid residues of the precursor is removed in the mature toxin. As antiserum against the purified toxin neutralized the fluid accumulation induced by living cells not only of A. sobria but also of A. hydrophila, this and antigenically related toxin(s) are thought to play an essential role in the induction of diarrhea by these organisms. The toxin-injured Chinese hamster ovary (CHO) cells induced the release of intracellular lactose dehydrogenase (LDH). The release of LDH from CHO cells and the lysis of erythrocytes by the toxin were repressed by the addition of dextran to the reaction solution, indicating that the toxin forms pores in the membranes and that the cells were injured by the osmotic gradient developed due to pore formation. However, the histopathological examination of intestinal cells exposed to the toxin showed that it caused fluid accumulation in the mouse intestinal loop without causing cellular damage.

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Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Enterotoxin Produced by Aeromonas sobria

Fujii

Nomura

Kanzawa

et al. 1998

Microbiology and Immunology

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“…Indeed although the receptors have not been identified for all these toxins, it is clear that they do not share the same acceptor sites on cells. Aerolysin has been shown to bind to GPI-anchored proteins cells (11)(12)(13)(14), and streptolysin O to cholesterol (for review, see Ref. 38).…”

Section: Discussionmentioning

confidence: 99%

“…However, different receptors were found on different cells types and a given cell type was found to have more then one receptor. For example, aerolysin was shown to bind to Thy-1 as well as other GPI-anchored proteins on Tlymphocytes, to Thy-1 and contactin in mouse brain (11,13), to VSG from Trypanosomes (13), to an 47-kDa receptor on rat erythrocytes (12) and to mainly an 80-kDa receptor on baby hamster kidney cells (14). Binding was shown to be determined both by the protein moiety and the olisaccharides of the anchor (13).…”

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confidence: 99%

Aerolysin Induces G-protein Activation and Ca2+Release from Intracellular Stores in Human Granulocytes

Krause¹,

Fivaz²,

Monod³

et al. 1998

Journal of Biological Chemistry

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Aerolysin is a pore-forming toxin that plays a key role in the pathogenesis of Aeromonas hydrophila infections. In this study, we have analyzed the effect of aerolysin on human granulocytes (HL-60 cells). Proaerolysin could bind to these cells, was processed into active aerolysin, and led to membrane depolarization, indicating that granulocytes are potential targets for this toxin. Fura-2 measurements were used to analyze the effect of aerolysin on cytosolic [Ca 2؉] homeostasis. As expected for a pore-forming toxin, aerolysin addition led to Ca 2؉ influx across the plasma membrane. In addition, the toxin triggered Ca 2؉ release from agonist and thapsigargin-sensitive intracellular Ca 2؉ stores. This Ca 2؉ release was independent of the aerolysin-induced Ca 2؉ influx and occurred in two kinetically distinct phases: an initial rapid and transient phase and a second, more sustained, phase. The first, but not the second phase was sensitive to pertussis toxin. Activation of pertussis toxin-sensitive G-proteins appeared to be a consequence of pore formation, rather than receptor activation through aerolysinbinding, as it: (i) was not observed with a binding competent, insertion-incompetent aerolysin mutant, (ii) had a marked lag time, and (iii) was also observed in response to other bacterial pore-forming toxins (staphylococcal ␣-toxin, streptolysin O) which are thought to bind to different receptors. G-protein activation through pore-forming toxins stimulated cellular functions, as evidenced by pertussis toxin-sensitive chemotaxis. Our results demonstrate that granulocytes are potential target cells for aerolysin and that in these cells, Ca 2؉ signaling in response to a pore-forming toxin involves G-proteindependent cell activation and Ca 2؉ release from intracellular stores.

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“…The toxin binds with high af®nity to several glycosylphosphatidylinositol (GPI)-anchored proteins on sensitive cells (Cowell et al, 1997;Nelson et al, 1997;Diep et al, 1998). On T lymphomas, these receptors include Thy-1 and at least one other GPI-anchored protein (Diep et al, 1998).…”

Section: Introductionmentioning

confidence: 99%