The Glycosylphosphatidylinositol-anchored Surface Glycoprotein Thy-1 Is a Receptor for the Channel-forming Toxin Aerolysin

Nelson, Kim L.; Raja, Srikumar M.; Buckley, J. Thomas

doi:10.1074/jbc.272.18.12170

Cited by 111 publications

(114 citation statements)

References 27 publications

(22 reference statements)

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“…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). Subsequently, the hemolysin from A. sobria strain AB3 (which has been named AEAER) was also reported to form pores in the membrane (4).…”

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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“…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%

Channels formed by subnanomolar concentrations of the toxin aerolysin trigger apoptosis of T lymphomas

Nelson

Brodsky²,

Buckley

1999

Cell Microbiol

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“…This toxin specifically binds to GPI-anchored proteins on mammalian cells, and the binding capacity is retained after SDS-PAGE of cellular extracts and blotting onto a nitrocellulose membrane (toxin overlay assay) (24,25). The main determinant for aerolysin binding is not the protein moiety but the glycan core common to all GPI-anchored proteins (39).…”

Section: Generation Of Cho Mutant Cell Lines Deficient In Gpi Biomentioning

confidence: 99%

Cross-talk between Caveolae and Glycosylphosphatidylinositol-rich Domains

Abrami¹,

Fivaz²,

Kobayashi³

et al. 2001

Journal of Biological Chemistry

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Most mammalian cells have in their plasma membrane at least two types of lipid microdomains, non-invaginated lipid rafts and caveolae. Glycosylphosphatidylinositol (GPI)-anchored proteins constitute a class of proteins that are enriched in rafts but not caveolae at steady state. We have analyzed the effects of abolishing GPI biosynthesis on rafts, caveolae, and cholesterol levels. GPI-deficient cells were obtained by screening for resistance to the pore-forming toxin aerolysin, which uses this class of proteins as receptors. Despite the absence of GPI-anchored proteins, mutant cells still contained lipid rafts, indicating that GPI-anchored proteins are not crucial structural elements of these domains. Interestingly, the caveolae-specific membrane proteins, caveolin-1 and 2, were up-regulated in GPI-deficient cells, in contrast to flotillin-1 and GM1, which were expressed at normal levels. Additionally, the number of surface caveolae was increased. This effect was specific since recovery of GPI biosynthesis by gene recomplementation restored caveolin expression and the number of surface caveolae to wild type levels. The inverse correlation between the expression of GPI-anchored proteins and caveolin-1 was confirmed by the observation that overexpression of caveolin-1 in wild type cells led to a decrease in the expression of GPI-anchored proteins. In cells lacking caveolae, the absence of GPI-anchored proteins caused an increase in cholesterol levels, suggesting a possible role of GPI-anchored proteins in cholesterol homeostasis, which in some cells, such as Chinese hamster ovary cells, can be compensated by caveolin up-regulation.

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The Glycosylphosphatidylinositol-anchored Surface Glycoprotein Thy-1 Is a Receptor for the Channel-forming Toxin Aerolysin

Cited by 111 publications

References 27 publications

Purification and Characterization of Enterotoxin Produced by Aeromonas sobria

Purification and Characterization of Enterotoxin Produced by Aeromonas sobria

Channels formed by subnanomolar concentrations of the toxin aerolysin trigger apoptosis of T lymphomas

Cross-talk between Caveolae and Glycosylphosphatidylinositol-rich Domains

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