Abstract
Listeriolysin O, the major virulent determinant of Listeria monocytogenes, is known for forming pores on cholesterol-rich membranes. In the present study, we reveal its other facet, rafts clustering. By immunofluorescence microscopy, we show that the glycosylphosphatidylinositol-anchored proteins CD14 and CD24, which normally exhibit uniform distribution on J774 cells, undergo clustering upon treatment with LLO. The non-raft marker transferrin receptor is unaffected by such treatment. Rafts clustering might explain the induction of tyrosine phosphorylation observed on LLO-treated cells.
MeSH terms
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Antigens, CD / biosynthesis
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Bacterial Toxins / pharmacology*
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CD24 Antigen
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Cell Line
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Cell Membrane / metabolism
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Cholesterol / chemistry
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Heat-Shock Proteins / pharmacology*
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Hemolysin Proteins
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Humans
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Lipopolysaccharide Receptors / biosynthesis
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Listeria monocytogenes / metabolism
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Membrane Glycoproteins / biosynthesis
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Membrane Microdomains / chemistry*
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Microscopy, Fluorescence
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Models, Biological
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Phosphorylation
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Signal Transduction
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Tyrosine / chemistry
Substances
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Antigens, CD
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Bacterial Toxins
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CD24 Antigen
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CD24 protein, human
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Heat-Shock Proteins
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Hemolysin Proteins
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Lipopolysaccharide Receptors
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Membrane Glycoproteins
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Tyrosine
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Cholesterol
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hlyA protein, Listeria monocytogenes