Abstract
We compared the abilities of structurally related cationic cyclodextrins to inhibit Bacillus anthracis lethal toxin and Staphylococcus aureus α-hemolysin. We found that both β- and γ-cyclodextrin derivatives effectively inhibited anthrax toxin action by blocking the transmembrane oligomeric pores formed by the protective antigen (PA) subunit of the toxin, whereas α-cyclodextrins were ineffective. In contrast, α-hemolysin was selectively blocked only by β-cyclodextrin derivatives, demonstrating that both symmetry and size of the inhibitor and the pore are important.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, N.I.H., Intramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antigens, Bacterial / chemistry
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Bacterial Toxins / chemistry*
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Cell Death / drug effects
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Cell Line
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Hemolysin Proteins / chemistry
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Molecular Conformation
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Staphylococcus aureus / metabolism
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alpha-Cyclodextrins / chemistry*
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beta-Cyclodextrins / chemistry*
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gamma-Cyclodextrins / chemistry*
Substances
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Antigens, Bacterial
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Bacterial Toxins
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Hemolysin Proteins
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alpha-Cyclodextrins
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anthrax toxin
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beta-Cyclodextrins
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gamma-Cyclodextrins