Abstract
A human pathogenic strain of Bacillus cereus produces an exoenzyme which selectively ADP-ribosylates 20-25 kDa GTP-binding proteins in platelet membranes. Pre-ADP-ribosylation of rho proteins of human platelet membranes with Clostridium botulinum exoenzyme C3 or Clostridium limosum exoenzyme inhibits subsequent ADP-ribosylation by the exoenzyme from B. cereus indicating similar substrate specificity of the transferases. The ADP-ribosyltransferase from B. cereus reveals no immunological cross-reactivity with C. botulinum C3 and C. limosum exoenzyme.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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ADP Ribose Transferases / immunology
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ADP Ribose Transferases / metabolism
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Adenosine Diphosphate / metabolism
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Bacillus cereus / enzymology*
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Blood Platelets / metabolism
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Botulinum Toxins*
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Clostridium / enzymology
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Cross Reactions
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GTP-Binding Proteins / metabolism*
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Membrane Proteins / metabolism
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Poly(ADP-ribose) Polymerases / immunology
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Poly(ADP-ribose) Polymerases / metabolism*
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Substrate Specificity
Substances
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Membrane Proteins
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Adenosine Diphosphate
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ADP Ribose Transferases
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exoenzyme C3, Clostridium botulinum
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Poly(ADP-ribose) Polymerases
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Botulinum Toxins
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GTP-Binding Proteins