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PMID: 3137166 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Actin-specific ADP-ribosyltransferase produced by a Clostridium difficile strain.

Infection and immunity ·Vol. 56 ·No. 9 ·1988-09-00 ·Pages 2299-306

Popoff MR, Rubin EJ, Gill DM, Boquet P

Abstract

By screening possible ADP-ribosyltransferase activities in culture supernatants from various Clostridium species, we have found one Clostridium difficile strain (CD196) (isolated in our laboratory) that is able to produce, in addition to toxins A and B, a new ADP-ribosyltransferase that was shown to covalently modify cell actin as Clostridium botulinum C2 or Clostridium perfringens E iota toxins do. The molecular weight of the CD196 ADP-ribosyltransferase (CDT) was determined to be 43 kilodaltons, and its isoelectric point was 7.8. No cytotoxic activity on Vero cells or lethal activity upon injection in mice was associated with this enzyme. CDT was neither related to C. difficile A or B toxins nor to C. botulinum C2 toxin component I. However, Vero cells cultivated in the presence of C. difficile B toxin had a lower amount of actin able to be ADP-ribosylated by CDT or C2 toxin in vitro. Antibodies raised against CDT reacted by immunoblot analysis with a 43-kilodalton protein of C. perfringens type E culture supernatant producing the iota toxin.

MeSH Terms
Actins/physiology Adult Animals Antibodies, Bacterial/physiology Cells, Cultured Clostridium/enzymology Culture Media Cytotoxins/toxicity Enterotoxins/pharmacology Female Humans Lethal Dose 50 Mice Molecular Weight Poly(ADP-ribose) Polymerases/biosynthesis,immunology,toxicity
Chemicals
Actins Antibodies, Bacterial Culture Media Cytotoxins Enterotoxins Poly(ADP-ribose) Polymerases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Popoff M R
Unité des Antigènes Bactériens, UA Centre National de la Recherche Scientifique, Paris, France.
Rubin E J
Gill D M
Boquet P
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
DOI
10.1128/iai.56.9.2299-2306.1988
Published
1988-09-00
Pages
2299-306
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC259564
Subset
IM
External Links
PubMed source DOI: 10.1128/iai.56.9.2299-2306.1988 PMC Full Text View journal details
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