Abstract
Antisera which distinguished between Pseudomonas aeruginosa exoenzyme S and toxin A neutralized the adenosine diphosphate ribosyl transferase activity of the homologous, but not the heterologous, enzyme. Skin extracts and sera from burned mice infected with the exoenzyme S-producing strain P. aeruginosa 388 contained adenosine diphosphate ribosyl transferase activity that was not found in skin extracts or sera from uninfected mice. On the basis of immunological reactivity and enzymatic properties, the adenosine diphosphate ribosyl transferase activity present in skin extracts and sera from P. aeruginosa 388-infected mice was identified as exoenzyme S. Active elongation factor 2 levels in tissues from strain 388-infected mice were normal at 24 h postinfection, indicating that strain 388 does not produce detectable amounts of toxin A in vivo. An unexpected finding in this investigation was the presence of exoenzyme S-inactivating activity in the sera from some nonimmunized animals.
MeSH Terms
Animals
Bacterial Toxins/biosynthesis
Burns/complications,enzymology
Dithiothreitol/pharmacology
Female
Mice
Nucleoside Diphosphate Sugars
Nucleotidyltransferases/biosynthesis
Pentosyltransferases/biosynthesis
Pseudomonas Infections/complications,enzymology
Pseudomonas aeruginosa/enzymology
Ribose/analogs & derivatives
Urea/pharmacology
Chemicals
Bacterial Toxins
Nucleoside Diphosphate Sugars
Ribose
Urea
Pentosyltransferases
Nucleotidyltransferases
Dithiothreitol
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Bjorn M J
Pavlovskis O R
Thompson M R
Iglewski B H
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