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Isolation and characterization of transposon-induced mutants of Pseudomonas aeruginosa deficient in production of exoenzyme S.
Exoenzyme S is an extracellular product of Pseudomonas aeruginosa. This enzyme catalyzes the transfer of ADP-ribose from NAD to a number of as yet unidentified eucaryotic proteins, but it is distinct from toxin A. To evaluate the role of exoenzyme S in the pathogenicity of P. aeruginosa, we isolated...
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| Main Authors: | , |
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| Formato: | Artigo |
| Idioma: | en |
| Publicado em: |
1984
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC263264/ https://ncbi.nlm.nih.gov/pubmed/6086529 |
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| Resumo: | Exoenzyme S is an extracellular product of Pseudomonas aeruginosa. This enzyme catalyzes the transfer of ADP-ribose from NAD to a number of as yet unidentified eucaryotic proteins, but it is distinct from toxin A. To evaluate the role of exoenzyme S in the pathogenicity of P. aeruginosa, we isolated transposon-induced mutants of strain 388, a clinical isolate that produces exoenzyme S but no toxin A. The transposon Tn1 was introduced by using a temperature-sensitive derivative of plasmid RP1. A Tn1-induced mutant was found which had no detectable exoenzyme S activity or antigen in culture supernatants or in cell lysates. Except for its lack of exoenzyme S and resistance to carbenicillin, this mutant was indistinguishable from the parent strain. When tested in an experimental mouse burn infection model, this Tn1-induced mutant was reduced in virulence by at least 2,000-fold, suggesting a role for exoenzyme S in the virulence of this strain. |
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