Isolation and characterization of transposon-induced mutants of Pseudomonas aeruginosa deficient in production of exoenzyme S.

AUTOR(ES)

Nicas, T I

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.

Documentos Relacionados

• Isolation and characterization of a transposon-induced cytotoxin-deficient mutant of Pseudomonas aeruginosa.
• Purification of Pseudomonas aeruginosa exoenzyme S.
• Functional domains of Pseudomonas aeruginosa exoenzyme S.
• Ecto-ADP-ribosyltransferase activity of Pseudomonas aeruginosa exoenzyme S.
• Molecular genetics of a transposon-induced dominant mutation in the Drosophila locus Glued.