Characterization of the chromosomal cephalosporinases produced by Acinetobacter lwoffii and Acinetobacter baumannii clinical isolates | Zendy

Mariagrazia Perilli | Zendy; Antonio Felici | Zendy; A Oratore | Zendy; Giuseppe Cornaglia | Zendy; Giovanni Bonfiglio | Zendy; Gian María Rossolini | Zendy; Gianfranco Amicosante | Zendy

Open Access

Characterization of the chromosomal cephalosporinases produced by Acinetobacter lwoffii and Acinetobacter baumannii clinical isolates

Author(s) -

Mariagrazia Perilli,

Antonio Felici,

A Oratore,

Giuseppe Cornaglia,

Giovanni Bonfiglio,

Gian María Rossolini,

Gianfranco Amicosante

Publication year - 1996

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.40.3.715

Subject(s) - acinetobacter baumannii , piperacillin , carbenicillin , sulbactam , cefotaxime , acinetobacter , microbiology and biotechnology , cephaloridine , benzylpenicillin , chemistry , ampicillin , enzyme , antibiotics , biochemistry , biology , cephalosporin , bacteria , penicillin , antibiotic resistance , imipenem , genetics , pseudomonas aeruginosa

The beta-lactamases produced by Acinetobacter lwoffii ULA-501, Acinetobacter baumannii ULA-187, and A. baumannii AC-14 strains were purified and characterized, and their kinetic interactions with several beta-lactam molecules, including substrates and inhibitors, were studied in detail. The three enzymes appeared to be cephalosporinases with different acylation efficiencies (kcat/Km ratio values), and their hydrolytic activities were inhibited by benzylpenicillin, piperacillin, and cefotaxime, which did not behave as substrates. Carbenicillin was a substrate for the beta-lactamase from A. lwoffii ULA-501, whereas it acted as a transient inactivator of the enzymes produced by the two A. baumannii strains. Clavulanic acid was unable to inactivate the three beta-lactamases, whereas sulbactam behaved as an inactivator only at a high concentration (1 mM) which is difficult to achieve during antibiotic therapy. Analysis of the interaction with 6-beta-iodopenicillanic acid also allowed us to better discriminate the three beta-lactamases analyzed in the present study, which can be included in the group 1 functional class (5).

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