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The “hidden” carbapenemase of Aeromonas hydrophila
Author(s) -
M. V. Hayes,
C. J. Thomson,
S. G. B. Amyes
Publication year - 1996
Publication title -
journal of antimicrobial chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.124
H-Index - 194
eISSN - 1460-2091
pISSN - 0305-7453
DOI - 10.1093/jac/37.1.33
Subject(s) - aeromonas hydrophila , aeromonas , cephalosporin , microbiology and biotechnology , biology , cefotaxime , bacteria , antibiotics , genetics
It has been presumed that there are just two beta-lactamases in the motile Aeromonas species, a carbapenemase and a cephalosporinase, based on the premise that all beta-lactamases can be detected by hydrolysis of the chromogenic cephalosporin, nitrocefin. However, when it was recently found that a non-motile species of Aeromonas that causes furunculosis in salmon, contained three beta-lactamases, one of which was a carbapenemase which could not be detected with nitrocefin, it was hypothesised that genetic exchange could occur between fish pathogens and human pathogens resulting in the transfer of the carbapenemase-encoding gene. This could have a potentially serious impact on intensive therapy units where carbapenems are employed. The purpose of this study was to determine whether the human pathogen Aeromonas hydrophila demonstrated the same beta-lactamase profile. After anion and cation exchange chromatography had been employed to separate the beta-lactamases of a clinical strain of A. hydrophila, three different beta-lactamases were found, one of which is a carbapenemase which does not hydrolyse nitrocefin. It is, therefore, probable that many strains of Aeromonas spp. contain a similar array of beta-lactamases which include a carbapenemase that cannot be detected with nitrocefin. Similar carbapenemases may well remain hidden in other species of bacteria unless appropriate techniques to detect the enzymes are employed.

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