Biochemical properties of beta-lactamase produced by Flavobacterium odoratum

Sato, Kenichi; Fujii, Tadashi; Okamoto, R; Inoue, Matsuhisa; Mitsuhashi, Susumu

doi:10.1128/aac.27.4.612

Cited by 71 publications

(47 citation statements)

References 12 publications

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“…The results of the current study are in concordance with those of a previous Japanese study of the MICs of imipenem and meropenem for these species (25). One possible explanation, according to Sato et al, for this difference in activity between imipenem and meropenem is the presence of a ␤-lactamase which inactivates imipenem in both N. brasiliensis and N. otitidiscaviarum (26).…”

Section: Discussionsupporting

confidence: 82%

In Vitro Comparison of Ertapenem, Meropenem, and Imipenem against Isolates of Rapidly Growing Mycobacteria and Nocardia by Use of Broth Microdilution and Etest

et al. 2016

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We compared the activities of the carbapenems ertapenem, meropenem, and imipenem against 180 isolates of rapidly growing mycobacteria (RGM) and 170 isolates of Nocardia using the Clinical and Laboratory Standards Institute (CLSI) guidelines. A subset of isolates was tested using the Etest. The rate of susceptibility to ertapenem and meropenem was limited and less than that to imipenem for the RGM. Analysis of major and minor discrepancies revealed that >90% of the isolates of Nocardia had higher MICs by the broth microdilution method than by Etest, in contrast to the lower broth microdilution MICs seen for >80% of the RGM. Imipenem remains the most active carbapenem against RGM, including Mycobacterium abscessus subsp. abscessus. For Nocardia, imipenem was significantly more active only against Nocardia farcinica. Although there may be utility in testing the activities of the newer carbapenems against Nocardia, their activities against the RGM should not be routinely tested. Testing by Etest is not recommended by the CLSI.T reatment of infections due to rapidly growing mycobacteria (RGM) and Nocardia remains difficult in part because of resistance to first-line antituberculous agents (for RGM) and other antimicrobial agents (for both RGM and Nocardia) (1, 2). Previous studies with the carbapenems have shown that these agents have limited activity against most pathogenic RGM, but few data on their activity against Nocardia exist (3, 4). Although ertapenem and meropenem have been in use against clinically significant bacteria for several years, there has been a paucity of data on the activities of these agents against RGM and Nocardia. Thus, we undertook a comparative study of the in vitro susceptibilities to imipenem, meropenem, and ertapenem of the most commonly encountered species of RGM and Nocardia, including the Isolates of RGM and Nocardia were identified to the species level by molecular methods, including PCR restriction enzyme analysis (PRA) of a 441-bp sequence of the 65-kDa hsp gene (6, 7), and their antimicrobial susceptibility patterns (2,(8)(9)(10)(11)(12)(13)(14)(15). Isolates that were not identifiable by PRA were subjected to 16S rRNA (16) and/or multigene target (hsp65, secA1, rpoB, etc.) sequence analysis (3,(17)(18)(19)(20). MATERIALS AND METHODS Organisms. Clinical isolates of RGM andSusceptibility testing. The MICs of imipenem, meropenem, and ertapenem were determined by broth microdilution using the CLSI-recommended procedure and interpretive criteria for RGM and Nocardia (21) with imipenem. MIC panels were custom manufactured to include meropenem and ertapenem by Thermo Fisher (formerly Trek Diagnostics, Inc.). Since no interpretive criteria for mycobacteria and Nocardia with ertapenem are currently available, the CLSI-recommended intermediate (I) breakpoint (4 g/ml) for testing of bacteria was employed (8). These bacterial breakpoints were also applied to testing of the Nocardia with meropenem and ertapenem, which has not been addressed by the CLSI. Additional testing by Etest (AB Biodis...

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Section: Discussionsupporting

confidence: 82%

In Vitro Comparison of Ertapenem, Meropenem, and Imipenem against Isolates of Rapidly Growing Mycobacteria and Nocardia by Use of Broth Microdilution and Etest

et al. 2016

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“…The β-lactamases produced by Gram-negative and Grampositive bacteria play vital role in resistance against β-lactam antibiotics (29). Mammeri et al (18) proposed that although Myroides spp.…”

Section: Discussionmentioning

confidence: 99%

Antibacterial activities of multi drug resistant Myroides odoratimimus bacteria isolated from adult flesh flies (Diptera: Sarcophagidae) are independent of metallo beta-lactamase gene

Dharne¹,

Gupta²,

Rangrez³

et al. 2008

Braz. J. Microbiol.

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Flesh flies (Diptera: Sarcophagidae) are well known cause of myiasis and their gut bacteria have never been studied for antimicrobial activity against bacteria. Antimicrobial studies of Myroides spp. are restricted to nosocomial strains. A Gram-negative bacterium, Myroides sp., was isolated from the gut of adult flesh flies (Sarcophaga sp.) and submitted to evaluation of nutritional parameters using Biolog GN, 16S rRNA gene sequencing, susceptibility to various antimicrobials by disc diffusion method and detection of metallo β-lactamase genes (TUS/MUS). The antagonistic effects were tested on Gram-negative and Gram-positive bacteria isolated from human clinical specimens, environmental samples and insect mid gut. Bacterial species included were Aeromonas hydrophila, A. culicicola, Morganella morganii subsp. sibonii, Ochrobactrum anthropi, Weissella confusa, Escherichia coli, Ochrobactrum sp., Serratia sp., Kestersia sp., Ignatzschineria sp., Bacillus sp. The Myroides sp. strain was resistant to penicillin-G, erythromycin, streptomycin, amikacin, kanamycin, gentamycin, ampicillin, trimethoprim and tobramycin. These strain showed antibacterial action against all bacterial strains except W. confusa, Ignatzschineria sp., A. hydrophila and M. morganii subsp. sibonii. The multidrug resistance of the strain was similar to the resistance of clinical isolates, inhibiting growth of bacteria from clinical, environmental and insect gut samples. The metallo β-lactamase (TUS/MUS) genes were absent, and resistance due to these genes was ruled out, indicating involvement of other secretion machinery.

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“…Interest in this group of enzymes has grown recently since an increasing number of metallo-1-lactamases have been described in several gram-negative species which share the important characteristic of being able to hydrolyze carbapenem compounds (2,7,9,22,25,26,31). Carbapenems are new P-lactam antibiotics of great therapeutic potential, since they are not hydrolyzed by most bacterial 3-lactamases and show a broad spectrum of activity.…”

mentioning

confidence: 99%

“…The prototype for this group of enzymes is the 1-lactamase II of Bacillus cereus, which has long been studied as a model of metallo-13-lactamases and for which molecular sequence data, along with enzymologic and crystallographic data, are available (3,12,17,27). In the molecular classification of 1-lactamases, a class B was devised for this enzyme (1).Interest in this group of enzymes has grown recently since an increasing number of metallo-1-lactamases have been described in several gram-negative species which share the important characteristic of being able to hydrolyze carbapenem compounds (2,7,9,22,25,26,31). Carbapenems are new P-lactam antibiotics of great therapeutic potential, since they are not hydrolyzed by most bacterial 3-lactamases and show a broad spectrum of activity.…”

mentioning

confidence: 99%

The Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-beta-lactamases

1991

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An Aeromonas hydrophila gene, named cphA, coding for a carbapenem-hydrolyzing metallo-,I-lactamase, was cloned in Escherichia coli by screening an Aeromonas genomic library for clones able to grow on imipenem-containing medium. From sequencing data, the cloned cphA gene appeared able to code for a polypeptide of 254 amino acids whose sequence includes a potential N-terminal leader sequence for targeting the protein to the periplasmic space. These data were in agreement with the molecular mass of the original Aeromonas enzyme and of the recombinant enzyme produced in E. coli, evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of crude P-lactamase preparations followed by renaturation treatment for proteins separated in the gel and localization of protein bands showing carbapenem-hydrolyzing I-lactamase activity by a modified iodometric technique. The deduced amino acid sequence of the CphA enzyme showed regions of partial homology with both the I-lactamase II of Bacillus cereus and the CfiA I-lactamase of Bacteroides fragilis. Sequence homologies were more pronounced in the regions encompassing the amino acid residues known in the enzyme of B. cereus to function as ligand-binding residues for the metal cofactor. The CphA enzyme, however, appeared to share a lower degree of similarity with the two other enzymes, which, in turn, seemed more closely related to each other. These results, therefore, suggest the existence of at least two molecular subclasses within molecular class B metallo-,I-lactamases.In recent classification schemes for ,B-lactamases, a distinct grouping has been reserved for those enzymes requiring a metal cofactor for activity (metallo-1-lactamases) (1, 4, 5). The prototype for this group of enzymes is the 1-lactamase II of Bacillus cereus, which has long been studied as a model of metallo-13-lactamases and for which molecular sequence data, along with enzymologic and crystallographic data, are available (3,12,17,27). In the molecular classification of 1-lactamases, a class B was devised for this enzyme (1).Interest in this group of enzymes has grown recently since an increasing number of metallo-1-lactamases have been described in several gram-negative species which share the important characteristic of being able to hydrolyze carbapenem compounds (2,7,9,22,25,26,31). Carbapenems are new P-lactam antibiotics of great therapeutic potential, since they are not hydrolyzed by most bacterial 3-lactamases and show a broad spectrum of activity.Information currently available on carbapenem-hydrolyzing (CH) metallo-1-lactamases is limited, in most cases, to a few biochemical features and suggests the existence of different molecular species within this group of enzymes (5). Molecular sequence data are presently available only for the CfiA P-lactamase of Bacteroides fragilis TAL2480 (28) and for the ,B-lactamase II of B. cereus 569/H (12) and 5/B/6 (17). A strong sequence similarity exists between these two enzymes (28), suggesting that the CfiA enzyme also belongs to molecular class B...

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Biochemical properties of beta-lactamase produced by Flavobacterium odoratum

Cited by 71 publications

References 12 publications

In Vitro Comparison of Ertapenem, Meropenem, and Imipenem against Isolates of Rapidly Growing Mycobacteria and Nocardia by Use of Broth Microdilution and Etest

In Vitro Comparison of Ertapenem, Meropenem, and Imipenem against Isolates of Rapidly Growing Mycobacteria and Nocardia by Use of Broth Microdilution and Etest

Antibacterial activities of multi drug resistant Myroides odoratimimus bacteria isolated from adult flesh flies (Diptera: Sarcophagidae) are independent of metallo beta-lactamase gene

The Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-beta-lactamases

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