Metallo-β-lactamase producers in environmental microbiota: New molecular class B enzyme in Janthinobacterium lividum
20 ноября 2020 года
12:47
Metallo-β-lactamase producers in environmental microbiota: New molecular class B enzyme in Janthinobacterium lividum
Текст новости:
Title: Metallo-β-lactamase producers in environmental microbiota: New molecular class B enzyme in Janthinobacterium lividum
Author, co-author: Rossolini, G. M.; Condemi, M. A.; Pantanella, F.; Docquier, Jean-Denis; Amicosante, G.; Thaller, M. C.
Abstract: Eleven environmental samples from different sources were screened for the presence of metallo-β-lactamase-producing bacteria by using a selective enrichment medium containing a carbapenem antibiotic and subsequently testing each isolate for production of EDTA-inhibitable carbapenemase activity. A total of 15 metallo-β-lactamase-producing isolates, including 10 Stenotrophomonas maltophilia isolates, 3 Chryseobacterium spp., one Aeromonas hydrophila isolate, and one Janthinobacterium lividum isolate (a species in which production of metallo-β-lactamase activity was not previously reported), were obtained from 8 samples. In the J. lividum isolate, named JAC1, production of metallo-β-lactamase activity was elicited upon exposure to β-lactams. Screening of a JAC1 genomic library for clones showing a reduced imipenem susceptibility led to the isolation of a metallo-β-lactamase determinant encoding a new member (named THIN-B) of the highly divergent subclass B3 lineage of metallo-β-lactamases. THIN-B is most closely related (35.6% identical residues) to the L1 enzyme of S. maltophilia and more distantly related to the FEZ-1 enzyme of Legionella gormanii (27.8% identity) and to the GOB-1 enzyme of Chryseobacterium meningosepticum (24.2% identity). Sequences related to blaTHIN-B, and inducible production of metallo-β-lactamase activity, were also detected in the J. lividum type strain DSM1522. Expression of the blaTHIN-B gene in Escherichia coli resulted in decreased susceptibility to several β-lactams, including penicillins, cephalosporins (including cephamycins and oxyimino cephalosporins), and carbapenems, revealing a broad substrate specificity of the enzyme. The results of this study indicated that metallo-β-lactamase-producing bacteria are widespread in the environment and identified a new molecular class B enzyme in the environmental species J. lividum.
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Текст со страницы (автоматическое получение):
Metallo-β-lactamase producers in environmental microbiota: New molecular class B enzyme in Janthinobacterium lividum
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Keywords :
[en] Aeromonas hydrophila ; Chryseobacterium ; Escherichia coli ; Janthinobacterium lividum ; Legionella ; Stenotrophomonas maltophilia ; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Environmental Microbiology ; Microbial Sensitivity Tests ; Molecular Sequence Data ; Phylogeny ; Proteobacteria ; Sequence Homology, Amino Acid
Abstract :
[en] Eleven environmental samples from different sources were screened for the presence of metallo-β-lactamase-producing bacteria by using a selective enrichment medium containing a carbapenem antibiotic and subsequently testing each isolate for production of EDTA-inhibitable carbapenemase activity. A total of 15 metallo-β-lactamase-producing isolates, including 10 Stenotrophomonas maltophilia isolates, 3 Chryseobacterium spp., one Aeromonas hydrophila isolate, and one Janthinobacterium lividum isolate (a species in which production of metallo-β-lactamase activity was not previously reported), were obtained from 8 samples. In the J. lividum isolate, named JAC1, production of metallo-β-lactamase activity was elicited upon exposure to β-lactams. Screening of a JAC1 genomic library for clones showing a reduced imipenem susceptibility led to the isolation of a metallo-β-lactamase determinant encoding a new member (named THIN-B) of the highly divergent subclass B3 lineage of metallo-β-lactamases. THIN-B is most closely related (35.6% identical residues) to the L1 enzyme of S. maltophilia and more distantly related to the FEZ-1 enzyme of Legionella gormanii (27.8% identity) and to the GOB-1 enzyme of Chryseobacterium meningosepticum (24.2% identity). Sequences related to blaTHIN-B, and inducible production of metallo-β-lactamase activity, were also detected in the J. lividum type strain DSM1522. Expression of the blaTHIN-B gene in Escherichia coli resulted in decreased susceptibility to several β-lactams, including penicillins, cephalosporins (including cephamycins and oxyimino cephalosporins), and carbapenems, revealing a broad substrate specificity of the enzyme. The results of this study indicated that metallo-β-lactamase-producing bacteria are widespread in the environment and identified a new molecular class B enzyme in the environmental species J. lividum.
Name of the research project :
Europena Training and Mobility of Researchers Network on Metallo-beta-Lactamases (grant no. FMRX-CT98-0232)
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