Abstract
Background: VIM (Verona Integron-encoded Metallo-beta-lactamase) is a member of the Metallo-Beta-Lactamases (MBLs), and is able to hydrolyze all beta-lactams antibiotics, except for monobactams, and including carbapenems. Here we characterize a VIM-producing IncA plasmid isolated from a clinical ST69 Escherichia coli strain from an Italian Long-Term Care Facility (LTCF) inpatient. Methods: An antimicrobial susceptibility test and conjugation assay were carried out, and the transferability of the blaVIM-type gene was confirmed in the transconjugant. Whole-genome sequencing (WGS) of the strain 550 was performed using the Sequel I platform. Genome assembly was performed using “Microbial Assembly”. Genomic analysis was conducted by uploading the contigs to ResFinder and PlasmidFinder databases. Results: Assembly resulted in three complete circular contigs: the chromosome (4,962,700 bp), an IncA plasmid (p550_IncA_VIM_1; 162,608 bp), harboring genes coding for aminoglycoside resistance (aac(6′)-Ib4, ant(3″)-Ia, aph(3″)-Ib, aph(3′)-XV, aph(6)-Id), beta-lactam resistance (blaSHV-12, blaVIM-1), macrolides resistance (mph(A)), phenicol resistance (catB2), quinolones resistance (qnrS1), sulphonamide resistance (sul1, sul2), and trimethoprim resistance (dfrA14), and an IncK/Z plasmid (p550_IncB_O_K_Z; 100,306 bp), free of antibiotic resistance genes. Conclusions: The increase in reports of IncA plasmids bearing different antimicrobial resistance genes highlights the overall important role of IncA plasmids in disseminating carbapenemase genes, with a preference for the blaVIM-1 gene in Italy.
Highlights
VIM (Verona Integron-encoded Metallo-beta-lactamase) is a member of the Metallo-beta-Lactamases (MBLs), and is able to hydrolyze all beta-lactams antibiotics, except for monobactams, but including carbapenems
VIM-1 and VIM-4 are geographically predominant in Europe, VIM-2 is globally distributed in P. aeruginosa, VIM-3 is widespread in Taiwan, VIM-6 in Asia, and VIM-7 in USA [3]
In916 has been identified in Escherichia coli (E. coli), Klebsiella pneumoniae (K. pneumoniae), Enterobacter cloacae (E. cloacae), Klebsiella aerogenes (K. aerogenes), and Klebsiella oxytoca (K. oxytoca); In339 has been reported in P. aeruginosa and Acinetobacter baumannii (A. baumannii); and In496 in P. aeruginosa and Pseudomonas putida (P. putida) [5]
Summary
VIM (Verona Integron-encoded Metallo-beta-lactamase) is a member of the Metallo-beta-Lactamases (MBLs), and is able to hydrolyze all beta-lactams antibiotics, except for monobactams, but including carbapenems. The VIM family was first detected and described in Italy from a Pseudomonas aeruginosa (P. aeruginosa) strain isolated in 1997 [1]; to date, 69 different enzyme variants have been described and grouped in sub-lineages: VIM-1 like, VIM-2 like, and VIM-7 like [2]. Among MBLs, VIM enzymes are commonly detected in European/Mediterranean countries such as Italy and Greece. The blaVIM-type genes are often inserted within class 1 integrons and located on plasmids playing a key role in the interspecies distribution of such determinants [4]. The blaVIM genes are mainly reported in IncN [6,7], IncY [8], IncR [9], and IncA type plasmids [10]. We characterize a VIM-producing IncA plasmid isolated from a clinical ST69 E. coli strain from an Italian Long-Term Care Facility (LTCF) inpatient
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