Emergence of Imipenem Resistance in a CpxA-H208P-Variant-Producing Proteus mirabilis Clinical Isolate

2020 ◽  
Author(s):  
Marion Lecuru ◽  
Marie-Hélène Nicolas-Chanoine ◽  
Sébastien Tanaka ◽  
Philippe Montravers ◽  
Laurence Armand-Lefevre ◽  
...  
Keyword(s):  
Clinical Isolate ◽  
Proteus Mirabilis ◽  
Imipenem Resistance

scholarly journals Emergence of Extensively Drug-Resistant Proteus mirabilis Harboring a Conjugative NDM-1 Plasmid and a Novel Salmonella Genomic Island 1 Variant, SGI1-Z

2015 ◽  
Vol 59 (10) ◽  
pp. 6601-6604 ◽  
Author(s):  
Shangshang Qin ◽  
Hui Qi ◽  
Qijing Zhang ◽  
Di Zhao ◽  
Zhen-Zhen Liu ◽  
...  
Keyword(s):  
Clinical Isolate ◽  
Molecular Analysis ◽  
Proteus Mirabilis ◽  
Genomic Island ◽  
Bacterial Species ◽  
Clinical Treatment ◽  
Drug Resistant ◽  
Content Type ◽  
Extensively Drug Resistant

ABSTRACTAcquisition ofblaNDM-1in bacterial species, such asProteus mirabilisthat is intrinsically resistant to tetracycline, tigecycline and colistin, will make clinical treatment extremely difficult. Here, we characterized an NDM-1-producing clinical isolate ofP. mirabilis(PM58) that displayed an extensively drug-resistant (XDR) phenotype, susceptible only to aztreonam. Molecular analysis revealed that PM58 harbored both a conjugative NDM-1 plasmid and a novelSalmonellagenomic island 1 variant on chromosome.

scholarly journals TEM-89 β-Lactamase Produced by a Proteus mirabilis Clinical Isolate: New Complex Mutant (CMT 3) with Mutations in both TEM-59 (IRT-17) and TEM-3

2001 ◽  
Vol 45 (12) ◽  
pp. 3591-3594 ◽  
Author(s):  
Catherine Neuwirth ◽  
Stephanie Madec ◽  
Eliane Siebor ◽  
Andre Pechinot ◽  
Jean-Marie Duez ◽  
...  
Keyword(s):  
Amino Acid ◽  
Clinical Isolate ◽  
Amino Acid Substitution ◽  
Proteus Mirabilis ◽  
Hydrolytic Activity ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Clinical Strain ◽  
Almost All

ABSTRACT TEM-89 (CMT-3) is the first complex mutant β-lactamase produced by a clinical strain of Proteus mirabilis (strain Pm 631). This new enzyme, which has a pI of 6.28, is derived from TEM-3 and has a single amino acid substitution also encountered in TEM-59 (inhibitor-resistant TEM β-lactamase IRT-17): Ser-130 to Gly. TEM-89 hydrolyzed penicillins to the same extent that TEM-3 did but lost almost all hydrolytic activity for cephalosporins and, like TEM-59, was highly resistant to inhibitors.

scholarly journals Chromosomally Encoded blaCMY-2 Located on a Novel SXT/R391-Related Integrating Conjugative Element in a Proteus mirabilis Clinical Isolate

2010 ◽  
Vol 54 (9) ◽  
pp. 3545-3550 ◽  
Author(s):  
Sohei Harada ◽  
Yoshikazu Ishii ◽  
Tomoo Saga ◽  
Kazuhiro Tateda ◽  
Keizo Yamaguchi
Keyword(s):  
Nucleotide Sequence ◽  
Clinical Isolate ◽  
Proteus Mirabilis ◽  
Hot Spot ◽  
Gram Negative Bacteria ◽  
High Similarity ◽  
New Host ◽  
Gram Negative ◽  
Antimicrobial Resistance Genes ◽  
Serovar Typhimurium

ABSTRACT Integrating conjugative elements (ICEs) are mobile genetic elements that can transfer from the chromosome of a host to the chromosome of a new host through the process of excision, conjugation, and integration. Although SXT/R391-related ICEs, originally demonstrated in Vibrio cholerae O139 isolates, have become prevalent among V. cholerae isolates in Asia, the prevalence of the ICEs among Gram-negative bacteria other than Vibrio spp. remains unknown. In addition, SXT/R391-related ICEs carrying genes conferring resistance to extended-spectrum cephalosporins have never been described. Here we carried out a genetic analysis of a cefoxitin-resistant Proteus mirabilis clinical isolate, TUM4660, which revealed the presence of a novel SXT/R391-related ICE, ICEPmiJpn1. ICEPmiJpn1 had a core genetic structure showing high similarity to that of R391 and carried xis and int genes completely identical to those of R391, while an IS10-mediated composite transposon carrying bla CMY-2 was integrated into the ICE. A nucleotide sequence identical to the 3′ part of ISEcp1 was located upstream of the bla CMY-2 gene, and other genes observed around bla CMY-2 in earlier studies were also present. Furthermore, the nucleotide sequences of hot spot 2 and hot spot 4 in ICEPmiJpn1 showed high similarity to that of hot spot 2 in SXTMO10 and with a part of the nucleotide sequence found in P. mirabilis ATCC 29906, respectively. ICEPmiJpn1 was successfully transferred to Escherichia coli, Klebsiella pneumoniae, Salmonella enterica serovar Typhimurium, and Citrobacter koseri in conjugation experiments. These observations suggest that ICEs may contribute to the dissemination of antimicrobial resistance genes among clinically relevant Enterobacteriaceae, which warrants careful observation of the prevalence of ICEs, including SXT/R391-related ICEs.

scholarly journals New Plasmid-Mediated Quinolone Resistance Gene, qnrC, Found in a Clinical Isolate of Proteus mirabilis

2009 ◽  
Vol 53 (5) ◽  
pp. 1892-1897 ◽  
Author(s):  
Minghua Wang ◽  
Qinglan Guo ◽  
Xiaogang Xu ◽  
Xiaoying Wang ◽  
Xinyu Ye ◽  
...  
Keyword(s):  
Amino Acid ◽  
Resistance Gene ◽  
Clinical Isolate ◽  
Proteus Mirabilis ◽  
Amino Acid Identity ◽  
Quinolone Resistance ◽  
Clinical Strain ◽  
E Coli ◽  
Acid Protein ◽  
New Gene

ABSTRACT Since the discovery of qnrA in 1998, two additional qnr genes, qnrB and qnrS, have been described. These three plasmid-mediated genes contribute to quinolone resistance in gram-negative pathogens worldwide. A clinical strain of Proteus mirabilis was isolated from an outpatient with a urinary tract infection and was susceptible to most antimicrobials but resistant to ampicillin, sulfamethoxazole, and trimethoprim. Plasmid pHS10, harbored by this strain, was transferred to azide-resistant Escherichia coli J53 by conjugation. A transconjugant with pHS10 had low-level quinolone resistance but was negative by PCR for the known qnr genes, aac(6′)-Ib-cr and qepA. The ciprofloxacin MIC for the clinical strain and a J53/pHS10 transconjugant was 0.25 μg/ml, representing an increase of 32-fold relative to that for the recipient, J53. The plasmid was digested with HindIII, and a 4.4-kb DNA fragment containing the new gene was cloned into pUC18 and transformed into E. coli TOP10. Sequencing showed that the responsible 666-bp gene, designated qnrC, encoded a 221-amino-acid protein, QnrC, which shared 64%, 42%, 59%, and 43% amino acid identity with QnrA1, QnrB1, QnrS1, and QnrD, respectively. Upstream of qnrC there existed a new IS3 family insertion sequence, ISPmi1, which encoded a frameshifted transposase. qnrC could not be detected by PCR, however, in 2,020 strains of Enterobacteriaceae. A new quinolone resistance gene, qnrC, was thus characterized from plasmid pHS10 carried by a clinical isolate of P. mirabilis.

scholarly journals Chromosomal Amplification of the blaOXA-58 Carbapenemase Gene in a Proteus mirabilis Clinical Isolate

2016 ◽  
Vol 61 (2) ◽  
Author(s):  
Delphine Girlich ◽  
Rémy A. Bonnin ◽  
Pierre Bogaerts ◽  
Morgane De Laveleye ◽  
Daniel T. Huang ◽  
...  
Keyword(s):  
Clinical Isolate ◽  
Resistance Genes ◽  
Proteus Mirabilis ◽  
Large Subunit ◽  
Antibiotic Resistance Genes ◽  
Biochemical Tests ◽  
Content Type ◽  
Class D ◽  
Carbapenemase Gene ◽  
Human Infections

ABSTRACT Horizontal gene transfer may occur between distantly related bacteria, thus leading to genetic plasticity and in some cases to acquisition of novel resistance traits. Proteus mirabilis is an enterobacterial species responsible for human infections that may express various acquired β-lactam resistance genes, including different classes of carbapenemase genes. Here we report a Proteus mirabilis clinical isolate (strain 1091) displaying resistance to penicillin, including temocillin, together with reduced susceptibility to carbapenems and susceptibility to expanded-spectrum cephalosporins. Using biochemical tests, significant carbapenem hydrolysis was detected in P. mirabilis 1091. Since PCR failed to detect acquired carbapenemase genes commonly found in Enterobacteriaceae, we used a whole-genome sequencing approach that revealed the presence of bla OXA-58 class D carbapenemase gene, so far identified only in Acinetobacter species. This gene was located on a 3.1-kb element coharboring a bla AmpC-like gene. Remarkably, these two genes were bracketed by putative XerC-XerD binding sites and inserted at a XerC-XerD site located between the terminase-like small- and large-subunit genes of a bacteriophage. Increased expression of the two bla genes resulted from a 6-time tandem amplification of the element as revealed by Southern blotting. This is the first isolation of a clinical P. mirabilis strain producing OXA-58, a class D carbapenemase, and the first description of a XerC-XerD-dependent insertion of antibiotic resistance genes within a bacteriophage. This study revealed a new role for the XerC-XerD recombinase in bacteriophage biology.

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