scholarly journals NDM-8 Metallo-β-Lactamase in a Multidrug-Resistant Escherichia coli Strain Isolated in Nepal

2013 ◽  
Vol 57 (5) ◽  
pp. 2394-2396 ◽  
Author(s):  
Tatsuya Tada ◽  
Tohru Miyoshi-Akiyama ◽  
Rajan K. Dahal ◽  
Manoj K. Sah ◽  
Hiroshi Ohara ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Respiratory Tract ◽  
Multidrug Resistant ◽  
Coli Strain ◽  
Enzymatic Activities ◽  
Content Type

ABSTRACTA novel metallo-β-lactamase, NDM-8, was identified in a multidrug-resistantEscherichia coliisolate, IOMTU11 (NCGM37), obtained from the respiratory tract of a patient in Nepal. The amino acid sequence of NDM-8 has substitutions at positions 130 (Asp to Gly) and 154 (Met to Leu) compared with NDM-1. NDM-8 showed enzymatic activities against β-lactams similar to those of NDM-1.

scholarly journals Biochemical Analysis of Metallo-β-Lactamase NDM-3 from a Multidrug-Resistant Escherichia coli Strain Isolated in Japan

2014 ◽  
Vol 58 (6) ◽  
pp. 3538-3540 ◽  
Author(s):  
Tatsuya Tada ◽  
Tohru Miyoshi-Akiyama ◽  
Kayo Shimada ◽  
Teruo Kirikae
Keyword(s):  
Escherichia Coli ◽  
Biochemical Analysis ◽  
Multidrug Resistant ◽  
Coli Strain ◽  
Enzymatic Activities ◽  
New Delhi ◽  
Content Type ◽  
Genetic Context

ABSTRACTNew Delhi metallo-β-lactamase-3 (NDM-3) was identified in a multidrug-resistantEscherichia coliisolate, NCGM77, obtained from the feces of a patient in Japan. The enzymatic activities of NDM-3 against β-lactams were similar to those of NDM-1, although NDM-3 showed slightly lowerkcat/Kmratios for all the β-lactams tested except for doripenem. The genetic context forblaNDM-3wastnpA-blaNDM-3-bleMBL-trpF-dsbC-tnpA-sulI-qacEdeltaI-aadA2-dfrA1, which was present on an approximately 250-kb plasmid.

scholarly journals Complete Circular Genome Sequence of a Multidrug-Resistant Escherichia coli Strain from Cuba Obtained with Nanopore and Illumina Hybrid Assembly

2019 ◽  
Vol 8 (48) ◽  
Author(s):  
Rosa Elena Hernández-Fillor ◽  
Michael Brilhante ◽  
Ivette Espinosa ◽  
Vincent Perreten
Keyword(s):  
Escherichia Coli ◽  
Genome Sequence ◽  
Antibiotic Resistance Genes ◽  
Generation Cephalosporin ◽  
Multidrug Resistant ◽  
Coli Strain ◽  
Hybrid Assembly ◽  
Content Type ◽  
Long Reads ◽  
Cephalosporin Resistance

The complete genome sequence of a multidrug-resistant Escherichia coli strain isolated from a healthy pig in Cuba was determined using short and long reads. This strain carried four plasmids, including a 42,683-kb IncX1 plasmid, which contains the third-generation cephalosporin resistance gene bla CTX-M-32 together with other disinfectant and antibiotic resistance genes.

scholarly journals Phenotypic, Biochemical, and Genetic Analysis of KPC-41, a KPC-3 Variant Conferring Resistance to Ceftazidime-Avibactam and Exhibiting Reduced Carbapenemase Activity

2019 ◽  
Vol 63 (12) ◽  
Author(s):  
Linda Mueller ◽  
Amandine Masseron ◽  
Guy Prod’Hom ◽  
Tatiana Galperine ◽  
Gilbert Greub ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Amino Acid ◽  
Klebsiella Pneumoniae ◽  
Genetic Analysis ◽  
Amino Acid Sequence ◽  
Cloning And Expression ◽  
Content Type ◽  
Amino Acid Insertion

ABSTRACT A novel KPC variant, KPC-41, was identified in a Klebsiella pneumoniae clinical isolate from Switzerland. This β-lactamase possessed a 3-amino-acid insertion (Pro-Asn-Lys) located between amino acids 269 and 270 compared to the KPC-3 amino acid sequence. Cloning and expression of the blaKPC-41 gene in Escherichia coli, followed by determination of MIC values and kinetic parameters, showed that KPC-41, compared to those of KPC-3, has an increased affinity to ceftazidime and a decreased sensitivity to avibactam, leading to resistance to ceftazidime-avibactam once produced in K. pneumoniae. Furthermore, KPC-41 exhibited a drastic decrease of its carbapenemase activity. This report highlights that a diversity of KPC variants conferring resistance to ceftazidime-avibactam already circulate in Europe.

scholarly journals NDM-12, a Novel New Delhi Metallo-β-Lactamase Variant from a Carbapenem-Resistant Escherichia coli Clinical Isolate in Nepal

2014 ◽  
Vol 58 (10) ◽  
pp. 6302-6305 ◽  
Author(s):  
Tatsuya Tada ◽  
Basudha Shrestha ◽  
Tohru Miyoshi-Akiyama ◽  
Kayo Shimada ◽  
Hiroshi Ohara ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Clinical Isolate ◽  
Urine Sample ◽  
Enzymatic Activities ◽  
Amino Acid Substitutions ◽  
New Delhi ◽  
Content Type ◽  
Carbapenem Resistant

ABSTRACTA novel New Delhi metallo-β-lactamase variant, NDM-12, was identified in a carbapenem-resistantEscherichia coliclinical isolate obtained from a urine sample from a patient in Nepal. NDM-12 differed from NDM-1 by two amino acid substitutions (M154L and G222D). The enzymatic activities of NDM-12 against β-lactams were similar to those of NDM-1, although NDM-12 showed lowerkcat/Kmratios for all β-lactams tested except doripenem. TheblaNDM-12gene was located in a plasmid of 160 kb.

scholarly journals Plasmid-Mediated Novel blaNDM-17 Gene Encoding a Carbapenemase with Enhanced Activity in a Sequence Type 48 Escherichia coli Strain

2017 ◽  
Vol 61 (5) ◽  
Author(s):  
Zhihai Liu ◽  
Yang Wang ◽  
Timothy R. Walsh ◽  
Dejun Liu ◽  
Zhangqi Shen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Treatment Options ◽  
Coli Strain ◽  
Sequence Type ◽  
Animal Origin ◽  
New Delhi ◽  
Gene Encoding ◽  
Content Type ◽  
Carbapenem Resistant

ABSTRACT Carbapenem-resistant Enterobacteriaceae (CRE) have spread worldwide, leaving very few treatment options available. New Delhi metallo-beta-lactamase (NDM) is the main carbapenemase mediating CRE resistance and is of increasing concern. NDM-positive Enterobacteriaceae of human origin are frequently identified; however, the emergence of NDM, and particularly novel variants, in bacteria of food animal origin has never been reported. Here, we characterize a novel NDM variant (assigned NDM-17) identified in a β-lactam-resistant sequence type 48 (ST48) Escherichia coli strain that was isolated from a chicken in China. Compared to NDM-1, NDM-17 had three amino acid substitutions (V88L, M154L, and E170K) that confer significantly enhanced carbapenemase activity. Compared to NDM-5, NDM-17 had only one amino acid substitution (E170K) and slightly increased isolate resistance to carbapenem, as indicated by increased MIC values. The gene encoding NDM-17 (bla NDM-17) was located on an IncX3 plasmid, which was readily transferrable to recipient E. coli strain J53 by conjugation, suggesting the possibility of the rapid dissemination of bla NDM-17. Enzyme kinetics showed that NDM-17 could hydrolyze all β-lactams tested, except for aztreonam, and had a significantly higher affinity for all β-lactams tested than did NDM-5. The emergence of this novel NDM variant could pose a threat to public health because of its transferability and enhanced carbapenemase activity.

scholarly journals Contribution of Novel Amino Acid Alterations in PmrA or PmrB to Colistin Resistance in mcr-Negative Escherichia coli Clinical Isolates, Including Major Multidrug-Resistant Lineages O25b:H4-ST131-H30Rx and Non-x

2018 ◽  
Vol 62 (9) ◽  
Author(s):  
Toyotaka Sato ◽  
Tsukasa Shiraishi ◽  
Yoshiki Hiyama ◽  
Hiroyuki Honda ◽  
Masaaki Shinagawa ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Bacterial Growth ◽  
Parent Strain ◽  
Lipid A ◽  
Multidrug Resistant ◽  
Clinical Isolates ◽  
Resistant Isolate ◽  
Colistin Resistance ◽  
Content Type

ABSTRACT Colistin is a last-line drug for multidrug-resistant Gram-negative bacteria. We previously reported four plasmid-mediated colistin resistance (mcr) gene-negative colistin-resistant Escherichia coli clinical isolates, including the major pathogenic and fluoroquinolone-resistant strains O25b:H4-ST131-H30Rx (isolates SRE34 and SRE44; MIC for colistin = 16 mg/liter), non-x (SME296; MIC = 8 mg/liter), and O18-ST416 (SME222; MIC = 4 mg/liter). In this study, we investigated the colistin resistance mechanism and identified novel amino acid substitutions or deletions in the PmrAB two-component system that activates eptA (encoding a phosphoethanolamine transferase) and arnT (encoding an undecaprenyl phosphate-alpha-4-amino-4-deoxy-l-arabinose arabinosyl transferase) in all colistin-resistant isolates. SRE34 possessed deletion Δ27–45 (LISVFWLWHESTEQIQLFE) in PmrB, SRE44 possessed substitution L105P in PmrA, and both SME222 and SME296 included substitution G206D in PmrB. Matrix-assisted laser desorption ionization–time of flight mass spectrometry revealed that lipid A is modified with phosphoethanolamine in all four isolates. Deletion of pmrAB decreased colistin MICs to 0.5 mg/liter and lowered eptA and arnT expression. Chromosomal replacement of mutated pmrA or pmrB in colistin-susceptible O25b:H4-ST131 strain SME98 (colistin MIC = 0.5 mg/liter) increased the colistin MIC to that of the respective parent colistin-resistant isolate. In addition, SME98 mutants in which pmrAB was replaced with mutated pmrAB showed no significant differences in bacterial growth and competition culture from the parent strain, except for the mutant with L105P in PmrA, whose growth was significantly suppressed in the presence of the parent strain. In conclusion, some O25b:H4-ST131 strains appear to acquire colistin resistance via phosphoethanolamine modification of lipid A through amino acid changes in PmrAB, and the amino acid changes in PmrB do not influence bacterial growth.

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