scholarly journals Identification of a Novel NDM Variant, NDM-13, from a Multidrug-Resistant Escherichia coli Clinical Isolate in Nepal

2015 ◽  
Vol 59 (9) ◽  
pp. 5847-5850 ◽  
Author(s):  
Basudha Shrestha ◽  
Tatsuya Tada ◽  
Tohru Miyoshi-Akiyama ◽  
Kayo Shimada ◽  
Hiroshi Ohara ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Enzymatic Activity ◽  
Clinical Isolate ◽  
Multidrug Resistant ◽  
New Delhi ◽  
Content Type ◽  
Genetic Environment ◽  
Carbapenem Resistant

ABSTRACTA novel New Delhi metallo-β-lactamase, NDM-13, was identified in a carbapenem-resistantEscherichia coliclinical isolate obtained from the urine of a patient in Nepal. The enzymatic activity of NDM-13 against β-lactams was similar to that of NDM-1. However, NDM-13 displayed significantly higherkcat/Kmratios for cefotaxime. The genetic environment ofblaNDM-13was determined to betnpA-IS30-blaNDM-13-bleMBL-trpF-dsbC-cutA-groES-groL, withblaNDM-13located within the chromosome.

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 Detection of an Escherichia coli Sequence Type 167 Strain with Two Tandem Copies ofblaNDM-1in the Chromosome

2016 ◽  
Vol 55 (1) ◽  
pp. 199-205 ◽  
Author(s):  
Ping Shen ◽  
Maoli Yi ◽  
Ying Fu ◽  
Zhi Ruan ◽  
Xiaoxing Du ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Insertion Sequence ◽  
Southern Blotting ◽  
Multidrug Resistant ◽  
Sequence Type ◽  
New Delhi ◽  
Genomic Context ◽  
Content Type ◽  
Link Type ◽  
Reference Genomes

ABSTRACTNew Delhi metallo-β-lactamase-1 (NDM-1)-producingEnterobacteriaceaehas disseminated rapidly throughout the world and poses an urgent threat to public health. Previous studies confirmed that theblaNDM-1gene is typically carried in plasmids but rarely in chromosome. We discovered a multidrug-resistantEscherichia colistrain Y5, originating from a urine sample and containing theblaNDM-1gene, which did not transfer by either conjugation or electrotransformation. We confirmed the possibility of its chromosome location by S1-pulsed-field gel electrophoresis (PFGE) and XbaI-PFGE, followed by Southern blotting. To determine the genomic background ofblaNDM-1, the genome of Y5 was completely sequenced and compared to other reference genomes. The results of our study revealed that this isolate consists of a 4.8-Mbp chromosome and three plasmids, it is an epidemic clone of sequence type (ST) 167, and it shows 99% identity withEscherichia coli6409 (GenBank accession no.CP010371), which lacks the sameblaNDM-1gene-surrounding structure as Y5. TheblaNDM-1gene is embedded in the chromosome along with two tandem copies of an insertion sequence common region 1 (ISCR1) element (sul1-ARR-3-cat-blaNDM-1-bleo-ISCR1), which appears intact in the plasmid fromProteus mirabilis(GenBank accession no.KP662515). The genomic context indicates that the ISCR1element mediated theblaNDM-1transposition from a single source plasmid to the chromosome. Our study is the first report of anEnterobacteriaceaestrain harboring a chromosomally integratedblaNDM-1, which directly reveals the vertical spreading pattern of the gene. Close surveillance is urgently needed to monitor the emergence and potential spread of ST167 strains that harborblaNDM-1.

scholarly journals New Variant of mcr-3 in an Extensively Drug-Resistant Escherichia coli Clinical Isolate Carrying mcr-1 and blaNDM-5

2017 ◽  
Vol 61 (12) ◽  
Author(s):  
Lu Liu ◽  
Yu Feng ◽  
Xiaoxia Zhang ◽  
Alan McNally ◽  
Zhiyong Zong
Keyword(s):  
Escherichia Coli ◽  
Clinical Isolate ◽  
Amino Acid Substitutions ◽  
Drug Resistant ◽  
Content Type ◽  
Carbapenem Resistant ◽  
Resistant Genes ◽  
Extensively Drug Resistant ◽  
New Variant ◽  
Carbapenemase Gene

ABSTRACT A colistin- and carbapenem-resistant Escherichia coli clinical isolate was found to carry two plasmid-borne colistin-resistant genes, mcr-1 and the newly identified mcr-3, and a carbapenemase gene, bla NDM-5. mcr-3 is a new variant (mcr-3.5) in the isolate and encodes three amino acid substitutions compared with the original MCR-3. mcr-3 was carried by a TnAs3-like transposon on a self-transmissible IncP plasmid in the isolate, highlighting that mcr-3 may have widely spread.

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 Outbreak Caused by Enterobacteriaceae Harboring NDM-1 Metallo-β-Lactamase Carried in an IncFII Plasmid in a Tertiary Care Hospital in Mexico City

2015 ◽  
Vol 59 (11) ◽  
pp. 7080-7083 ◽  
Author(s):  
Pedro Torres-González ◽  
Miriam Bobadilla-del Valle ◽  
Estrella Tovar-Calderón ◽  
Francisco Leal-Vega ◽  
Araceli Hernández-Cruz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Mexico City ◽  
Tertiary Care Hospital ◽  
Bacterial Species ◽  
Tertiary Care ◽  
Enterobacter Cloacae ◽  
New Delhi ◽  
Care Hospital ◽  
Content Type ◽  
Carbapenem Resistant

ABSTRACTCarbapenem-resistantEnterobacteriaceaecarrying New Delhi metallo-β-lactamase 1 (NDM-1) have rarely been reported in Latin America. We report of an outbreak caused by ablaNDM-1-harboring plasmid spread through different bacterial species, includingEscherichia coli(ST617) andEnterobacter cloacae(ST182) isolates from the same patient and threeKlebsiella pneumoniaeisolates (ST22) derived from three epidemiologically related patients. IncFII plasmids were found in all strains. Measures to control the outbreak were applied successfully.

scholarly journals Identification of a Novel 6′-N-Aminoglycoside Acetyltransferase, AAC(6′)-Iak, from a Multidrug-Resistant Clinical Isolate of Stenotrophomonas maltophilia

2014 ◽  
Vol 58 (10) ◽  
pp. 6324-6327 ◽  
Author(s):  
Tatsuya Tada ◽  
Tohru Miyoshi-Akiyama ◽  
Rajan K. Dahal ◽  
Shyam K. Mishra ◽  
Kayo Shimada ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Thin Layer ◽  
Thin Layer Chromatography ◽  
Clinical Isolate ◽  
Stenotrophomonas Maltophilia ◽  
Multidrug Resistant ◽  
Content Type ◽  
Encoding Gene ◽  
Layer Chromatography

ABSTRACTStenotrophomonas maltophiliaIOMTU250 has a novel 6′-N-aminoglycoside acetyltransferase-encoding gene,aac(6′)-Iak. The encoded protein, AAC(6′)-Iak, consists of 153 amino acids and has 86.3% identity to AAC(6′)-Iz.Escherichia colitransformed with a plasmid containingaac(6′)-Iakexhibited decreased susceptibility to arbekacin, dibekacin, neomycin, netilmicin, sisomicin, and tobramycin. Thin-layer chromatography showed that AAC(6′)-Iak acetylated amikacin, arbekacin, dibekacin, isepamicin, kanamycin, neomycin, netilmicin, sisomicin, and tobramycin but not apramycin, gentamicin, or lividomycin.

scholarly journals In VitroActivity of LYS228, a Novel Monobactam Antibiotic, against Multidrug-ResistantEnterobacteriaceae

2018 ◽  
Vol 62 (10) ◽  
Author(s):  
Johanne Blais ◽  
Sara Lopez ◽  
Cindy Li ◽  
Alexey Ruzin ◽  
Srijan Ranjitkar ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Klebsiella Pneumoniae ◽  
Carbapenem Resistance ◽  
Multidrug Resistant ◽  
Minimal Bactericidal Concentration ◽  
Content Type ◽  
Carbapenem Resistant ◽  
Time Kill ◽  
Reference Strains ◽  
M 14

ABSTRACTLYS228 is a novel monobactam with potent activity againstEnterobacteriaceae. LYS228 is stable to metallo-β-lactamases (MBLs) and serine carbapenemases, includingKlebsiella pneumoniaecarbapenemases (KPCs), resulting in potency against the majority of extended-spectrum β-lactamase (ESBL)-producing and carbapenem-resistantEnterobacteriaceaestrains tested. Overall, LYS228 demonstrated potent activity against 271Enterobacteriaceaestrains, including multidrug-resistant isolates. Based on MIC90values, LYS228 (MIC90, 1 μg/ml) was ≥32-fold more active against those strains than were aztreonam, ceftazidime, ceftazidime-avibactam, cefepime, and meropenem. The tigecycline MIC90was 4 μg/ml against the strains tested. AgainstEnterobacteriaceaeisolates expressing ESBLs (n= 37) or displaying carbapenem resistance (n= 77), LYS228 had MIC90values of 1 and 4 μg/ml, respectively. LYS228 exhibited potent bactericidal activity, as indicated by low minimal bactericidal concentration (MBC) to MIC ratios (MBC/MIC ratios of ≤4) against 97.4% of theEnterobacteriaceaestrains tested (264/271 strains). In time-kill studies, LYS228 consistently achieved reductions in CFU per milliliter of 3 log10units (≥99.9% killing) at concentrations ≥4× MIC forEscherichia coliandK. pneumoniaereference strains, as well as isolates encoding TEM-1, SHV-1, CTX-M-14, CTX-M-15, KPC-2, KPC-3, and NDM-1 β-lactamases.

scholarly journals A Novel New Delhi Metallo-β-Lactamase Variant, NDM-14, Isolated in a Chinese Hospital Possesses Increased Enzymatic Activity against Carbapenems

2015 ◽  
Vol 59 (4) ◽  
pp. 2450-2453 ◽  
Author(s):  
Dayang Zou ◽  
Yong Huang ◽  
Xiangna Zhao ◽  
Wei Liu ◽  
Derong Dong ◽  
...  
Keyword(s):  
Intensive Care Unit ◽  
Intensive Care ◽  
Amino Acid ◽  
Intensive Care Unit Patient ◽  
Enzymatic Activity ◽  
Clinical Isolate ◽  
Kinetic Data ◽  
New Delhi ◽  
Local Hospital ◽  
Content Type

ABSTRACTA novel New Delhi metallo-β-lactamase (NDM) variant, NDM-14, was identified in clinical isolateAcinetobacter lwoffiiJN49-1, which was recovered from an intensive care unit patient at a local hospital in China. NDM-14, which differs from other existing enzymes by an amino acid substitution at position 130 (Asp130Gly), possesses enzymatic activity toward carbapenems that is greater than that of NDM-1. Kinetic data indicate that NDM-14 has a higher affinity for imipenem and meropenem.

scholarly journals Coexistence of Two bla NDM-5 Genes on an IncF Plasmid as Revealed by Nanopore Sequencing

2018 ◽  
Vol 62 (5) ◽  
Author(s):  
Yu Feng ◽  
Lu Liu ◽  
Alan McNally ◽  
Zhiyong Zong
Keyword(s):  
Escherichia Coli ◽  
Clinical Isolate ◽  
Sequence Type ◽  
Nanopore Sequencing ◽  
Content Type ◽  
Carbapenem Resistant ◽  
Transmissible Plasmid

ABSTRACT In a carbapenem-resistant Escherichia coli clinical isolate of sequence type 167, two copies of bla NDM-5 were found on a 144,225-bp IncF self-transmissible plasmid of the F36:A4:B − type. Both bla NDM-5 genes were located in 11,065-bp regions flanked by two copies of IS 26 . The two regions were identical in sequence but were present at different locations on the plasmid, suggesting a duplication of the same region. This study highlights the complex genetic contexts of bla NDM-5 .

scholarly journals Whole-Genome Sequences of Two NDM-1-Producing Pseudomonas aeruginosa Strains Isolated in a Clinical Setting in Albania in 2018

2020 ◽  
Vol 9 (1) ◽  
Author(s):  
Silva Tafaj ◽  
Floriana Gona ◽  
Célia F. Rodrigues ◽  
Perlat Kapisyzi ◽  
Fatmir Caushi ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Draft Genome ◽  
Multidrug Resistant ◽  
Sequence Type ◽  
New Delhi ◽  
Surgical Wound ◽  
Genome Sequences ◽  
Content Type ◽  
Carbapenem Resistant ◽  
Public Health Threat

Isolation of metallo-β-lactamase-producing, carbapenem-resistant, Pseudomonas aeruginosa strains is increasingly being documented worldwide; their presence constitutes a public health threat. Here, we report draft genome sequences of two New Delhi metallo-β-lactamase-1-producing, multidrug-resistant, P. aeruginosa strains of sequence type 235 that were isolated from the surgical wound of two patients hospitalized in the same ward.

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