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Saitama, Japan

Teramura H.,Kohjin Bio Co. | Sekiguchi J.-I.,Kohjin Bio Co. | Shimojima M.,BML Inc.
Diagnostic Microbiology and Infectious Disease | Year: 2014

MRSA-chrom, a novel chromogenic screening agar medium for methicillin-resistant Staphylococcus aureus (MRSA), was developed. There were all MRSA strains recovered in 24. h as a specific blue-colored colony among 130 microbes including 42 MRSA strains. MRSA-chrom showed the highest detection ratio among 4 commercially available selective media using 50 clinical specimens. © 2014 Elsevier Inc. Source


Kitao T.,Japan National Institute of Infectious Diseases | Miyoshi-Akiyama T.,Japan National Institute of Infectious Diseases | Tanaka M.,Mizuho Medy Co. | Narahara K.,Mizuho Medy Co. | And 2 more authors.
Journal of Microbiological Methods | Year: 2011

Rapid and reliable detection of carbapenem-resistant bacteria is an important infection-control measure and a crucial aspect of antimicrobial chemotherapy. IMP-type metallo-β-lactamase (MBL) is an emzyme that mediate carbapenem resistance in bacteria. Here, an immunochromatographic assay was newly developed using novel monoclonal antibodies (mAbs) recognizing IMP-type MBL. Epitope mapping of mAbs and mutational analysis of the epitope region in IMP antigen suggested that the mAbs could react to all known subtypes of IMP-type MBL. Evaluation of the assay using Pseudomonas aeruginosa strains (n=248) showed that the results of the immunochromatographic detection of the IMP-type MBLs were fully consistent with those of the PCR analysis for bla IMP genes, showing false positives and negatives. All positive strains were resistant to carbapenem (MIC≥16μg/ml). The assay also accurately distinguished the production of IMP-type MBLs in Pseudomonas putida, Acinetobacter baumannii, and Alcaligenes xylosoxidans. The detection limit of the assay was 5.7×10 4cfu per test. Taken together, these data suggest that the developed assay can be used for rapid and reliable diagnosis of the production of IMP-type MBLs in Gram-negative bacteria. © 2011 Elsevier B.V. Source


Tada T.,Japan National Institute of Infectious Diseases | Miyoshi-Akiyama T.,Japan National Institute of Infectious Diseases | Shimada K.,Japan National Institute of Infectious Diseases | Shimojima M.,BML Inc. | Kirikae T.,Japan National Institute of Infectious Diseases
Antimicrobial Agents and Chemotherapy | Year: 2013

Pseudomonas aeruginosa NCGM1588 has a novel chromosomal class 1 integron, In151, which includes the aac(6′)-Iaj gene. The encoded protein, AAC(6′)-Iaj, was found to consist of 184 amino acids, with 70% identity to AAC(6′)-Ia. Escherichia coli transformed with a plasmid containing the aac(6′)-Iaj gene acquired resistance to all aminoglycosides tested except gentamicin. Of note, aac(6′)-Iaj contributed to the resistance to arbekacin. Thin-layer chromatography revealed that AAC(6′)-Iaj acetylated all aminoglycosides tested except gentamicin. These findings indicated that AAC(6′)-Iaj is a functional acetyltransferase that modifies the amino groups at the 6′ positions of aminoglycosides and contributes to aminoglycoside resistance of P. aeruginosa NCGM1588, including arbekacin. Copyright © 2013, American Society for Microbiology. All Rights Reserved. Source


Kitao T.,National Center for Global Health and Medicine | Tada T.,National Center for Global Health and Medicine | Tanaka M.,Mizuho Medy Co. R and D | Narahara K.,Mizuho Medy Co. R and D | And 4 more authors.
International Journal of Antimicrobial Agents | Year: 2012

The emergence of multidrug-resistant (MDR) Pseudomonas aeruginosa isolates producing IMP-type metallo-β-lactamases (MBLs) and aminoglycoside 6′-N-acetyltransferase [AAC(6′)-Iae] has become a serious problem in medical settings in Japan. A total of 217 MDR P. aeruginosa isolates were obtained from August 2009 to April 2010 from patients at 144 hospitals in Japan, of which 145 (66.8%) were positive for IMP-type MBLs and AAC(6′)-Iae when tested with an immunochromatographic assay. Polymerase chain reaction (PCR) showed that these isolates were also positive for blaIMP and aac(6′)-Iae genes. When these IMP-type MBL- and AAC(6′)-Iae-producing isolates were analysed by pulsed-field gel electrophoresis (PFGE), two clusters (I and II) were detected. Most of the isolates (88.3%; 128/145) were grouped under cluster I and had multilocus sequence type ST235 and serotype O11, except for one isolate that was ST991 and serotype O3. The isolates were mainly isolated from the urinary tract (82/145; 56.6%) and respiratory tract (58/145; 40.0%). The epidemiological properties of the isolates belonging to cluster I were similar to those of MDR P. aeruginosa isolates that have been previously reported in Japan. The remaining 16 isolates belonged to cluster II, had identical PFGE patterns and were multilocus sequence type ST991 and serotype O18; all of these isolates were isolated from the respiratory tract. The properties of isolates belonging to cluster II have not been previously described, indicating that a novel IMP-type MBL- and AAC(6′)-Iae producing P. aeruginosa strain is emerging in Japan. Isolates belonging to both clusters were isolated from different parts of the country. © 2012 Elsevier B.V. and the International Society of Chemotherapy. All rights reserved. Source


Tada T.,Japan National Institute of Infectious Diseases | Miyoshi-Akiyama T.,Japan National Institute of Infectious Diseases | Shimada K.,Japan National Institute of Infectious Diseases | Shimojima M.,BML Inc. | Kirikae T.,Japan National Institute of Infectious Diseases
Antimicrobial Agents and Chemotherapy | Year: 2013

Two novel IMP-type metallo-β-lactamase variants, IMP-43 and IMP-44, were identified in multidrug-resistant Pseudomonas aeruginosa isolates obtained in medical settings in Japan. Analysis of their predicted amino acid sequences revealed that IMP-43 had an amino acid substitution (Val67Phe) compared with IMP-7 and that IMP-44 had two substitutions (Val67Phe and Phe87Ser) compared with IMP-11. The amino acid residue at position 67 is located at the end of a loop close to the active site, consisting of residues 60 to 66 in IMP-1, and the amino acid residue at position 87 forms a hydrophobic patch close to the active site with other amino acids. An Escherichia coli strain expressing bla IMP-43 was more resistant to doripenem and meropenem but not to imipenem than one expressing blaIMP-7. An E. coli strain expressing blaIMP-44 was more resistant to doripenem, imipenem and meropenem than one expressing blaIMP-11. IMP-43 had more efficient catalytic activities against all three carbapenems than IMP-7, indicating that the Val67Phe substitution contributed to increased catalytic activities against carbapenems. IMP-44 had more efficient catalytic activities against all carbapenems tested than IMP-11, as well as increased activities compared with IMP-43, indicating that both the Val67Phe and Phe87Ser substitutions contributed to increased catalytic activities against carbapenems. Copyright © 2013, American Society for Microbiology. All Rights Reserved. Source

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