Novel plasmid-mediated 16S rRNA methylase, RmtC, found in a Proteus mirabilis isolate demonstrating extraordinary high-level resistance against various aminoglycosides

Jun Ichi Wachino, Kunikazu Yamane, Keigo Shibayama, Hiroshi Kurokawa, Naohiro Shibata, Satowa Suzuki, Yohei Doi, Kouji Kimura, Yasuyoshi Ike, Yoshichika Arakawa

Research output: Contribution to journalArticle

91 Citations (Scopus)

Abstract

Proteus mirabilis ARS68, which demonstrated a very high level of resistance to various aminoglycosides, was isolated in 2003 from an inpatient in Japan. The aminoglycoside resistance of this strain could not be transferred to recipient strains Escherichia coli CSH-2 and E. coli HB101 by a general conjugation experiment, but E. coli DHSα was successfully transformed by electroporation with the plasmid of the parent strain, ARS68, and acquired an unusually high degree of resistance against aminoglycosides. Cloning and sequencing analyses revealed that the presence of a novel 16S rRNA methylase gene, designated rmtC, was responsible for resistance in strain ARS68 and its transformant. The G+C content of rmtC was 41.1%, and the deduced amino acid sequences of the newly identified 16S rRNA methylase, RmtC, shared a relatively low level of identity (£29%) to other plasmid-mediated 16S rRNA methylases, RmtA, RmtB, and ArmA, which have also been identified in pathogenic gram-negative bacilli. Also, RmtC shared a low level of identity (≤28%) with the other 16S rRNA methylases found in aminoglycoside-producing actinomycetes. The purified histidine-tagged RmtC clearly showed niethyltransferase activity against E. coli 16S rRNA in vitro. rmtC was located downstream of an ISEcp1-like element containing trip A. Several plasmid-mediated 16S rRNA methylases have been identified in pathogenic gram-negative bacilli belonging to the family Enterobacteriaceae, and some of them are dispersing worldwide. The acceleration of aminoglycoside resistance among gram-negative bacilli by producing plasmid-mediated 16S rRNA methylases, such as RmtC, RmtB, and RmtA, may indeed become an actual clinical hazard in the near future.

Original languageEnglish
Pages (from-to)178-184
Number of pages7
JournalAntimicrobial agents and chemotherapy
Volume50
Issue number1
DOIs
Publication statusPublished - 01-01-2006
Externally publishedYes

Fingerprint

Proteus mirabilis
Aminoglycosides
Plasmids
Bacillus
Escherichia coli
Electroporation
Actinobacteria
Base Composition
Enterobacteriaceae
rRNA Genes
Histidine
rRNA (adenosine-O-2'-)methyltransferase
Organism Cloning
Inpatients
Amino Acid Sequence
Japan

All Science Journal Classification (ASJC) codes

  • Pharmacology
  • Pharmacology (medical)
  • Infectious Diseases

Cite this

Wachino, Jun Ichi ; Yamane, Kunikazu ; Shibayama, Keigo ; Kurokawa, Hiroshi ; Shibata, Naohiro ; Suzuki, Satowa ; Doi, Yohei ; Kimura, Kouji ; Ike, Yasuyoshi ; Arakawa, Yoshichika. / Novel plasmid-mediated 16S rRNA methylase, RmtC, found in a Proteus mirabilis isolate demonstrating extraordinary high-level resistance against various aminoglycosides. In: Antimicrobial agents and chemotherapy. 2006 ; Vol. 50, No. 1. pp. 178-184.
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abstract = "Proteus mirabilis ARS68, which demonstrated a very high level of resistance to various aminoglycosides, was isolated in 2003 from an inpatient in Japan. The aminoglycoside resistance of this strain could not be transferred to recipient strains Escherichia coli CSH-2 and E. coli HB101 by a general conjugation experiment, but E. coli DHSα was successfully transformed by electroporation with the plasmid of the parent strain, ARS68, and acquired an unusually high degree of resistance against aminoglycosides. Cloning and sequencing analyses revealed that the presence of a novel 16S rRNA methylase gene, designated rmtC, was responsible for resistance in strain ARS68 and its transformant. The G+C content of rmtC was 41.1{\%}, and the deduced amino acid sequences of the newly identified 16S rRNA methylase, RmtC, shared a relatively low level of identity (£29{\%}) to other plasmid-mediated 16S rRNA methylases, RmtA, RmtB, and ArmA, which have also been identified in pathogenic gram-negative bacilli. Also, RmtC shared a low level of identity (≤28{\%}) with the other 16S rRNA methylases found in aminoglycoside-producing actinomycetes. The purified histidine-tagged RmtC clearly showed niethyltransferase activity against E. coli 16S rRNA in vitro. rmtC was located downstream of an ISEcp1-like element containing trip A. Several plasmid-mediated 16S rRNA methylases have been identified in pathogenic gram-negative bacilli belonging to the family Enterobacteriaceae, and some of them are dispersing worldwide. The acceleration of aminoglycoside resistance among gram-negative bacilli by producing plasmid-mediated 16S rRNA methylases, such as RmtC, RmtB, and RmtA, may indeed become an actual clinical hazard in the near future.",
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Novel plasmid-mediated 16S rRNA methylase, RmtC, found in a Proteus mirabilis isolate demonstrating extraordinary high-level resistance against various aminoglycosides. / Wachino, Jun Ichi; Yamane, Kunikazu; Shibayama, Keigo; Kurokawa, Hiroshi; Shibata, Naohiro; Suzuki, Satowa; Doi, Yohei; Kimura, Kouji; Ike, Yasuyoshi; Arakawa, Yoshichika.

In: Antimicrobial agents and chemotherapy, Vol. 50, No. 1, 01.01.2006, p. 178-184.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Novel plasmid-mediated 16S rRNA methylase, RmtC, found in a Proteus mirabilis isolate demonstrating extraordinary high-level resistance against various aminoglycosides

AU - Wachino, Jun Ichi

AU - Yamane, Kunikazu

AU - Shibayama, Keigo

AU - Kurokawa, Hiroshi

AU - Shibata, Naohiro

AU - Suzuki, Satowa

AU - Doi, Yohei

AU - Kimura, Kouji

AU - Ike, Yasuyoshi

AU - Arakawa, Yoshichika

PY - 2006/1/1

Y1 - 2006/1/1

N2 - Proteus mirabilis ARS68, which demonstrated a very high level of resistance to various aminoglycosides, was isolated in 2003 from an inpatient in Japan. The aminoglycoside resistance of this strain could not be transferred to recipient strains Escherichia coli CSH-2 and E. coli HB101 by a general conjugation experiment, but E. coli DHSα was successfully transformed by electroporation with the plasmid of the parent strain, ARS68, and acquired an unusually high degree of resistance against aminoglycosides. Cloning and sequencing analyses revealed that the presence of a novel 16S rRNA methylase gene, designated rmtC, was responsible for resistance in strain ARS68 and its transformant. The G+C content of rmtC was 41.1%, and the deduced amino acid sequences of the newly identified 16S rRNA methylase, RmtC, shared a relatively low level of identity (£29%) to other plasmid-mediated 16S rRNA methylases, RmtA, RmtB, and ArmA, which have also been identified in pathogenic gram-negative bacilli. Also, RmtC shared a low level of identity (≤28%) with the other 16S rRNA methylases found in aminoglycoside-producing actinomycetes. The purified histidine-tagged RmtC clearly showed niethyltransferase activity against E. coli 16S rRNA in vitro. rmtC was located downstream of an ISEcp1-like element containing trip A. Several plasmid-mediated 16S rRNA methylases have been identified in pathogenic gram-negative bacilli belonging to the family Enterobacteriaceae, and some of them are dispersing worldwide. The acceleration of aminoglycoside resistance among gram-negative bacilli by producing plasmid-mediated 16S rRNA methylases, such as RmtC, RmtB, and RmtA, may indeed become an actual clinical hazard in the near future.

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