Characterization of a Rifampin-Inactivating Glycosyltransferase from a Screen of Environmental Actinomycetes

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Published inAntimicrobial Agents and Chemotherapy Vol. 56; no. 10; pp. 5061 - 5069
Main Authors Spanogiannopoulos, Peter, Thaker, Maulik, Koteva, Kalinka, Waglechner, Nicholas, Wright, Gerard D.
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.10.2012
Subjects
Actinobacteria
Actinobacteria - drug effects
Actinobacteria - enzymology
Actinobacteria - metabolism
Antibiotics. Antiinfectious agents. Antiparasitic agents
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biological and medical sciences
Genome, Bacterial - genetics
Glycosyltransferases
Glycosyltransferases - genetics
Glycosyltransferases - metabolism
Mechanisms of Resistance
Medical sciences
Molecular Sequence Data
Open Reading Frames - genetics
Pharmacology. Drug treatments
Phylogeny
Rifampin
Rifampin - metabolism
Rifampin - pharmacology
Streptomyces - drug effects
Streptomyces - enzymology
Streptomyces - metabolism
Enzyme
Transferases
Glycosyltransferases
Medical screening
Characterization
Antibiotic
Rifampicin
Bacteria
Environment
Actinomycetes
Antituberculous agent
Protein synthesis inhibitor
Antibacterial agent
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Abstract Classifications Services AAC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue AAC About AAC Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy AAC RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0066-4804 Online ISSN: 1098-6596 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to AAC .asm.org, visit: AAC       
AbstractList Identifying and understanding the collection of all antibiotic resistance determinants presented in the global microbiota, the antibiotic resistome, provides insight into the evolution of antibiotic resistance and critical information for the development of future antimicrobials. The rifamycins are broad-spectrum antibiotics that target bacterial transcription by inhibition of RNA polymerase. Although mutational alteration of the drug target is the predominant mechanism of resistance to this family of antibiotics in the clinic, a number of diverse inactivation mechanisms have also been reported. In this report, we investigate a subset of environmental rifampin-resistant actinomycete isolates and identify a diverse collection of rifampin inactivation mechanisms. We describe a single isolate, WAC1438, capable of inactivating rifampin by glycosylation. A draft genome sequence of WAC1438 (most closely related to Streptomyces speibonae , according to a 16S rRNA gene comparison) was assembled, and the associated rifampin glycosyltransferase open reading frame, rgt1438 , was identified. The role of rgt1438 in rifampin resistance was confirmed by its disruption in the bacterial chromosome, resulting in a loss of antibiotic inactivation and a 4-fold decrease in MIC. Interestingly, examination of the RNA polymerase β-subunit sequence of WAC1438 suggests that it harbors a resistant target and thus possesses dual mechanisms of rifamycin resistance. Using an in vitro assay with purified enzyme, Rgt1438 could inactivate a variety of rifamycin antibiotics with comparable steady-state kinetics constants. Our results identify rgt1438 as a rifampin resistance determinant from WAC1438 capable of inactivating an assortment of rifamycins, adding a new element to the rifampin resistome.
Identifying and understanding the collection of all antibiotic resistance determinants presented in the global microbiota, the antibiotic resistome, provides insight into the evolution of antibiotic resistance and critical information for the development of future antimicrobials. The rifamycins are broad-spectrum antibiotics that target bacterial transcription by inhibition of RNA polymerase. Although mutational alteration of the drug target is the predominant mechanism of resistance to this family of antibiotics in the clinic, a number of diverse inactivation mechanisms have also been reported. In this report, we investigate a subset of environmental rifampin-resistant actinomycete isolates and identify a diverse collection of rifampin inactivation mechanisms. We describe a single isolate, WAC1438, capable of inactivating rifampin by glycosylation. A draft genome sequence of WAC1438 (most closely related to Streptomyces speibonae, according to a 16S rRNA gene comparison) was assembled, and the associated rifampin glycosyltransferase open reading frame, rgt1438, was identified. The role of rgt1438 in rifampin resistance was confirmed by its disruption in the bacterial chromosome, resulting in a loss of antibiotic inactivation and a 4-fold decrease in MIC. Interestingly, examination of the RNA polymerase β-subunit sequence of WAC1438 suggests that it harbors a resistant target and thus possesses dual mechanisms of rifamycin resistance. Using an in vitro assay with purified enzyme, Rgt1438 could inactivate a variety of rifamycin antibiotics with comparable steady-state kinetics constants. Our results identify rgt1438 as a rifampin resistance determinant from WAC1438 capable of inactivating an assortment of rifamycins, adding a new element to the rifampin resistome.
Identifying and understanding the collection of all antibiotic resistance determinants presented in the global microbiota, the antibiotic resistome, provides insight into the evolution of antibiotic resistance and critical information for the development of future antimicrobials. The rifamycins are broad-spectrum antibiotics that target bacterial transcription by inhibition of RNA polymerase. Although mutational alteration of the drug target is the predominant mechanism of resistance to this family of antibiotics in the clinic, a number of diverse inactivation mechanisms have also been reported. In this report, we investigate a subset of environmental rifampin-resistant actinomycete isolates and identify a diverse collection of rifampin inactivation mechanisms. We describe a single isolate, WAC1438, capable of inactivating rifampin by glycosylation. A draft genome sequence of WAC1438 (most closely related to Streptomyces speibonae, according to a 16S rRNA gene comparison) was assembled, and the associated rifampin glycosyltransferase open reading frame, rgt1438, was identified. The role of rgt1438 in rifampin resistance was confirmed by its disruption in the bacterial chromosome, resulting in a loss of antibiotic inactivation and a 4-fold decrease in MIC. Interestingly, examination of the RNA polymerase β-subunit sequence of WAC1438 suggests that it harbors a resistant target and thus possesses dual mechanisms of rifamycin resistance. Using an in vitro assay with purified enzyme, Rgt1438 could inactivate a variety of rifamycin antibiotics with comparable steady-state kinetics constants. Our results identify rgt1438 as a rifampin resistance determinant from WAC1438 capable of inactivating an assortment of rifamycins, adding a new element to the rifampin resistome.Identifying and understanding the collection of all antibiotic resistance determinants presented in the global microbiota, the antibiotic resistome, provides insight into the evolution of antibiotic resistance and critical information for the development of future antimicrobials. The rifamycins are broad-spectrum antibiotics that target bacterial transcription by inhibition of RNA polymerase. Although mutational alteration of the drug target is the predominant mechanism of resistance to this family of antibiotics in the clinic, a number of diverse inactivation mechanisms have also been reported. In this report, we investigate a subset of environmental rifampin-resistant actinomycete isolates and identify a diverse collection of rifampin inactivation mechanisms. We describe a single isolate, WAC1438, capable of inactivating rifampin by glycosylation. A draft genome sequence of WAC1438 (most closely related to Streptomyces speibonae, according to a 16S rRNA gene comparison) was assembled, and the associated rifampin glycosyltransferase open reading frame, rgt1438, was identified. The role of rgt1438 in rifampin resistance was confirmed by its disruption in the bacterial chromosome, resulting in a loss of antibiotic inactivation and a 4-fold decrease in MIC. Interestingly, examination of the RNA polymerase β-subunit sequence of WAC1438 suggests that it harbors a resistant target and thus possesses dual mechanisms of rifamycin resistance. Using an in vitro assay with purified enzyme, Rgt1438 could inactivate a variety of rifamycin antibiotics with comparable steady-state kinetics constants. Our results identify rgt1438 as a rifampin resistance determinant from WAC1438 capable of inactivating an assortment of rifamycins, adding a new element to the rifampin resistome.
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Author Maulik Thaker
Kalinka Koteva
Nicholas Waglechner
Gerard D. Wright
Peter Spanogiannopoulos
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  surname: Spanogiannopoulos
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  givenname: Maulik
  surname: Thaker
  fullname: Thaker, Maulik
  organization: M. G. DeGroote Institute for Infectious Disease Research, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada
– sequence: 3
  givenname: Kalinka
  surname: Koteva
  fullname: Koteva, Kalinka
  organization: M. G. DeGroote Institute for Infectious Disease Research, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada
– sequence: 4
  givenname: Nicholas
  surname: Waglechner
  fullname: Waglechner, Nicholas
  organization: M. G. DeGroote Institute for Infectious Disease Research, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada
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  givenname: Gerard D.
  surname: Wright
  fullname: Wright, Gerard D.
  organization: M. G. DeGroote Institute for Infectious Disease Research, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada
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Copyright © 2012, American Society for Microbiology. All Rights Reserved.
Copyright © 2012, American Society for Microbiology. All Rights Reserved. 2012 American Society for Microbiology
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Issue 10
Keywords Enzyme
Transferases
Glycosyltransferases
Medical screening
Characterization
Antibiotic
Rifampicin
Bacteria
Environment
Actinomycetes
Antituberculous agent
Protein synthesis inhibitor
Antibacterial agent
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PublicationTitle Antimicrobial Agents and Chemotherapy
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Identifying and understanding the collection of all antibiotic resistance determinants presented in the global microbiota, the antibiotic resistome, provides...
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StartPage 5061
SubjectTerms Actinobacteria
Actinobacteria - drug effects
Actinobacteria - enzymology
Actinobacteria - metabolism
Antibiotics. Antiinfectious agents. Antiparasitic agents
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biological and medical sciences
Genome, Bacterial - genetics
Glycosyltransferases
Glycosyltransferases - genetics
Glycosyltransferases - metabolism
Mechanisms of Resistance
Medical sciences
Molecular Sequence Data
Open Reading Frames - genetics
Pharmacology. Drug treatments
Phylogeny
Rifampin
Rifampin - metabolism
Rifampin - pharmacology
Streptomyces - drug effects
Streptomyces - enzymology
Streptomyces - metabolism
Title Characterization of a Rifampin-Inactivating Glycosyltransferase from a Screen of Environmental Actinomycetes
URI http://aac.asm.org/content/56/10/5061.abstract
https://www.ncbi.nlm.nih.gov/pubmed/22802246
https://journals.asm.org/doi/10.1128/AAC.01166-12
https://www.proquest.com/docview/1039883016
https://pubmed.ncbi.nlm.nih.gov/PMC3457401
Volume 56
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