Elsevier

Plasmid

Volume 15, Issue 2, March 1986, Pages 119-131
Plasmid

Regular article
Characterization of transferable plasmids from Shigella flexneri 2a that confer resistance to trimethoprim, streptomycin, and sulfonamides

https://doi.org/10.1016/0147-619X(86)90048-XGet rights and content

Abstract

A set of plasmids conferring resistance to several antibiotics, including the combination of trimethoprim and sulfamethoxazole, has been isolated from Escherichia coli following conjugative cotransfer from a clinical isolate of Shigella flexneri 2a. One of the plasmids, pCN1, was shown by subcloning and DNA sequencing to carry a gene encoding a trimethoprim-insensitive dihydrofolate reductase identical to that found in E. coli transposon 7. This plasmid was also shown to confer resistance to both streptomycin and spectinomycin by production of an adenylyltransferase that inactivated the drugs and the gene encoding this enzyme has also been sequenced. A second plasmid from the set, pCN2, was shown to inactivate streptomycin by a phosphotransferase mechanism and also to confer resistance to sulfonamides. The third plasmid from the set could not be correlated with a drug-resistance phenotype, but does appear to play a crucial role in plasmid mobilization.

References (55)

  • F. Shareck et al.

    Structure and molecular properties of the R.SmSu plasmid pSAS1206

    Plasmid

    (1983)
  • O. Sköld et al.

    A new dihydrofolate reductase with low trimethoprim sensitivity induced by an R factor mediating high resistance to trimethoprim

    J. Biol. Chem

    (1974)
  • S.L. Smith et al.

    R plasmid dihydrofolate reductase with subunit structure

    J. Biol. Chem

    (1979)
  • D. Stone et al.

    The amino acid sequence of the trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67

    J. Biol. Chem

    (1979)
  • B. Tennhammar-Ekman et al.

    Trimethoprim resistance plasmids of different origin encode different drug-resistant dihydrofolate reductases

    Plasmid

    (1979)
  • D. Baccanari et al.

    Purification and properties of Escherichia coli dihydrofolate reductase

    Biochemistry

    (1975)
  • R.M. Bannatyne et al.

    Resistance to trimethoprim and other antibiotics in Shigellae isolated in the Province of Ontario

    Canad. J. Microbiol

    (1980)
  • F.A. Barada et al.

    Sulfamethoxazole-trimethoprim versus ampicillin in treatment of acute invasive diarrhea in adults

    Antimicrob. Agents Chemother

    (1980)
  • P.T. Barth et al.

    Transposition of a deoxyribonucleic acid sequence encoding trimethoprim and streptomycin resistances from R483 to other replicons

    J. Bacteriol

    (1976)
  • P.T. Barth et al.

    Comparison of the deoxyribonucleic acid molecular weights and homologies of plasmids conferring linked resistance to streptomycin and sulfonamides

    J. Bacteriol

    (1974)
  • A.W. Bauer et al.

    Antibiotic susceptibility testing by a standardized single disk method

    Amer. J. Clin. Pathol

    (1966)
  • D.E. Berg et al.

    Transposition of R factor genes to bacteriophage λ

  • H.C. Birnboim et al.

    A rapid alkaline extraction procedure for screening recombinant plasmid DNA

    Nucleic Acids Res

    (1979)
  • D. Chun et al.

    Transferable resistance to trimethoprim in Shigella

    J. Infect. Dis

    (1981)
  • D.B. Clewell

    Nature of ColE1 plasmid replication to Escherichia coli in the presence of chloramphenicol

    J. Bacteriol

    (1972)
  • N. Datta et al.

    Trimethoprim resistance conferred by W plasmids in Enterobacteriaceae

    J. Gen. Microbiol

    (1972)
  • J.E. Davies et al.

    Transmissible multiple drug resistance in Enterobacteriaceae

    Science (Washington, D. C.)

    (1972)
  • Cited by (26)

    • Plant selectable genes, reporter genes and promoters

      2012, Plant Molecular Biology LabFax: A Volume in LabFax
    • Plant transformation and expression vectors

      2012, Plant Molecular Biology LabFax: A Volume in LabFax
    • Nucleic acid analysis of antibiotic resistance

      1992, International Journal of Antimicrobial Agents
    View all citing articles on Scopus
    2

    Present address: Department of Biochemistry, Dalhousie University, Halifax, Nova Scotia B3H 4H7, Canada.

    View full text