Evolved neomycin phosphotransferase from an isolate of Klebsiella pneumoniae

K. Y. Lee, J. D. Hopkins, Michael Syvanen

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

A new aminoglycoside resistance gene (aphA1-IAB) confers high-level resistance to neomycin. The sequence of aphA1-IAB is closely related to aphA1 found in the transposons TN4352, TN903 and Tn602. For example, aphA1-IAB differs from aphA1-903 at five nucleotides that result in four amino acid replacements. The enzyme encoded by aphA1-IAB has a significantly higher turnover number with neomycin, kanamycin and G418 as substrates than does the aphA1-903 enzyme. A parsimonious phylogenetic tree suggests that aphA1-IAB evolved from an ancestral form that is closely related or identical to the aphA1 found in Tn903. The excess of replacement substitutions over silent substitutions in aphA1-IAB, as well as its convergence toward aphA3 from Staphylococcus aureus, is indicative of selective evolution. Our hypothesis to explain these results is that aphA1-IAB evolved under the selective pressure of neomycin use in relatively recent times.

Original languageEnglish (US)
Pages (from-to)2039-2046
Number of pages8
JournalMolecular Microbiology
Volume5
Issue number8
StatePublished - Aug 1991

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Kanamycin Kinase
Neomycin
Klebsiella pneumoniae
Kanamycin
Aminoglycosides
Enzymes
Staphylococcus aureus
Nucleotides
Amino Acids
Genes

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

Cite this

Evolved neomycin phosphotransferase from an isolate of Klebsiella pneumoniae. / Lee, K. Y.; Hopkins, J. D.; Syvanen, Michael.

In: Molecular Microbiology, Vol. 5, No. 8, 08.1991, p. 2039-2046.

Research output: Contribution to journalArticle

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