Pseudomonas fluorescens proliferates in a mouse organ homogenate at low temperature

Yota Tatara, Takahiro Terakawa, Youhei Yamagata, Takafumi Uchida

Research output: Contribution to journalArticlepeer-review

Abstract

In this study we observed the proliferation of Pseudomonas fluorescens (P. fluorescens) in mouse organ homogenates at 4°C. P. fluorescens secreted a protease possessing properties different from those of the mammalian tissue proteases. The specificity of this protease required a basic amino acid residue at the P1 position at a pH optimum of 6.0. The specificity of the protease was similar to that of trypsin, but the pH optimum was different. The protease mildly degraded elastin-Congo red; this suggests that the protease serves as an alternative for elastase in the case of P. fluorescens strains that lack virulent elastase. The protease was identified as an alkaline protease of P. fluorescens by liquid chromatography-tandem mass spectrometry analysis. Our results show that proteome analysis of the soluble proteins is useful in identifying bacterial species, particularly the bacterial contaminants in samples containing antibiotics.

Original languageEnglish
Pages (from-to)621-626
Number of pages6
JournalInternational journal of molecular medicine
Volume21
Issue number5
DOIs
Publication statusPublished - 2008 May

Keywords

  • Elastase
  • Extracellular metalloprotease
  • Indigenous bacterium
  • Multidrug resistance
  • Opportunistic infection
  • Pseudomonas fluorescens

ASJC Scopus subject areas

  • Genetics

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