The tail nick augments Aeromonas sobria serine protease (ASP) activity in plasma through retarding inhibition by α2-macroglobulin

Yoji Murakami, Yoshihiro Wada, Hidetomo Kobayashi, Makoto Hasegawa, Keinosuke Okamoto, Masatoshi Eto, Takahisa Imamura

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

ASP is a serine protease secreted by Aeromonas sobria, a sepsis-causing bacterium, and induces sepsis-mimicking disorders through plasma protein cleavage. The pathogen also secretes nASP that has a nick in the carboxy-terminal region. Compared with single-chain ASP (sASP), nASP had near-equivalent activity for small peptide substrates but was less proteolytic. Surprisingly, nASP cleaved proteins more in plasma and was inhibited by human α2-macroglobulin more slowly than sASP. Retarded inhibition by α2-macroglobulin allows nASP to keep proteolytic activity for longer in the host and exacerbate disorders at Aeromonas sobria infection sites. nASP may be an evolutional form to augment ASP virulence.

Original languageEnglish
Pages (from-to)3613-3617
Number of pages5
JournalFEBS Letters
Volume586
Issue number20
DOIs
Publication statusPublished - Oct 19 2012

Keywords

  • Aeromonas
  • Bacteria
  • Inhibitor
  • Protease
  • Virulence
  • α-Macroglobulin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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