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 language | English |
|---|---|
| Pages (from-to) | 3613-3617 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 586 |
| Issue number | 20 |
| DOIs | |
| Publication status | Published - 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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Cite this
Murakami, Y., Wada, Y., Kobayashi, H., Hasegawa, M., Okamoto, K., Eto, M., & Imamura, T. (2012). The tail nick augments Aeromonas sobria serine protease (ASP) activity in plasma through retarding inhibition by α2-macroglobulin. FEBS Letters, 586(20), 3613-3617. https://doi.org/10.1016/j.febslet.2012.08.004