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 |
Fingerprint
Keywords
- α-Macroglobulin
- Aeromonas
- Bacteria
- Inhibitor
- Protease
- Virulence
ASJC Scopus subject areas
- Structural Biology
- Biophysics
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
Cite this
The tail nick augments Aeromonas sobria serine protease (ASP) activity in plasma through retarding inhibition by α2-macroglobulin. / Murakami, Yoji; Wada, Yoshihiro; Kobayashi, Hidetomo; Hasegawa, Makoto; Okamoto, Keinosuke; Eto, Masatoshi; Imamura, Takahisa.
In: FEBS Letters, Vol. 586, No. 20, 19.10.2012, p. 3613-3617.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The tail nick augments Aeromonas sobria serine protease (ASP) activity in plasma through retarding inhibition by α2-macroglobulin
AU - Murakami, Yoji
AU - Wada, Yoshihiro
AU - Kobayashi, Hidetomo
AU - Hasegawa, Makoto
AU - Okamoto, Keinosuke
AU - Eto, Masatoshi
AU - Imamura, Takahisa
PY - 2012/10/19
Y1 - 2012/10/19
N2 - 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.
AB - 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.
KW - α-Macroglobulin
KW - Aeromonas
KW - Bacteria
KW - Inhibitor
KW - Protease
KW - Virulence
UR - http://www.scopus.com/inward/record.url?scp=84867580141&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84867580141&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2012.08.004
DO - 10.1016/j.febslet.2012.08.004
M3 - Article
C2 - 22971340
AN - SCOPUS:84867580141
VL - 586
SP - 3613
EP - 3617
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 20
ER -