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The tail nick augments Aeromonas sobria serine protease (ASP) activity in plasma through retarding inhibition by α 2 ‐macroglobulin
Author(s) -
Murakami Yoji,
Wada Yoshihiro,
Kobayashi Hidetomo,
Hasegawa Makoto,
Okamoto Keinosuke,
Eto Masatoshi,
Imamura Takahisa
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.08.004
Subject(s) - serine protease , macroglobulin , protease , virulence , microbiology and biotechnology , serine , proteases , chemistry , biology , biochemistry , enzyme , gene
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 α 2 ‐macroglobulin more slowly than sASP. Retarded inhibition by α 2 ‐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.