The tail nick augments Aeromonas sobria serine protease (ASP) activity in plasma through retarding inhibition by α2-macroglobulin.
The tail nick augments Aeromonas sobria serine protease (ASP) activity in plasma through retarding inhibition by α2-macroglobulin.
复制标题
尾部切口通过延缓 α2-巨球蛋白的抑制作用来增强血浆中的气单胞菌丝氨酸蛋白酶 (ASP) 活性。
DOI：
10.1016/j.febslet.2012.08.004
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发表时间：
2012
期刊：
影响因子：
3.5
通讯作者：
Imamura. T
中科院分区：
文献类型：
--
作者：
Murakami Y;Wada Y;Kobayashi H;Hasegawa M;Okamoto K;Eto M;Imamura. T
ASP是由引起败血症的温和气单胞菌分泌的一种丝氨酸蛋白酶，通过裂解血浆蛋白诱导类脓毒症。病原菌还分泌在羧基末端有缺口的NASP。与单链天冬氨酸(SASP)相比，NASP对小肽底物具有相近的活性，但对蛋白质的降解作用较弱。令人惊讶的是，与α相比，NaSP能更多地切割血浆中的蛋白质，并且被人SASP 2-巨球蛋白抑制的速度更慢。α-2-巨球蛋白的延缓抑制使其能够在宿主中保持更长时间的蛋白分解活性，并加剧温和气单胞菌感染部位的紊乱。NASP可能是增强其毒力的一种进化形式。
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.