微生物学杂志
微生物學雜誌
미생물학잡지
Journal of Microbiology
2015年
4期
98-101
,共4页
杨淑凤%刘欣%邓国英%王晓丽%孙文长
楊淑鳳%劉訢%鄧國英%王曉麗%孫文長
양숙봉%류흔%산국영%왕효려%손문장
结核分枝杆菌%O-甘露糖基化%Apa蛋白%ConA-lectin
結覈分枝桿菌%O-甘露糖基化%Apa蛋白%ConA-lectin
결핵분지간균%O-감로당기화%Apa단백%ConA-lectin
Mycobacterium tuberculosis%O-mannosylation%Apa%ConA-lectin
蛋白质的O-甘露糖基化修饰不仅在真菌和哺乳类细胞中广泛存在,在原核生物中例如分枝杆菌属、棒状杆菌属和链霉菌属中也存在,尤其在引起人类疾病的结核分枝杆菌中研究最多。许多O-甘露糖基化蛋白在结核分枝杆菌毒力以及与宿主相互作用过程中发挥了重要作用。本文就结核分枝杆菌中O-甘露糖基化蛋白生物学功能的进展加以综述。
蛋白質的O-甘露糖基化脩飾不僅在真菌和哺乳類細胞中廣汎存在,在原覈生物中例如分枝桿菌屬、棒狀桿菌屬和鏈黴菌屬中也存在,尤其在引起人類疾病的結覈分枝桿菌中研究最多。許多O-甘露糖基化蛋白在結覈分枝桿菌毒力以及與宿主相互作用過程中髮揮瞭重要作用。本文就結覈分枝桿菌中O-甘露糖基化蛋白生物學功能的進展加以綜述。
단백질적O-감로당기화수식불부재진균화포유류세포중엄범존재,재원핵생물중례여분지간균속、봉상간균속화련매균속중야존재,우기재인기인류질병적결핵분지간균중연구최다。허다O-감로당기화단백재결핵분지간균독력이급여숙주상호작용과정중발휘료중요작용。본문취결핵분지간균중O-감로당기화단백생물학공능적진전가이종술。
O-mannosylation decoration of proteins not only widely exists in fungal and mammalian cells, but also ex-ists in prokaryotes, e.g.Mycobacterium, Corynebaterium and Streptomyces, especially in Mycobacterium tuberculosis that causes human illness and draw studies the most.Many O-mannosylated proteins play important role during mutual actions in M.tuberculosis virulence and the host.Advances in biological function of O-mannosylated proteins in M. tuberculosis were summarized in this paper.