Hsp100 Molecular Chaperone ClpB and Its Role in Virulence of Bacterial Pathogens.
Hsp100 Molecular Chaperone ClpB and Its Role in Virulence of Bacterial Pathogens.
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DOI：
10.3390/ijms22105319
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发表时间：
2021-05-18
影响因子：
5.6
通讯作者：
Zolkiewski M
中科院分区：
文献类型：
--
作者：
Kędzierska-Mieszkowska S;Zolkiewski M
本文综述了AAA+ATPase中Hsp100/CLP亚家族的分子伴侣ClpB及其在包括人畜共患病在内的多种人类感染性疾病中的生物学功能。已经证实，ClpB解聚并重新激活聚集的细胞蛋白。据推测，ClpB的蛋白质解聚活性支持病原菌在宿主诱导的应激(如高温和氧化应激)下生存，从而使它们能够迅速适应人类宿主并建立感染。有趣的是，ClpB还可以在病原菌中执行其他功能，这是它们毒力所必需的。由于在人类细胞中没有发现ClpB，这种伴侣蛋白成为对抗细菌感染的新型抗菌疗法的一个有吸引力的靶点。
This review focuses on the molecular chaperone ClpB that belongs to the Hsp100/Clp subfamily of the AAA+ ATPases and its biological function in selected bacterial pathogens, causing a variety of human infectious diseases, including zoonoses. It has been established that ClpB disaggregates and reactivates aggregated cellular proteins. It has been postulated that ClpB’s protein disaggregation activity supports the survival of pathogenic bacteria under host-induced stresses (e.g., high temperature and oxidative stress), which allows them to rapidly adapt to the human host and establish infection. Interestingly, ClpB may also perform other functions in pathogenic bacteria, which are required for their virulence. Since ClpB is not found in human cells, this chaperone emerges as an attractive target for novel antimicrobial therapies in combating bacterial infections.
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影响因子：
5.2
作者：
Cantas L;Suer K
通讯作者：
Suer K
影响因子：
3.7
作者：
Erives AJ;Fassler JS
通讯作者：
Fassler JS
影响因子：
11.8
作者：
Hendriksen, SWM;Orsel, K;van Duijkeren, E
通讯作者：
van Duijkeren, E
DOI：
10.1074/jbc.ra120.015413
发表时间：
2021-01
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Glaza P;Ranaweera CB;Shiva S;Roy A;Geisbrecht BV;Schoenen FJ;Zolkiewski M
通讯作者：
Zolkiewski M
影响因子：
4.6
作者：
Alam A;Golovliov I;Javed E;Sjöstedt A
通讯作者：
Sjöstedt A