Department of General and Medical Biochemistry, Faculty of Biology, University of Gdańsk, 80-308 Gdańsk, Poland.
Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506, USA.
Int J Mol Sci. 2021 May 18;22(10):5319. doi: 10.3390/ijms22105319.
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.
这篇综述聚焦于分子伴侣 ClpB，它属于 Hsp100/Clp 亚家族的 AAA+ATP 酶，及其在一些引起多种人类传染病（包括人畜共患病）的细菌病原体中的生物学功能。已证实 ClpB 可解聚和重新激活聚集的细胞蛋白。有人假设 ClpB 的蛋白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）下的存活，使它们能够快速适应人类宿主并建立感染。有趣的是，ClpB 在病原菌中可能还具有其他功能，这些功能对其毒力是必需的。由于 ClpB 不在人类细胞中发现，这种伴侣蛋白成为新型抗菌疗法治疗细菌感染的有吸引力的靶标。
