Zhang Yongrong, Feng Hanping
Department of Microbial Pathogenesis, University of Maryland Baltimore, 650 W. Baltimore Street, Baltimore, MD 21201, USA.
Department of Microbial Pathogenesis, University of Maryland Baltimore, 650 W. Baltimore Street, Baltimore, MD 21201, USA
Pathog Dis. 2016 Jun;74(4):ftw024. doi: 10.1093/femspd/ftw024. Epub 2016 Apr 4.
The glucosyltransferase domain ofClostridium difficiletoxins modifies guanine nucleotide-binding proteins of Rho family. It is the major virulent domain of the holotoxins. Various pathogenic effects ofC. difficiletoxins in response to Rho glucosylation have been investigated including cytoskeleton damage, cell death and inflammation. The most recent studies have revealed some significant characteristics of the holotoxins that are independent of glucosylating activity. These findings arouse discussion about the role of glucosyltransferase activity in toxin pathogenesis and open up new insights for toxin mechanism study. In this review, we summarize the pathogenic effects of glucosyltransferase domain of the toxins in the past years.
艰难梭菌毒素的葡糖基转移酶结构域修饰Rho家族的鸟嘌呤核苷酸结合蛋白。它是全毒素的主要毒性结构域。针对Rho糖基化,人们研究了艰难梭菌毒素的各种致病作用,包括细胞骨架损伤、细胞死亡和炎症。最近的研究揭示了全毒素一些与葡糖基化活性无关的重要特征。这些发现引发了关于葡糖基转移酶活性在毒素致病机制中作用的讨论,并为毒素机制研究开辟了新的思路。在本综述中,我们总结了过去几年中该毒素葡糖基转移酶结构域的致病作用。