The complexes excreted by VerticiUium dahliae are phytotoxins, which are responsible for most of the symptoms associated with Verticillium wilt disease. Verticillium dahliae toxins （VD-toxins） can be purified by dif...The complexes excreted by VerticiUium dahliae are phytotoxins, which are responsible for most of the symptoms associated with Verticillium wilt disease. Verticillium dahliae toxins （VD-toxins） can be purified by different methods. In the present study, we reported a simpler, more effective method to purify VD-toxins. The supematant of V. dahliae culture was frozen, lyophilized and dialyzed by 1 kDa Dialysis Membranes （MWCO）. We also partially identified the characteristics of the purified VD-toxins. The results showed that the components of VD-toxins include glycoprotein within 35.8-83.2 kDa. The phytotoxic activity of VD-toxins was remained after VD-toxins were pretreated by high temperature, Concanavalin-A, and proteinase E, respectively. These data suggest that VD-toxins are heat-stable, and the protein fraction and glycosyl are both important contributors to the phytotoxic activity. VD-toxins purified effectively from the culture filtrates of V. dahliae may help in further understanding the mechanisms of interactions between V. dahliae and plants.展开更多
基金Acknowledgments： This research was supported by National Natural Science Foundation of China （No. 3017555）, （No. 30170087）.
文摘The complexes excreted by VerticiUium dahliae are phytotoxins, which are responsible for most of the symptoms associated with Verticillium wilt disease. Verticillium dahliae toxins （VD-toxins） can be purified by different methods. In the present study, we reported a simpler, more effective method to purify VD-toxins. The supematant of V. dahliae culture was frozen, lyophilized and dialyzed by 1 kDa Dialysis Membranes （MWCO）. We also partially identified the characteristics of the purified VD-toxins. The results showed that the components of VD-toxins include glycoprotein within 35.8-83.2 kDa. The phytotoxic activity of VD-toxins was remained after VD-toxins were pretreated by high temperature, Concanavalin-A, and proteinase E, respectively. These data suggest that VD-toxins are heat-stable, and the protein fraction and glycosyl are both important contributors to the phytotoxic activity. VD-toxins purified effectively from the culture filtrates of V. dahliae may help in further understanding the mechanisms of interactions between V. dahliae and plants.
