Billington S J, Jost B H, Songer J G
Department of Veterinary Science and Microbiology, 1117 East Lowell Street, The University of Arizona, Tucson, AZ 85721, USA.
FEMS Microbiol Lett. 2000 Jan 15;182(2):197-205. doi: 10.1016/s0378-1097(99)00536-4.
Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell function and cytokine induction. Crystal structure, electron microscopy, mutagenesis and antibody binding studies have led to the modeling of a novel mechanism of pore formation, encompassing membrane-binding, membrane insertion and oligomerization. Despite their designation as thiol-activated cytolysins, it is now clear that thiol activation is not an important property of this group of toxins.
硫醇激活的溶细胞素家族成员参与了多种革兰氏阳性菌的致病机制。虽然它们是成孔毒素，但其主要致病作用可能比简单地裂解宿主细胞更为微妙，可能包括干扰免疫细胞功能和诱导细胞因子。晶体结构、电子显微镜、诱变和抗体结合研究已导致一种新型成孔机制的模型建立，包括膜结合、膜插入和寡聚化。尽管它们被命名为硫醇激活的溶细胞素，但现在很清楚，硫醇激活并非这类毒素的重要特性。
