Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysins.
Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysins.
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DOI:
10.1007/978-94-017-8881-6_5
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发表时间:
2014
影响因子:
--
通讯作者:
Heuck AP
中科院分区:
文献类型:
--
作者:
Johnson BB;Heuck AP
Cholesterol-dependent cytolysins (CDCs) constitute a family of pore forming toxins secreted by Gram positive bacteria. These toxins form transmembrane pores by inserting a large β-barrel into cholesterol-containing membrane bilayers. Binding of water-soluble CDCs to the membrane triggers the formation of oligomers containing 35-50 monomers. The coordinated insertion of more than seventy β-hairpins into the membrane requires multiple structural conformational changes. Perfringolysin O (PFO), secreted by Clostridium perfringens, has become the prototype for the CDCs. In this chapter, we will describe current knowledge on the mechanism of PFO cytolysis, with special focus on cholesterol recognition, oligomerization, and the conformational changes involved in pore formation.