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Journal of Biochemistry 2004 136(5):563-567; doi:10.1093/jb/mvh160
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© 2004 The Japanese Biochemical Society

JB MINIREVIEWS

Cooperative Assembly of ß-Barrel Pore-Forming Toxins

Vananh T. Nguyen1,2 and Yoshiyuki Kamio1,*

1 Laboratory of Applied Microbiology, Department of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku University, Sendai 981-8555; and 2 Department of Biochemistry and Plant Physiology, Center for Molecular Biology and Cell Technology, Faculty of Biology, Hanoi University of Science, Vietnam

Bacterial ß-barrel pore–forming toxins are secreted as water-soluble monomeric proteins and assemble into ß-barrel–shaped pores/channels through membranes of target cells, causing cell death and lysis. The pore assemblies that undergo various intermediate stages are symbolized by the association of multi-subunit structures in cells. Crystal structures of water-soluble monomers and membrane-embedded oligomeric pores, and recent studies involving biochemical detection and direct visualization of the sequential assembly of the toxin monomers have solved the mystery of how the pores are formed. Here, we review the mechanism of the cooperative assembly of several toxins of interest to explain the nature of the activities of the toxins.

* To whom correspondence should be addressed. Tel: +81-22-717-8779, Fax: +81-22-717-8780, E-mail: ykamio{at}biochem.tohoku.ac.jp


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