title: Cooperative assembly of beta-barrel pore-forming toxins.
abstract: Bacterial beta-barrel pore-forming toxins are secreted as water-soluble monomeric proteins and assemble into beta-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.
authors.affiliation: Laboratory of Applied Microbiology, Department of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku University, Sendai 981-8555, Japan.
authors.forename: Vananh T
authors.initials: VT
authors.lastname: Nguyen
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Kamio
mesh_terms: D000818:Animals; D001427:Bacterial Toxins / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D001427:Bacterial Toxins