@article{mbs:/content/journal/micro/10.1099/mic.0.2007/011700-0, author = "Hunt, Stuart and Moir, Arthur J. G. and Tzokov, Svetomir and Bullough, Per A. and Artymiuk, Peter J. and Green, Jeffrey", title = "The formation and structure of Escherichia coli K-12 haemolysin E pores", journal= "Microbiology", year = "2008", volume = "154", number = "2", pages = "633-642", doi = "https://doi.org/10.1099/mic.0.2007/011700-0", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.2007/011700-0", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "β-OG, n-octyl β-d-glucopyranoside", abstract = "Some enteric bacteria synthesize a pore-forming toxin, HlyE, which is cytolytic and cytotoxic to host cells. Measurement of HlyE binding to erythrocyte ghosts and the kinetics of HlyE-mediated erythrocyte lysis suggests that interaction with target membranes is not the rate-limiting step in the formation of HlyE pores, but that there is a temperature-dependent lag phase before a functional pore is formed. Circular dichroism and fluorescence energy transfer analyses show that HlyE protomers retain an α-helical structure when oligomerized to form a pore consisting of parallel HlyE protomers. Comparison of the proteolytic sensitivities of the water-soluble and oligomeric forms of HlyE identifies inner and outer surfaces of the pore. This new information has been used to constrain a model of the HlyE pore, which allows a more detailed interpretation of previous low-resolution 3D reconstructions and suggests a novel mechanism for insertion of HlyE into target membranes.", }