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Microbiology 154 (2008), 633-642; DOI  10.1099/mic.0.2007/011700-0
© 2008 Society for General Microbiology

The formation and structure of Escherichia coli K-12 haemolysin E pores

Stuart Hunt, Arthur J. G. Moir, Svetomir Tzokov, Per A. Bullough, Peter J. Artymiuk and Jeffrey Green

Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield S10 2TN, UK

Correspondence
Jeffrey Green
jeff.green{at}sheffield.ac.uk
Peter J. Artymiuk
p.j.artymiuk{at}sheffield.ac.uk

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 {alpha}-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.

Abbreviations: β-OG, n-octyl β-D-glucopyranoside

Two supplementary figures of models of octameric and 13-meric HlyE pores showing proteolytic cleavage sites and of the locations of proteolytic sites mapped onto an HlyE protomer are available with the online version of this paper.






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