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The leukocidin pore: Evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis

Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Oxford OX1 3TA, England, United Kingdom

(RECEIVED June 11, 2005; FINAL REVISION June 11, 2005; ACCEPTED June 25, 2005)

The staphylococcal -hemolysin (HL) and leukocidin (Luk) polypeptides are members of a family of related -barrel pore-forming toxins. Upon binding to susceptible cells, HL forms water-filled homoheptameric transmembrane pores. By contrast, Luk pores are formed by two classes of subunit, F and S, rendering a heptameric structure displeasing on symmetry grounds at least. Both the subunit stoichiometry and arrangement within the Luk pore have been contentious issues. Here we use chemical and genetic approaches to show that (1) the predominant, or perhaps the only, form of the Luk pore is an octamer; (2) the subunit stoichiometry is 1:1; and (3) the subunits are arranged in an alternating fashion about a central axis of symmetry, at least when a fused LukS-LukF construct is used. The experimental approaches we have used also open up new avenues for engineering the arrangement of the subunits of -barrel pore-forming toxins.

Keywords: -barrel; chemical cross-linking; concatameric subunits; leukocidin; pore-forming toxin; staphylococcal -hemolysin; subunit stoichiometry; subunit arrangement

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051648505.

Reprint requests to: Hagan Bayley, Department of Chemistry, University of Oxford, Oxford OX1 3TA, England, United Kingdom; e-mail: hagan.bayley{at}chem.ox.ac.uk; fax: +44-1865-275708.

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