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J. Biol. Chem., Vol. 278, Issue 40, 38167-38173, October 3, 2003

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Characterization of Streptococcus agalactiae CAMP Factor as a Pore-forming Toxin^*

Shenhui Lang and Michael Palmer 

From the Department of Chemistry, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada

A recombinant form of CAMP factor of Streptococcus agalactiae has been expressed as glutathione S-transferase-CAMP fusion protein in Escherichia coli. After thrombin cleavage of the fusion protein, the recombinant CAMP factor exhibited hemolytic activity comparable with that of the native form. Osmotic protection experiments with polyethylene glycols show that CAMP factor forms discrete transmembrane pores with a diameter upward of 1.6 nm on susceptible membranes; electron microscopy reveals circular membrane lesions of heterogeneous size, up to 12–15 nm in diameter. Liposome permeabilization studies show that pore formation is a highly cooperative process, which suggests that it involves the oligomerization of CAMP factor. Chemical cross-linking experiments also support an oligomeric mode of action.

Received for publication, April 4, 2003 , and in revised form, June 23, 2003.

^* This work was supported by Natural Sciences and Engineering Research Council (Canada) Grant 250265-2003 GSC-032). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 519-888-4567; Fax: 519-746-0435; E-mail: mpalmer{at}uwaterloo.ca.

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