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Article Dans Une Revue Journal of Biomedicine and Biotechnology Année : 2007

Distinction between Pore Assembly by Staphylococcal α-Toxin versus Leukotoxins

Résumé

The staphylococcal bipartite leukotoxins and the homoheptameric α-toxin belong to the same family of β-barrel pore-forming tox-ins despite slight differences. In the α-toxin pore, the N-terminal extremity of each protomer interacts as a deployed latch with two consecutive protomers in the vicinity of the pore lumen. N-terminal extremities of leukotoxins as seen in their three-dimensional structures are heterogeneous in length and take part in the β-sandwich core of soluble monomers. Hence, the interaction of these N-terminal extremities within structures of adjacent monomers is questionable. We show here that modifications of their N-termini by two different processes, using fusion with glutathione S-transferase (GST) and bridging of the N-terminal extremity to the adjacent β-sheet via disulphide bridges, are not deleterious for biological activity. Therefore, bipartite leukotoxins do not need a large extension of their N-terminal extremities to form functional pores, thus illustrating a microheterogeneity of the structural organizations between bipartite leukotoxins and α-toxin.
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Dates et versions

hal-03003420 , version 1 (13-11-2020)

Identifiants

Citer

Olivier R. Joubert, Joëlle Voegelin, Valérie Guillet, Samuel Tranier, Sandra Werner, et al.. Distinction between Pore Assembly by Staphylococcal α-Toxin versus Leukotoxins. Journal of Biomedicine and Biotechnology, 2007, 2007, pp.025935. ⟨10.1155/2007/25935⟩. ⟨hal-03003420⟩
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