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Distinction between Pore Assembly by Staphylococcal α-Toxin versus Leukotoxins
The staphylococcal bipartite leukotoxins and the homoheptameric α-toxin belong to the same family of β-barrel pore-forming toxins 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...
Autores principales: | , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Hindawi Publishing Corporation
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1847480/ https://www.ncbi.nlm.nih.gov/pubmed/17497023 http://dx.doi.org/10.1155/2007/25935 |
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author | Joubert, Olivier Voegelin, Joëlle Guillet, Valérie Tranier, Samuel Werner, Sandra Colin, Didier A. Serra, Mauro Dalla Keller, Daniel Monteil, Henri Mourey, Lionel Prévost, Gilles |
author_facet | Joubert, Olivier Voegelin, Joëlle Guillet, Valérie Tranier, Samuel Werner, Sandra Colin, Didier A. Serra, Mauro Dalla Keller, Daniel Monteil, Henri Mourey, Lionel Prévost, Gilles |
author_sort | Joubert, Olivier |
collection | PubMed |
description | The staphylococcal bipartite leukotoxins and the homoheptameric α-toxin belong to the same family of β-barrel pore-forming toxins 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. |
format | Text |
id | pubmed-1847480 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-18474802007-04-30 Distinction between Pore Assembly by Staphylococcal α-Toxin versus Leukotoxins Joubert, Olivier Voegelin, Joëlle Guillet, Valérie Tranier, Samuel Werner, Sandra Colin, Didier A. Serra, Mauro Dalla Keller, Daniel Monteil, Henri Mourey, Lionel Prévost, Gilles J Biomed Biotechnol Research Article The staphylococcal bipartite leukotoxins and the homoheptameric α-toxin belong to the same family of β-barrel pore-forming toxins 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. Hindawi Publishing Corporation 2007 2007-02-28 /pmc/articles/PMC1847480/ /pubmed/17497023 http://dx.doi.org/10.1155/2007/25935 Text en Copyright © 2007 Olivier Joubert et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Joubert, Olivier Voegelin, Joëlle Guillet, Valérie Tranier, Samuel Werner, Sandra Colin, Didier A. Serra, Mauro Dalla Keller, Daniel Monteil, Henri Mourey, Lionel Prévost, Gilles Distinction between Pore Assembly by Staphylococcal α-Toxin versus Leukotoxins |
title | Distinction between Pore Assembly by Staphylococcal α-Toxin versus Leukotoxins |
title_full | Distinction between Pore Assembly by Staphylococcal α-Toxin versus Leukotoxins |
title_fullStr | Distinction between Pore Assembly by Staphylococcal α-Toxin versus Leukotoxins |
title_full_unstemmed | Distinction between Pore Assembly by Staphylococcal α-Toxin versus Leukotoxins |
title_short | Distinction between Pore Assembly by Staphylococcal α-Toxin versus Leukotoxins |
title_sort | distinction between pore assembly by staphylococcal α-toxin versus leukotoxins |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1847480/ https://www.ncbi.nlm.nih.gov/pubmed/17497023 http://dx.doi.org/10.1155/2007/25935 |
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