Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.

Throughout evolution, one of the most ancient forms of aggression between cells or organisms has been the production of proteins or peptides affecting the permeability of the target cell membrane. This class of virulence factors includes the largest family of bacterial toxins, the pore-forming toxin...

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Autores principales:	Ioan Iacovache, Matteo T Degiacomi, Lucile Pernot, Sylvia Ho, Marc Schiltz, Matteo Dal Peraro, F Gisou van der Goot
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/797d55a4f57141e19f10db5aefa4b5a9
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spelling	oai:doaj.org-article:797d55a4f57141e19f10db5aefa4b5a92021-11-18T06:03:13ZDual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.1553-73661553-737410.1371/journal.ppat.1002135https://doaj.org/article/797d55a4f57141e19f10db5aefa4b5a92011-07-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21779171/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Throughout evolution, one of the most ancient forms of aggression between cells or organisms has been the production of proteins or peptides affecting the permeability of the target cell membrane. This class of virulence factors includes the largest family of bacterial toxins, the pore-forming toxins (PFTs). PFTs are bistable structures that can exist in a soluble and a transmembrane state. It is unclear what drives biosynthetic folding towards the soluble state, a requirement that is essential to protect the PFT-producing cell. Here we have investigated the folding of aerolysin, produced by the human pathogen Aeromonas hydrophila, and more specifically the role of the C-terminal propeptide (CTP). By combining the predictive power of computational techniques with experimental validation using both structural and functional approaches, we show that the CTP prevents aggregation during biosynthetic folding. We identified specific residues that mediate binding of the CTP to the toxin. We show that the CTP is crucial for the control of the aerolysin activity, since it protects individual subunits from aggregation within the bacterium and later controls assembly of the quaternary pore-forming complex at the surface of the target host cell. The CTP is the first example of a C-terminal chain-linked chaperone with dual function.Ioan IacovacheMatteo T DegiacomiLucile PernotSylvia HoMarc SchiltzMatteo Dal PeraroF Gisou van der GootPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 7, Iss 7, p e1002135 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Ioan Iacovache Matteo T Degiacomi Lucile Pernot Sylvia Ho Marc Schiltz Matteo Dal Peraro F Gisou van der Goot Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.
description	Throughout evolution, one of the most ancient forms of aggression between cells or organisms has been the production of proteins or peptides affecting the permeability of the target cell membrane. This class of virulence factors includes the largest family of bacterial toxins, the pore-forming toxins (PFTs). PFTs are bistable structures that can exist in a soluble and a transmembrane state. It is unclear what drives biosynthetic folding towards the soluble state, a requirement that is essential to protect the PFT-producing cell. Here we have investigated the folding of aerolysin, produced by the human pathogen Aeromonas hydrophila, and more specifically the role of the C-terminal propeptide (CTP). By combining the predictive power of computational techniques with experimental validation using both structural and functional approaches, we show that the CTP prevents aggregation during biosynthetic folding. We identified specific residues that mediate binding of the CTP to the toxin. We show that the CTP is crucial for the control of the aerolysin activity, since it protects individual subunits from aggregation within the bacterium and later controls assembly of the quaternary pore-forming complex at the surface of the target host cell. The CTP is the first example of a C-terminal chain-linked chaperone with dual function.
format	article
author	Ioan Iacovache Matteo T Degiacomi Lucile Pernot Sylvia Ho Marc Schiltz Matteo Dal Peraro F Gisou van der Goot
author_facet	Ioan Iacovache Matteo T Degiacomi Lucile Pernot Sylvia Ho Marc Schiltz Matteo Dal Peraro F Gisou van der Goot
author_sort	Ioan Iacovache
title	Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.
title_short	Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.
title_full	Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.
title_fullStr	Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.
title_full_unstemmed	Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.
title_sort	dual chaperone role of the c-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/797d55a4f57141e19f10db5aefa4b5a9
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Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.

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