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Article ; Online: Production of Highly Active Recombinant Dermonecrotic Toxin of Bordetella Pertussis

Ondrej Stanek / Irena Linhartova / Jana Holubova / Ladislav Bumba / Zdenko Gardian / Anna Malandra / Barbora Bockova / Shihono Teruya / Yasuhiko Horiguchi / Radim Osicka / Peter Sebo

Toxins, Vol 12, Iss 596, p

2020  Volume 596

Abstract: Pathogenic Bordetella bacteria release a neurotropic dermonecrotic toxin (DNT) that is endocytosed into animal cells and permanently activates the Rho family GTPases by polyamination or deamidation of the glutamine residues in their switch II regions (e ... ...

Abstract Pathogenic Bordetella bacteria release a neurotropic dermonecrotic toxin (DNT) that is endocytosed into animal cells and permanently activates the Rho family GTPases by polyamination or deamidation of the glutamine residues in their switch II regions (e.g., Gln63 of RhoA). DNT was found to enable high level colonization of the nasal cavity of pigs by B. bronchiseptica and the capacity of DNT to inhibit differentiation of nasal turbinate bone osteoblasts causes atrophic rhinitis in infected pigs. However, it remains unknown whether DNT plays any role also in virulence of the human pathogen B. pertussis and in pathogenesis of the whooping cough disease. We report a procedure for purification of large amounts of LPS-free recombinant DNT that exhibits a high biological activity on cells expressing the DNT receptors Cav3.1 and Cav3.2Electron microscopy and single particle image analysis of negatively stained preparations revealed that the DNT molecule adopts a V-shaped structure with well-resolved protein domains. These results open the way to structure–function studies on DNT and its interactions with airway epithelial layers.
Keywords Bordetella ; GTPase ; deamidation ; dermonecrotic toxin ; recombinant ; electron microscopy ; negative staining ; image analysis ; Medicine ; R
Subject code 630
Language English
Publishing date 2020-09-01T00:00:00Z
Publisher MDPI AG
Document type Article ; Online
Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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