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Production of Highly Active Recombinant Dermonecrotic Toxin ofBordetella Pertussis

  1. 1.
    SYSNO ASEP0535246
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleProduction of Highly Active Recombinant Dermonecrotic Toxin ofBordetella Pertussis
    Author(s) Staněk, Ondřej (MBU-M) RID, ORCID
    Linhartová, Irena (MBU-M) RID, ORCID
    Holubová, Jana (MBU-M) RID, ORCID
    Bumba, Ladislav (MBU-M) RID, ORCID
    Gardian, Zdenko (BC-A) RID
    Malandra, Anna (MBU-M) ORCID
    Bočková, Barabora (MBU-M)
    Teruya, S. (JP)
    Horiguchi, Y. (JP)
    Osička, Radim (MBU-M) RID, ORCID
    Šebo, Peter (MBU-M) RID, ORCID
    Article number596
    Source TitleToxins. - : MDPI - ISSN 2072-6651
    Roč. 12, č. 9 (2020)
    Number of pages14 s.
    Languageeng - English
    CountryCH - Switzerland
    KeywordsBordetella ; GTPase ; deamidation ; dermonecrotic toxin ; recombinant
    Subject RIVEE - Microbiology, Virology
    OECD categoryMicrobiology
    Subject RIV - cooperationBiology Centre (since 2006) - Genetics ; Molecular Biology
    R&D ProjectsGX19-27630X GA ČR - Czech Science Foundation (CSF)
    GA19-12695S GA ČR - Czech Science Foundation (CSF)
    LM2018133 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    Research InfrastructureCzech-BioImaging - 90062 - Ústav molekulární genetiky AV ČR, v. v. i.
    Method of publishingOpen access
    Institutional supportMBU-M - RVO:61388971 ; BC-A - RVO:60077344
    UT WOS000580188900001
    EID SCOPUS85091192446
    DOI10.3390/toxins12090596
    AnnotationPathogenicBordetellabacteria 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 byB. bronchisepticaand 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 pathogenB. pertussisand 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 Cav3.2. Electron 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.
    WorkplaceInstitute of Microbiology
    ContactEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Year of Publishing2021
    Electronic addresshttps://www.mdpi.com/2072-6651/12/9/596
Number of the records: 1  

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