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Production of Highly Active Recombinant Dermonecrotic Toxin ofBordetella Pertussis
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SYSNO ASEP 0535246 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Production 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, ORCIDArticle number 596 Source Title Toxins. - : MDPI - ISSN 2072-6651
Roč. 12, č. 9 (2020)Number of pages 14 s. Language eng - English Country CH - Switzerland Keywords Bordetella ; GTPase ; deamidation ; dermonecrotic toxin ; recombinant Subject RIV EE - Microbiology, Virology OECD category Microbiology Subject RIV - cooperation Biology Centre (since 2006) - Genetics ; Molecular Biology R&D Projects GX19-27630X 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 Infrastructure Czech-BioImaging - 90062 - Ústav molekulární genetiky AV ČR, v. v. i. Method of publishing Open access Institutional support MBU-M - RVO:61388971 ; BC-A - RVO:60077344 UT WOS 000580188900001 EID SCOPUS 85091192446 DOI 10.3390/toxins12090596 Annotation PathogenicBordetellabacteria 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. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2021 Electronic address https://www.mdpi.com/2072-6651/12/9/596
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