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Structure-Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes
J. Novak, O. Cerny, A. Osickova, I. Linhartova, J. Masin, L. Bumba, P. Sebo, R. Osicka,
Language English Country Switzerland
Document type Journal Article, Review, Research Support, Non-U.S. Gov't
Grant support
NV16-28126A
MZ0
CEP Register
Digital library NLK
Full text - Article
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PubMed
28946636
DOI
10.3390/toxins9100300
Knihovny.cz E-resources
- MeSH
- Adenylate Cyclase Toxin chemistry MeSH
- Macrophages, Alveolar cytology MeSH
- Cyclic AMP chemistry MeSH
- Bordetella pertussis MeSH
- Dendritic Cells cytology MeSH
- Phagocytes chemistry MeSH
- Syk Kinase MeSH
- Humans MeSH
- Macrophage-1 Antigen MeSH
- Neutrophils cytology MeSH
- Protein Domains MeSH
- Signal Transduction * MeSH
- Protein Structure, Tertiary MeSH
- Structure-Activity Relationship MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
Bordetellae, pathogenic to mammals, produce an immunomodulatory adenylate cyclase toxin-hemolysin (CyaA, ACT or AC-Hly) that enables them to overcome the innate immune defense of the host. CyaA subverts host phagocytic cells by an orchestrated action of its functional domains, where an extremely catalytically active adenylyl cyclase enzyme is delivered into phagocyte cytosol by a pore-forming repeat-in-toxin (RTX) cytolysin moiety. By targeting sentinel cells expressing the complement receptor 3, known as the CD11b/CD18 (αMβ₂) integrin, CyaA compromises the bactericidal functions of host phagocytes and supports infection of host airways by Bordetellae. Here, we review the state of knowledge on structural and functional aspects of CyaA toxin action, placing particular emphasis on signaling mechanisms by which the toxin-produced 3',5'-cyclic adenosine monophosphate (cAMP) subverts the physiology of phagocytic cells.
References provided by Crossref.org
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