Structure-Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00482215" target="_blank" >RIV/61388971:_____/17:00482215 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/17:10366606
Result on the web
<a href="http://dx.doi.org/10.3390/toxins9100300" target="_blank" >http://dx.doi.org/10.3390/toxins9100300</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/toxins9100300" target="_blank" >10.3390/toxins9100300</a>
Alternative languages
Result language
angličtina
Original language name
Structure-Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes
Original language description
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 ((M2)) 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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Toxins
ISSN
2072-6651
e-ISSN
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Volume of the periodical
9
Issue of the periodical within the volume
10
Country of publishing house
CH - SWITZERLAND
Number of pages
28
Pages from-to
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UT code for WoS article
000414626100008
EID of the result in the Scopus database
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