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Trimeric Form of In...
Trimeric Form of Intracellular ATP Synthase Subunit β of Aggregatibacter actinomycetemcomitans Binds Human Interleukin-1β.
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Paino, Annamari (författare)
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Tuominen, Heidi (författare)
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Jääskeläinen, Mari (författare)
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- Alanko, Jonna (författare)
- Umeå universitet,Oral mikrobiologi
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Nuutila, Jari (författare)
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- Asikainen, Sirkka E (författare)
- Umeå universitet,Oral mikrobiologi
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Pelliniemi, Lauri J (författare)
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Pöllänen, Marja T (författare)
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Chen, Casey (författare)
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Ihalin, Riikka (författare)
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(creator_code:org_t)
- 2011-04-18
- 2011
- Engelska.
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Ingår i: PloS one. - : Public Library of Science. - 1932-6203. ; 6:4, s. e18929-
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https://umu.diva-por... (primary) (Raw object)
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https://journals.plo...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Bacterial biofilms resist host defenses and antibiotics partly because of their decreased metabolism. Some bacteria use proinflammatory cytokines, such as interleukin (IL)-1β, as cues to promote biofilm formation and to alter virulence. Although one potential bacterial IL-1β receptor has been identified, current knowledge of the bacterial IL-1β sensing mechanism is limited. In chronic biofilm infection, periodontitis, Aggregatibacter actinomycetemcomitans requires tight adherence (tad)-locus to form biofilms, and tissue destroying active lesions contain more IL-1β than inactive ones. The effect of IL-1β on the metabolic activity of A. actinomycetemcomitans biofilm was tested using alamarBlue™. The binding of IL-1β to A. actinomycetemcomitans cells was investigated using transmission electron microscopy and flow cytometry. To identify the proteins which interacted with IL-1β, different protein fractions from A. actinomycetemcomitans were run in native-PAGE and blotted using biotinylated IL-1β and avidin-HRP, and identified using mass spectroscopy. We show that although IL-1β slightly increases the biofilm formation of A. actinomycetemcomitans, it reduces the metabolic activity of the biofilm. A similar reduction was observed with all tad-locus mutants except the secretin mutant, although all tested mutant strains as well as wild type strains bound IL-1β. Our results suggest that IL-1β might be transported into the A. actinomycetemcomitans cells, and the trimeric form of intracellular ATP synthase subunit β interacted with IL-1β, possibly explaining the decreased metabolic activity. Because ATP synthase is highly conserved, it might universally enhance biofilm resistance to host defense by binding IL-1β during inflammation.
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PloS one
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Paino, Annamari
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Tuominen, Heidi
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Jääskeläinen, Ma ...
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Alanko, Jonna
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Nuutila, Jari
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Asikainen, Sirkk ...
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visa fler...
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Pelliniemi, Laur ...
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Pöllänen, Marja ...
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Chen, Casey
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Ihalin, Riikka
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visa färre...
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PloS one
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Umeå universitet