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"last-update": "2016-09-28T09:44:18",
"secondary-accession": "ERP012949",
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"study-abstract": "The human diarrheal pathogens Campylobacter jejuni and Campylobacter coli interfere with host innate immune signalling by different means, and their flagellins, FlaA and FlaB, have a low intrinsic property to activate the innate immune receptor TLR5. We have investigated here the hypothesis that the unusual secreted, flagellin-like molecule FlaC present in C. jejuni, C. coli and other Campylobacterales might activate cells via TLR5 and interact with TLR5. FlaC shows a striking sequence identity in its D1 domains to TLR5-activating flagellins of other bacteria such as Salmonella, in contrast to non-stimulating Campylobacter flagellins. We overexpressed and purified FlaC, and tested its immunostimulatory properties on cells of human and chicken origin. Treatment of cells with highly purified FlaC resulted in p38 activation. FlaC directly interacted with TLR5. Preincubation with FlaC decreased the responsiveness of chicken and human macrophages towards the bacterial TLR4 agonist LPS, suggesting that FlaC mediates crosstolerance. C. jejuni flaC mutants induced an increase of cell responses in comparison to the wild type, which was suppressed by genetic complementation. Supplementing excess purified FlaC likewise reduced the cellular response to C. jejuni. In vivo, the administration of ultapure FlaC led to a decrease in caecal IL-1beta expression and a significant change of the caecal microbiota in chickens. We propose that Campylobacter spp. have evolved a novel type of immunostimulatory flagellin-like secreted effector in order to specifically modulate host responses, for example towards other PRR ligands such as LPS.",
"study-name": "Novel immunomodulatory flagellin-like protein FlaC in Campylobacter jejuni and other Campylobacterales",
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