A Naturally Occurring Deletion in FliE from Salmonella enterica Serovar Dublin Results in an Aflagellate Phenotype and Defective Proinflammatory Properties

serovar Dublin is adapted to cattle but is able to infect humans with high invasiveness. An acute inflammatory response at the intestine helps to prevent dissemination to systemic sites. Flagella contribute to this response by providing motility and FliC-mediated signaling through pattern recognitio...

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Bibliographic Details
Published in:Infection and immunity 2018-01, Vol.86 (1)
Main Authors: Sasías, Sebastián, Martínez-Sanguiné, Adriana, Betancor, Laura, Martínez, Arací, D'Alessandro, Bruno, Iriarte, Andrés, Chabalgoity, José A, Yim, Lucía
Format: Article
Language:English
Subjects:
Molecular Pathogenesis
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Summary:serovar Dublin is adapted to cattle but is able to infect humans with high invasiveness. An acute inflammatory response at the intestine helps to prevent dissemination to systemic sites. Flagella contribute to this response by providing motility and FliC-mediated signaling through pattern recognition receptors. In a previous work, we reported a high frequency (11 out of 25) of Dublin isolates lacking flagella in a collection obtained from humans and cattle. The aflagellate strains were impaired in their proinflammatory properties and The aim of this work was to elucidate the underlying cause of the absence of flagella in Dublin isolates. We report here that class 3 flagellar genes are repressed in the human aflagellate isolates, due to impaired secretion of FliA anti-sigma factor FlgM. This phenotype is due to an in-frame 42-nucleotide deletion in the gene, which codes for a protein located in the flagellar basal body. The deletion is predicted to produce a protein lacking amino acids 18 to 31. The aflagellate phenotype was highly stable; revertants were obtained only when was artificially overexpressed combined with several successive passages in motility agar. DNA sequence analysis revealed that motile revertants resulted from duplications of DNA sequences in adjacent to the deleted region. These duplications produced a FliE protein of similar length to the wild type and demonstrate that amino acids 18 to 31 of FliE are not essential. The same deletion was detected in Dublin isolates obtained from cattle, indicating that this mutation circulates in nature.
ISSN:0019-9567
1098-5522
DOI:10.1128/iai.00517-17