Polar glycosylated and lateral non-glycosylated flagella from Aeromonas hydrophila strain AH-1 (serotype O11)

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DOIResolve DOI: http://doi.org/10.3390/ijms161226097
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TypeArticle
Journal titleInternational Journal of Molecular Sciences
ISSN1422-0067
Volume16
Issue12
Pages2825528269
SubjectO-flagellin polar glycosylation; lateral flagellin non-glycosylated; adhesion; biofilm; immune stimulation
AbstractPolar and but not lateral flagellin proteins from Aeromonas hydrophila strain AH-1 (serotype O11) were found to be glycosylated. Top-down mass spectrometry studies of purified polar flagellins suggested the presence of a 403 Da glycan of mass. Bottom-up mass spectrometry studies showed the polar flagellin peptides to be modified with 403 Da glycans in O-linkage. The MS fragmentation pattern of this putative glycan was similar to that of pseudaminic acid derivative. Mutants lacking the biosynthesis of pseudaminic acid (pseB and pseI homologues) were unable to produce polar flagella but no changes were observed in lateral flagella by post-transcriptional regulation of the flagellin. Complementation was achieved by reintroduction of the wild-type pseB and pseI. We compared two pathogenic features (adhesion to eukaryotic cells and biofilm production) between the wild-type strain and two kinds of mutants: mutants lacking polar flagella glycosylation and lacking the O11-antigen lipopolysaccharide (LPS) but with unaltered polar flagella glycosylation. Results suggest that polar flagella glycosylation is extremely important for A. hydrophila AH-1 adhesion to Hep-2 cells and biofilm formation. In addition, we show the importance of the polar flagella glycosylation for immune stimulation of IL-8 production via toll-“like” receptor 5 (TLR5).
Publication date
PublisherMDPI
LanguageEnglish
AffiliationHuman Health Therapeutics; National Research Council Canada
Peer reviewedYes
NPARC number23001584
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Record identifier8ebaa774-9eea-45c6-81c3-ab34c29c21eb
Record created2017-03-08
Record modified2017-03-08
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