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Open AccessArticle

Polar Glycosylated and Lateral Non-Glycosylated Flagella from Aeromonas hydrophila Strain AH-1 (Serotype O11)

1
National Research Council, 100 Sussex Drive, Ottawa, ON K1A0R1, Canada
2
Departamento de Microbiología, Facultad de Biología, Universidad de Barcelona, Diagonal 645, Barcelona 08071, Spain
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Patricia Berninsone
Int. J. Mol. Sci. 2015, 16(12), 28255-28269; https://doi.org/10.3390/ijms161226097
Received: 8 October 2015 / Revised: 17 November 2015 / Accepted: 18 November 2015 / Published: 27 November 2015
(This article belongs to the Special Issue Glycosylation and Glycoproteins)
Polar 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). View Full-Text
Keywords: O-flagellin polar glycosylation; lateral flagellin non-glycosylated; adhesion; biofilm; immune stimulation O-flagellin polar glycosylation; lateral flagellin non-glycosylated; adhesion; biofilm; immune stimulation
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Fulton, K.M.; Mendoza-Barberá, E.; Twine, S.M.; Tomás, J.M.; Merino, S. Polar Glycosylated and Lateral Non-Glycosylated Flagella from Aeromonas hydrophila Strain AH-1 (Serotype O11). Int. J. Mol. Sci. 2015, 16, 28255-28269.

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