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Int. J. Mol. Sci. 2015, 16(12), 28255-28269; doi:10.3390/ijms161226097

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
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Patricia Berninsone
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)
View Full-Text   |   Download PDF [2365 KB, uploaded 27 November 2015]   |  

Abstract

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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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

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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