Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 15, Issue 12, Pages 21935-21946Publisher
MDPI
DOI: 10.3390/ijms151221935
Keywords
O-flagellin glycosylation; adhesion; biofilm; immune stimulation
Funding
- Ministerio de Economia y Competitividad
- Ministerio de Sanidad, Spain
- Generalitat de Catalunya (Centre de Referencia en Biotecnologia)
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Polar flagellin proteins from Aeromonas hydrophila strain AH-3 (serotype O34) were found to be O-glycosylated with a heterogeneous heptasaccharide glycan. Two mutants with altered (light and strong) polar flagella glycosylation still able to produce flagella were previously obtained, as well as mutants lacking the O34-antigen lipopolysaccharide (LPS) but with unaltered polar flagella glycosylation. We compared these mutants, altogether with the wild type strain, in different studies to conclude that polar flagella glycosylation is extremely important for A. hydrophila adhesion to Hep-2 cells and biofilm formation. Furthermore, the polar flagella glycosylation is an important factor for the immune stimulation of IL-8 production via toll receptor 5 (TLR5).
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