Differential glycosylation of polar and lateral flagellins in Aeromonas hydrophila AH-3.
Polar and lateral flagellin proteins from Aeromonas hydrophila strain AH-3 (serotype O34) were found to be glycosylated with different carbohydrate moieties. The lateral flagellin was modified at three sites in O-linkage, with a single monosaccharide of 376 Da, which we show to be a pseudaminic acid derivative. The polar flagellin was modified with a heterogeneous glycan, comprised of a heptasaccharide, linked through the same 376-Da sugar to the protein backbone, also in O-linkage. In-frame deletion mutants of pseudaminic acid biosynthetic genes pseB and pseF homologues resulted in abolition of polar and lateral flagellar formation by posttranscriptional regulation of the flagellins, which was restored by complementation with wild type pseB or F homologues or Campylobacter pseB and F.
Departamento de Microbiología, Facultad de Biología, Universidad de Barcelona, Diagonal 645, 08071 Barcelona, Spain.
Markus
M
Wilhelms
Kelly M
KM
Fulton
Susan M
SM
Twine
Juan M
JM
Tomás
Susana
S
Merino
D016980:Aeromonas hydrophila / Q000235:genetics / Q000378:metabolism*; D002167:Campylobacter / Q000235:genetics / Q000378:metabolism; D005408:Flagellin / Q000235:genetics / Q000378:metabolism*; D005816:Genetic Complementation Test; D006031:Glycosylation; D006836:Hydro-Lyases / Q000235:genetics / Q000378:metabolism; D009844:Oligosaccharides / Q000235:genetics / Q000378:metabolism*
D009844:Oligosaccharides; D005408:Flagellin; D006836:Hydro-Lyases; C533785:UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase, Campylobacter jejuni