Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 33, Pages 27851-27862Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.376525
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Funding
- Plan Nacional de I + D + i (Ministerio de Educacion, Ciencia y Deporte and Ministerio de Sanidad, Spain)
- Generalitat de Catalunya (Centre de Referencia en Biotecnologia)
- National Research Council Canada
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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.
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