Differential glycosylation of polar and lateral flagellins in Aeromonas hydrophila AH-3.
J Biol Chem
; 287(33): 27851-62, 2012 Aug 10.
Article
em En
| MEDLINE
| ID: mdl-22733809
ABSTRACT
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Oligossacarídeos
/
Aeromonas hydrophila
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Flagelina
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article