Differential glycosylation of polar and lateral flagellins in Aeromonas hydrophila AH-3

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DOIResolve DOI: http://doi.org/10.1074/jbc.M112.376525
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TypeArticle
Journal titleJournal of Biological Chemistry
ISSN0021-9258
1083-351X
Volume287
Issue33
Pages2785127862; # of pages: 12
SubjectBacteria; Genetics; Glycoprotein; Molecular Biology; Mutagenesis; Flagellin; Mass Spectrometry; Pseudaminic Acid
AbstractPolar 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.
Publication date
LanguageEnglish
AffiliationHuman Health Therapeutics; National Research Council Canada
Peer reviewedYes
NPARC number21269084
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Record identifier231964a8-d413-4bfe-85a1-ecb09a19ef3f
Record created2013-12-05
Record modified2016-05-09
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