Please use this identifier to cite or link to this item: https://doi.org/10.1099/mic.0.038091-0
Title: Modification of the Campylobacter jejuni flagellin glycan by the product of the Cj1295 homopolymeric-tract-containing gene
Authors: Hitchen, P
Brzostek, J 
Panico, M
Butler, J.A
Morris, H.R
Dell, A
Linton, D
Keywords: bacterial protein
campylobacter jejuni 1295 protein
flagellin
glycan
pseudomonic acid
unclassified drug
flagellin
polysaccharide
article
bacterial strain
biosynthesis
Campylobacter jejuni
gene structure
glycosylation
liquid chromatography
mass spectrometry
nonhuman
nucleotide repeat
polyacrylamide gel electrophoresis
priority journal
single nucleotide polymorphism
Campylobacter jejuni
genetics
metabolism
Campylobacter jejuni
Flagellin
Glycosylation
Polysaccharides
Campylobacter jejuni
Campylobacter jejuni
Flagellin
Glycosylation
Polysaccharides
Issue Date: 2010
Citation: Hitchen, P, Brzostek, J, Panico, M, Butler, J.A, Morris, H.R, Dell, A, Linton, D (2010). Modification of the Campylobacter jejuni flagellin glycan by the product of the Cj1295 homopolymeric-tract-containing gene. Microbiology 156 (7) : 1953-1962. ScholarBank@NUS Repository. https://doi.org/10.1099/mic.0.038091-0
Rights: Attribution 4.0 International
Abstract: The Campylobacter jejuni flagellin protein is O-glycosylated with structural analogues of the nine-carbon sugar pseudaminic acid. The most common modifications in the C. jejuni 81-176 strain are the 5,7-di-N-acetylated derivative (Pse5Ac7Ac) and an acetamidino-substituted version (Pse5Am7Ac). Other structures detected include O-acetylated and N-acetylglutamine-substituted derivatives (Pse5Am7Ac8OAc and Pse5Am7Ac8GlnNAc, respectively). Recently, a derivative of pseudaminic acid modified with a di-O-methylglyceroyl group was detected in C. jejuni NCTC 11168 strain. The gene products required for Pse5Ac7Ac biosynthesis have been characterized, but those genes involved in generating other structures have not. We have demonstrated that the mobility of the NCTC 11168 flagellin protein in SDS-PAGE gels can vary spontaneously and we investigated the role of single nucleotide repeats or homopolymeric- tractcontaining genes from the flagellin glycosylation locus in this process. One such gene, Cj1295, was shown to be responsible for structural changes in the flagellin glycoprotein. Mass spectrometry demonstrated that the Cj1295 gene is required for glycosylation with the di-O-methylglyceroyl-modified version of pseudaminic acid. © 2010 SGM.
Source Title: Microbiology
URI: https://scholarbank.nus.edu.sg/handle/10635/180988
ISSN: 1350-0872
DOI: 10.1099/mic.0.038091-0
Rights: Attribution 4.0 International
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