Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural heterogeneity of carbohydrate modifications affects serospecificity of Campylobacter flagellins.

Molecular microbiology - 1 Oct 2002

Logan Susan M, Kelly John F, Thibault Pierre, Ewing Cheryl P, Guerry Patricia

Abstract excerpt

Flagellin from Campylobacter coli VC167 is post-translationally modified at > or = 16 amino acid residues with pseudaminic acid and three related derivatives. The predominant modification was 5,7-diacetamido-3,5,7,9 - tetradeoxy - l - glycero - l - manno - nonulosonic acid (pseudaminic acid, Pse5Ac7Ac), a modification that has been described previously on flagellin from Campylobacter jejuni 81-176. VC167 lacked...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antibodies, Bacterial
Share to Campylobacter coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Campylobacter jejuni

Share to Flagellin

Share to Glycosylation

Share to Mass Spectrometry

Share to Protein Processing, Post-Translational

Share to Sialic Acids

Source

Identifiers

PMID: 12406231
DOI: 10.1046/j.1365-2958.2002.03185.x

Genes

SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural heterogeneity of carbohydrate modifications affects serospecificity of Campylobacter flagellins.PMID 12406231Read ↗

Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene.Semantic proximity Read ↗

Targeted metabolomics analysis of Campylobacter coli VC167 reveals legionaminic acid derivatives as novel flagellar glycans.Semantic proximity Read ↗

Functional characterization of the flagellar glycosylation locus in Campylobacter jejuni 81-176 using a focused metabolomics approach.Semantic proximity Read ↗

Characterization of a post-translational modification of Campylobacter flagellin: identification of a sero-specific glycosyl moiety.Semantic proximity Read ↗

Identification and characterization of genes required for post-translational modification of Campylobacter coli VC167 flagellin.Semantic proximity Read ↗

Identification of a core set of Campylobacter jejuni flagella modification genes and a reversible non-motile maf3 phenotype.Semantic proximity Read ↗

Identification of unusual bacterial glycosylation by tandem mass spectrometry analyses of intact proteins.Semantic proximity Read ↗

Uncovering bacterial pseudaminylation with pan-specific antibody toolsSemantic proximity Read ↗

Temperature-dependent phenotypic variation of Campylobacter jejuni lipooligosaccharides.Semantic proximity Read ↗

Modification of the Campylobacter jejuni N-Linked Glycan by EptC Protein-mediated Addition of PhosphoethanolamineSemantic proximity Read ↗

Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori.Semantic proximity Read ↗

Genetics behind the biosynthesis of nonulosonic acid containing lipooligosaccharides in <i>Campylobacter coli</i>Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.