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

Identification of glycosylation genes and glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci.

Cellular microbiology - 1 Jun 2006

Taguchi Fumiko, Takeuchi Kasumi, Katoh Etsuko, Murata Katsuyoshi, Suzuki Tomoko, Marutani Mizuri, Kawasaki Takayuki, Eguchi Minako, Katoh Shizue, Kaku Hanae, Yasuda Chihiro, Inagaki Yoshishige, Toyoda Kazuhiro, Shiraishi Tomonori, Ichinose Yuki

Abstract excerpt

A glycosylation island is a genetic region required for glycosylation. The glycosylation island of flagellin in Pseudomonas syringae pv. tabaci 6605 consists of three orfs: orf1, orf2 and orf3. Orf1 and orf2 encode putative glycosyltransferases, and their deletion mutants, Deltaorf1 and Deltaorf2, exhibit deficient flagellin glycosylation or produce partially glycosylated flagellin respectively. Digestion of...

Read the complete abstract on PubMed

Topics

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

Share to Flagella
Share to Flagellin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genomic Islands

Share to Glycosyltransferases

Share to Microscopy, Electron, Scanning

Share to Nicotiana

Share to Pseudomonas syringae

Share to Sequence Analysis, Protein

Source

Identifiers

PMID: 16681835
DOI: 10.1111/j.1462-5822.2005.00674.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of glycosylation genes and glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci.PMID 16681835Read ↗

Defects in flagellin glycosylation affect the virulence of Pseudomonas syringae pv. tabaci 6605.Semantic proximity Read ↗

Flagellin glycosylation island in Pseudomonas syringae pv. glycinea and its role in host specificity.Semantic proximity Read ↗

Genetic analysis of genes involved in synthesis of modified 4-amino-4,6-dideoxyglucose in flagellin of Pseudomonas syringae pv. tabaci.Semantic proximity Read ↗

A genomic island in Pseudomonas aeruginosa carries the determinants of flagellin glycosylation.Semantic proximity Read ↗

Identification of the Flagellin Glycosylation System in Burkholderia cenocepacia and the Contribution of Glycosylated Flagellin to Evasion of Human Innate Immune ResponsesSemantic proximity Read ↗

Flagellin glycosylation in Paenibacillus alvei CCM 2051T.Semantic proximity Read ↗

A homologue of the 3-oxoacyl-(acyl carrier protein) synthase III gene located in the glycosylation island of Pseudomonas syringae pv. tabaci regulates virulence factors via N-acyl homoserine lactone and fatty acid synthesis.Semantic proximity Read ↗

Type IV pilin is glycosylated in Pseudomonas syringae pv. tabaci 6605 and is required for surface motility and virulence.Semantic proximity Read ↗

Flagellin glycans from two pathovars of Pseudomonas syringae contain rhamnose in D and L configurations in different ratios and modified 4-amino-4,6-dideoxyglucose.Semantic proximity Read ↗

Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the HostSemantic proximity Read ↗

Roles of specific amino acids in the N terminus of Pseudomonas aeruginosa flagellin and of flagellin glycosylation in the innate immune response.Semantic proximity Read ↗

The consensus N <sub>glyco</sub> -X-S/T motif and a previously unknown N <sub>glyco</sub> -N -linked glycosylation are necessary for growth and pathogenicity of <i>Phytophthora</i>Semantic proximity Read ↗

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