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Article

Defects in flagellin glycosylation affect the virulence of Pseudomonas syringae pv. tabaci 6605.

Microbiology (Reading, England) - 1 Jan 2010

Taguchi Fumiko, Yamamoto Masanobu, Ohnishi-Kameyama Mayumi, Iwaki Masako, Yoshida Mitsuru, Ishii Tadashi, Konishi Tomoyuki, Ichinose Yuki

Abstract excerpt

Flagellar motility and its glycosylation are indispensable for the virulence of Pseudomonas syringae pv. tabaci 6605. Six serine residues of the flagellin protein at positions 143, 164, 176, 183, 193 and 201 are glycosylated, and the glycan structure at 201 was determined to consist of a trisaccharide of two L-rhamnosyl residues and a modified 4-amino-4,6-dideoxyglucosyl (viosamine) residue. To investigate the...

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Identifiers

PMID: 19815579
DOI: 10.1099/mic.0.030700-0

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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.

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