Identification of Genes Involved in the Glycosylation of Modified Viosamine of Flagellins in Pseudomonas syringae by Mass Spectrometry

Genes

Masanobu Yamamoto¹  Mayumi Ohnishi-Kameyama¹  Chi L. Nguyen²  Fumiko Taguchi²  Kazuhiro Chiku¹  Tadashi Ishii¹  Hiroshi Ono¹  Mitsuru Yoshida¹ 

[1] National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan; E-Mails:;The Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka 1-1-1, Okayama 700-8530, Japan; E-Mails:

关键词: flagellin;    glycosylation;    mass spectrometry;    viosamine island;   

DOI  :  10.3390/genes2040788

来源: mdpi

【 摘 要 】

Previously we revealed that flagellin proteins in Pseudomonas syringae pv. tabaci 6605 (Pta 6605) were glycosylated with a trisaccharide, modified viosamine (mVio)-rhamnose-rhamnose and that glycosylation was required for virulence. We further identified some glycosylation-related genes, including vioA, vioB, vioT, fgt1, and fgt2. In this study, we newly identified vioR and vioM in a so-called viosamine island as biosynthetic genes for glycosylation of mVio in Pta 6605 by the mass spectrometry (MS) of flagellin glycan in the respective mutants. Furthermore, characterization of the mVio-related genes and MS analyses of flagellin glycans in other pathovars of P. syringae revealed that mVio-related genes were essential for mVio biosynthesis in flagellin glycans, and that P. syringae pv. syringae B728a, which does not possess a viosamine island, has a different structure of glycan in its flagellin protein.

【 授权许可】

CC BY   
© 2011 by the authors; licensee MDPI, Basel, Switzerland.