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@article{1080458,
author = {Balonová, Lucie and Mann, B.F. and Červený, Lukáš and Alley, W.R.Jr and Chovancová, Eva and Forslund, AnnaandLena and Solomonsson, E.N. and Forsbeg, A. and Damborský, Jiří and Novotný, L.V. and Henrychová, Lenka and Stulík, Jiří},
article_location = {Bethesda},
article_number = {7},
doi = {http://dx.doi.org/10.1074/mcp.M111.015016},
keywords = {Francisella tularensis; glycosylation; FTH_0069; DsbA; PilA; O-antigen; mass spectrometry},
language = {eng},
issn = {1535-9476},
journal = {Molecular and Cellurar Proteomic},
title = {Characterization of Protein Glycosylation in Francisella tularensis subsp. holarctica},
url = {http://www.mcponline.org/content/11/7/M111.015016},
volume = {11},
year = {2012}
}
TY - JOUR
ID - 1080458
AU - Balonová, Lucie - Mann, B.F. - Červený, Lukáš - Alley, W.R.Jr - Chovancová, Eva - Forslund, Anna-Lena - Solomonsson, E.N. - Forsbeg, A. - Damborský, Jiří - Novotný, L.V. - Henrychová, Lenka - Stulík, Jiří
PY - 2012
TI - Characterization of Protein Glycosylation in Francisella tularensis subsp. holarctica
JF - Molecular and Cellurar Proteomic
VL - 11
IS - 7
SP - 1-12
EP - 1-12
PB - Amer Soc Biochem Biol
SN - 15359476
KW - Francisella tularensis
KW - glycosylation
KW - FTH_0069
KW - DsbA
KW - PilA
KW - O-antigen
KW - mass spectrometry
UR - http://www.mcponline.org/content/11/7/M111.015016
N2 - : FTH_0069 is a previously uncharacterized strongly immunoreactive protein that has been proposed to be a novel virulence factor in Francisella tularensis. Here, the glycan structure modifying two C-terminal peptides of FTH_0069 was identified utilizing high resolution, high mass accuracy mass spectrometry, combined with in-source CID tandem MS experiments. The glycan observed at m/z 1156 was determined to be a hexasaccharide, consisting of two hexoses, three N-acetylhexosamines, and an unknown monosaccharide containing a phosphate group. The monosaccharide sequence of the glycan is tentatively proposed as X-P-HexNAc-HexNAc-Hex-Hex-HexNAc, where X denotes the unknown monosaccharide. The glycan is identical to that of DsbA glycoprotein, as well as to one of the multiple glycan structures modifying the type IV pilin PilA, suggesting a common biosynthetic pathway for the protein modification.Here, we demonstrate that the glycosylation of FTH_0069, DsbA, and PilA was affected in an isogenic mutant with a disrupted wbtDEF gene cluster encoding O-antigen synthesis and in a mutant with a deleted pglA gene encoding pilin oligosaccharyltransferase PglA. Based on our findings, we propose that PglA is involved in both pilin and general F. tularensis protein glycosylation, and we further suggest an inter-relationship between the O-antigen and the glycan synthesis in the early steps in their biosynthetic pathways.
ER -
BALONOVÁ, Lucie, B.F. MANN, Lukáš ČERVENÝ, W.R.Jr ALLEY, Eva CHOVANCOVÁ, Anna-Lena FORSLUND, E.N. SOLOMONSSON, A. FORSBEG, Jiří DAMBORSKÝ, L.V. NOVOTNÝ, Lenka HENRYCHOVÁ and Jiří STULÍK. Characterization of Protein Glycosylation in Francisella tularensis subsp. holarctica. \textit{Molecular and Cellurar Proteomic}. Bethesda: Amer Soc Biochem Biol, 2012, vol.~11, No~7, p.~1-12. ISSN~1535-9476. Available from: https://dx.doi.org/10.1074/mcp.M111.015016.
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