2012
Characterization of Protein Glycosylation in Francisella tularensis subsp. holarctica
BALONOVÁ, Lucie; B.F. MANN; Lukáš ČERVENÝ; W.R.Jr ALLEY; Eva CHOVANCOVÁ et al.Základní údaje
Originální název
Characterization of Protein Glycosylation in Francisella tularensis subsp. holarctica
Autoři
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 a Jiří STULÍK
Vydání
Molecular and Cellurar Proteomic, Bethesda, Amer Soc Biochem Biol, 2012, 1535-9476
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 7.251
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:14310/12:00062587
Organizační jednotka
Přírodovědecká fakulta
UT WoS
Klíčová slova anglicky
Francisella tularensis; glycosylation; FTH_0069; DsbA; PilA; O-antigen; mass spectrometry
Změněno: 10. 4. 2013 18:20, Ing. Andrea Mikešková
Anotace
V originále
: 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.