Salt-adaptation of tobacco BY2 cells induces change in glycoform of N-glycans: Enhancement of exo- and endo-glycosidase activities by salt-adaptation

Yoshinobu Kimura, Takao Watanabe, Mariko Kimura, Megumi Maeda, Yoshiyuki Murata, Kazuhito Fujiyama

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

In this report, we describe that a salt adaptation of plant cells induces glycoform changes in N-glycoproteins. Intracellular and cell-wall glycopeptides were prepared from glycoproteins expressed in wild-type BY2 cells and salt-adapted cells. N-Glycans were liberated from those glycopeptides by hydrazinolysis, and the released oligosaccharides were N-acetylated and pyridylaminated. The structures of pyridylaminated (PA-) N-glycans were analyzed by a combination of two-dimensional sugar-chain mapping, MS analysis, and exoglycosidase digestion. In both wild-type cells and salt-adapted cells, the plant complex type structure was predominant among N-glycans expressed on glycoproteins, but we found that the Man2Xyl1Fuc1GlcNAc2 structure was significantly expressed on intracellular and cell-wall glycoproteins of the salt-adapted cells. Furthermore, enhancement of the specific activities of α-mannosidase and β-N-acetylglucosaminidase was observed in the salt-adapted BY2 cells, suggesting that the glycoform changes are due to changes in glycosidase activities.

Original languageEnglish
Pages (from-to)514-522
Number of pages9
JournalBioscience, Biotechnology and Biochemistry
Volume72
Issue number2
DOIs
Publication statusPublished - 2008

Fingerprint

Tobacco
glycosidases
Glycoside Hydrolases
Glycoproteins
Polysaccharides
tobacco
polysaccharides
Salts
salts
glycoproteins
Glycopeptides
glycopeptides
cells
Cell Wall
Mannosidases
Salt-Tolerant Plants
Acetylglucosaminidase
Oligosaccharides
Plant Structures
mannosidases

Keywords

  • Glycoform change
  • N-glycan
  • Plant glycoprotein
  • Salt-adaptation
  • Tobacco BY2 cells

ASJC Scopus subject areas

  • Bioengineering
  • Biotechnology
  • Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry (miscellaneous)
  • Applied Microbiology and Biotechnology
  • Food Science

Cite this

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title = "Salt-adaptation of tobacco BY2 cells induces change in glycoform of N-glycans: Enhancement of exo- and endo-glycosidase activities by salt-adaptation",
abstract = "In this report, we describe that a salt adaptation of plant cells induces glycoform changes in N-glycoproteins. Intracellular and cell-wall glycopeptides were prepared from glycoproteins expressed in wild-type BY2 cells and salt-adapted cells. N-Glycans were liberated from those glycopeptides by hydrazinolysis, and the released oligosaccharides were N-acetylated and pyridylaminated. The structures of pyridylaminated (PA-) N-glycans were analyzed by a combination of two-dimensional sugar-chain mapping, MS analysis, and exoglycosidase digestion. In both wild-type cells and salt-adapted cells, the plant complex type structure was predominant among N-glycans expressed on glycoproteins, but we found that the Man2Xyl1Fuc1GlcNAc2 structure was significantly expressed on intracellular and cell-wall glycoproteins of the salt-adapted cells. Furthermore, enhancement of the specific activities of α-mannosidase and β-N-acetylglucosaminidase was observed in the salt-adapted BY2 cells, suggesting that the glycoform changes are due to changes in glycosidase activities.",
keywords = "Glycoform change, N-glycan, Plant glycoprotein, Salt-adaptation, Tobacco BY2 cells",
author = "Yoshinobu Kimura and Takao Watanabe and Mariko Kimura and Megumi Maeda and Yoshiyuki Murata and Kazuhito Fujiyama",
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T2 - Enhancement of exo- and endo-glycosidase activities by salt-adaptation

AU - Kimura, Yoshinobu

AU - Watanabe, Takao

AU - Kimura, Mariko

AU - Maeda, Megumi

AU - Murata, Yoshiyuki

AU - Fujiyama, Kazuhito

PY - 2008

Y1 - 2008

N2 - In this report, we describe that a salt adaptation of plant cells induces glycoform changes in N-glycoproteins. Intracellular and cell-wall glycopeptides were prepared from glycoproteins expressed in wild-type BY2 cells and salt-adapted cells. N-Glycans were liberated from those glycopeptides by hydrazinolysis, and the released oligosaccharides were N-acetylated and pyridylaminated. The structures of pyridylaminated (PA-) N-glycans were analyzed by a combination of two-dimensional sugar-chain mapping, MS analysis, and exoglycosidase digestion. In both wild-type cells and salt-adapted cells, the plant complex type structure was predominant among N-glycans expressed on glycoproteins, but we found that the Man2Xyl1Fuc1GlcNAc2 structure was significantly expressed on intracellular and cell-wall glycoproteins of the salt-adapted cells. Furthermore, enhancement of the specific activities of α-mannosidase and β-N-acetylglucosaminidase was observed in the salt-adapted BY2 cells, suggesting that the glycoform changes are due to changes in glycosidase activities.

AB - In this report, we describe that a salt adaptation of plant cells induces glycoform changes in N-glycoproteins. Intracellular and cell-wall glycopeptides were prepared from glycoproteins expressed in wild-type BY2 cells and salt-adapted cells. N-Glycans were liberated from those glycopeptides by hydrazinolysis, and the released oligosaccharides were N-acetylated and pyridylaminated. The structures of pyridylaminated (PA-) N-glycans were analyzed by a combination of two-dimensional sugar-chain mapping, MS analysis, and exoglycosidase digestion. In both wild-type cells and salt-adapted cells, the plant complex type structure was predominant among N-glycans expressed on glycoproteins, but we found that the Man2Xyl1Fuc1GlcNAc2 structure was significantly expressed on intracellular and cell-wall glycoproteins of the salt-adapted cells. Furthermore, enhancement of the specific activities of α-mannosidase and β-N-acetylglucosaminidase was observed in the salt-adapted BY2 cells, suggesting that the glycoform changes are due to changes in glycosidase activities.

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KW - Plant glycoprotein

KW - Salt-adaptation

KW - Tobacco BY2 cells

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