Effect of O-glycosylation on amyloid fibril formation of the variable domain in the Vλ6 light chain mutant Wil

Yoshito Abe, Hinako Shibata, Kousuke Oyama, Tadashi Ueda

研究成果: Contribution to journalArticle査読

抄録

Glycosylation is one of the major post-translational modifications in eukaryotic cells and has been reported to affect the amyloid fibril formation in several amyloidogenic proteins and peptides. In this study, we expressed a Vλ6 light chain mutant, Wil, which is an amyloidogenic mutant in AL amyloidosis, by the yeast Pichia pastoris. After separation by cation exchange chromatography, we obtained the O-glycosylated and non-glycosylated Wil mutants in high yield. The structures of these Wil mutants were identical except with respect to glycosylation, and the stabilities were also identical. On the other hand, the O-glycosylation retarded the amyloid fibril formation in a sugar size-dependent manner. From these results, we discussed the role of covalently attached glycan in the retardation of amyloid fibril formation.

本文言語英語
ページ(範囲)342-351
ページ数10
ジャーナルInternational Journal of Biological Macromolecules
166
DOI
出版ステータス出版済み - 1 1 2021

All Science Journal Classification (ASJC) codes

  • 構造生物学
  • 生化学
  • 分子生物学
  • 経済学、計量経済学
  • エネルギー(全般)

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