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

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)342-351
Number of pages10
JournalInternational Journal of Biological Macromolecules
Volume166
DOIs
Publication statusPublished - Jan 1 2021

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Economics and Econometrics
  • Energy(all)

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