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

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.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Abe Y,Shibata H,Oyama K,Ueda T

doi

10.1016/j.ijbiomac.2020.10.194

subject

Has Abstract

pub_date

2021-01-01 00:00:00

pages

342-351

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(20)34850-9

journal_volume

166

pub_type

杂志文章

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