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

International journal of biological macromolecules 2021 Jan 01

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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. Copyright © 2020 Elsevier B.V. All rights reserved.

Citation

Yoshito Abe, Hinako Shibata, Kousuke Oyama, Tadashi Ueda. Effect of O-glycosylation on amyloid fibril formation of the variable domain in the Vλ6 light chain mutant Wil. International journal of biological macromolecules. 2021 Jan 01;166:342-351