TY - JOUR
T1 - Effect of O-glycosylation on amyloid fibril formation of the variable domain in the Vλ6 light chain mutant Wil
AU - Abe, Yoshito
AU - Shibata, Hinako
AU - Oyama, Kousuke
AU - Ueda, Tadashi
N1 - Funding Information:
We thank KN International for improving the English usage in the manuscript. We appreciate Mr. Shogo Inoue and Mr. Neo Matsuda for their helpful support for the experiments of peptide analysis and size-exclusion chromatography.
PY - 2021/1/1
Y1 - 2021/1/1
N2 - 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.
AB - 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.
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U2 - 10.1016/j.ijbiomac.2020.10.194
DO - 10.1016/j.ijbiomac.2020.10.194
M3 - Article
C2 - 33127550
AN - SCOPUS:85095744448
VL - 166
SP - 342
EP - 351
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
SN - 0141-8130
ER -