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Glycoprotemics for Hypsibius exemplaris

ABSTRACT: We conducted nanoLC-MS/MS analysis on protein fractions derived from H. exemplaris.

ORGANISM(S): Cellular Organisms

SUBMITTER: Hirokazu Yagi

PROVIDER: PXD055533 | JPOST Repository | Thu Oct 16 00:00:00 BST 2025

REPOSITORIES: jPOST

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Dataset's files

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			Action	DRS
	20200324_kuma64_glycoPepConc_Inj10uL_01.raw	Raw
	20200324_kuma64_glycoPepConc_Inj10uL_01.raw.byspec2	Raw
	Tardigrate%20Glycoproteomics.byparms	Other
	Tardigrate%20Glycoproteomics.byrslt	Other
	Tardigrate%20Glycoproteomics.mgf	Mgf

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Publications

Uncommon N-Glycan Structures in Anhydrobiotic Tardigrades.

Yagi Hirokazu H Saito Taiki T Guu Shih-Yun SY Yamakawa Nao N Shimamura Shigeru S Kondo Sachiko S Yagi-Utsumi Maho M Takai Ken K Furukawa Jun-Ichi JI Guérardel Yann Y Khoo Kay-Hooi KH Arakawa Kazuharu K Kato Koichi K

Molecular & cellular proteomics : MCP 20250428 6

We characterized the N-glycosylation profiles of anhydrobiotic tardigrades, Ramazzottius varieornatus and Hypsibius exemplaris, identifying high-mannose, paucimannose, and complex-type oligosaccharides, while hybrid-type glycans were undetectable. Notably, paucimannose-type oligosaccharides accounted for 39% of the N-glycans in R. varieornatus and 17% in H. exemplaris, with a substantial proportion of them exhibiting fucosylation of the innermost GlcNAc via an α1,6-linkage. This core fucosylatio ...[more]

PMID: 40306492

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