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Glycoproteomic and genetic analysis of N-glycosylation of complement component C3 reveals immune pathway regulation

ABSTRACT: This dataset comprises site-specific glycopeptide analysis of complement component C3 from plasma samples of 816 adults from the Korčula cohort (Croatia). C3 glycopeptides were enriched using Concanavalin A lectin affinity chromatography and analyzed by nano-LC-MS/MS. The study characterizes the N-glycan repertoire at both occupied glycosylation sites (N63 and N917), which carry exclusively high-mannose structures including unusual monoglucosylated glycoforms (Glc1Man9GlcNAc2, Glc1Man8GlcNAc2). Glycopeptide quantification was performed to assess associations with demographic and biochemical traits, and to conduct genome-wide association analysis identifying genetic determinants of C3 glycosylation. This represents the first large-scale population-level analysis of site-specific C3 N-glycosylation.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood

SUBMITTER: Dinko Šoić

LAB HEAD: Olga Gornik

PROVIDER: PXD074569 | Pride | 2026-05-30

REPOSITORIES: Pride

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			Action	DRS
	KOR1003.mzML	Mzml
	KOR1006.mzML	Mzml
	KOR1016.mzML	Mzml
	KOR1023.mzML	Mzml
	KOR1031.mzML	Mzml

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