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Mannose receptor (CD206) N-glycosylation

ABSTRACT: To explore the influence of glycosylation on mannose receptor (MR) binding to glycan ligands, we used the mouse CTLD4-7, fused to the Fc-portion of human IgG (MR-Fc) and human full-length MR. A detailed N- and O-glycopeptide analysis was performed using tryptic glycopeptides. In addition the samples were partially treated with different exoglycosidases to increase glycopeptide coverage.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

SUBMITTER: Kathrin Stavenhagen

LAB HEAD: Richard D. Cummungs

PROVIDER: PXD034781 | Pride | 2023-03-11

REPOSITORIES: Pride

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			Action	DRS
	KS_MR-Fc_ingel_CHO_LEc_-sia-og_01FA_2018_66_5and5_438.raw	Raw
	KS_MR-Fc_ingel_CHO_LEc_-sia-og_01FA_2018_67_5and5_439.raw	Raw
	KS_MR-Fc_ingel_CHO_LEc_-sia-og_01FA_2018_68_5and5_440.raw	Raw
	KS_MR-Fc_ingel_CHO_PIRP_-sia-og_01FA_2018_63_5and5_434.raw	Raw
	KS_MR-Fc_ingel_CHO_PIRP_-sia-og_01FA_2018_64_5and5_435.raw	Raw

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Publications

N-glycosylation of mannose receptor (CD206) regulates glycan binding by C-type lectin domains.

Stavenhagen Kathrin K Mehta Akul Y AY Laan Lisa L Gao Chao C Heimburg-Molinaro Jamie J van Die Irma I Cummings Richard D RD

The Journal of biological chemistry 20221013 12

The macrophage mannose receptor (MR, CD206) is a transmembrane endocytic lectin receptor, expressed in selected immune and endothelial cells, and is involved in immunity and maintaining homeostasis. Eight of the ten extracellular domains of the MR are C-type lectin domains (CTLDs) which mediate the binding of mannose, fucose, and GlcNAc in a calcium-dependent manner. Previous studies indicated that self-glycosylation of MR regulates its glycan binding. To further explore this structure-function ...[more]

PMID: 36244450

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