Site-Specific Classification of N -Linked Oligosaccharides of the Extracellular Regions of Fcγ Receptor IIIb Expressed in Baby Hamster Kidney Cells

Kato, Koichi

doi:10.4172/2153-0637.1000116

Cited by 1 publication

(1 citation statement)

References 30 publications

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“…To study this functional impact, it is important to use the expressing system that assembles the revealed endogenous-like glycosylation profile. Among all five mammalian system producing differently processed N-glycans (HEK293, CHO, BHK, NS0) 33,48,49 , CHO cells constitute a good expression vehicle, where the highly-branched N74 glycans in FcγRIIIa were carrying LacNAc repetitions. However, to produce and investigate antennary fucosylation, which was observed at high levels for FcγRIIIb, the HEK293 system constitutes a better vehicle.…”

Section: Noticeable Differences In Glycosylation Profiles Between Fcγmentioning

confidence: 99%

Site-specific glycosylation mapping of Fc gamma receptor IIIb from neutrophils of health donors

Wójcik

Sénard

Graaf

et al. 2020

Preprint

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Fc gamma receptors (FcγR) translate antigen-recognition by immunoglobulin G (IgG) into various immune responses. A better understanding of this key element of immunity promises novel insights into mechanisms of (auto-/allo-)immune diseases and more rationally designed antibody-based drugs. Glycosylation on both IgG and FcγR impacts their interaction dramatically. In this study, we developed a straightforward and comprehensive analytical methodology to map FcγRIIIb glycosylation from primary human material. In contrast to recently published alternatives, we assessed all glycosylation sites in a single LC-MS/MS run and simultaneously determined the donor allotype. Studying FcγRIIIb derived from healthy donor neutrophils, we observed profound differences as compared to the soluble variant and the homologous FcγRIIIa on natural killer cells. This method will allow assessment of FcγRIII glycosylation differences between individuals, cell types, subcellular locations and pathophysiological conditions.

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Section: Noticeable Differences In Glycosylation Profiles Between Fcγmentioning

confidence: 99%

Site-specific glycosylation mapping of Fc gamma receptor IIIb from neutrophils of health donors

Wójcik

Sénard

Graaf

et al. 2020

Preprint

View full text Add to dashboard Cite

show abstract

Site-Specific Classification of N -Linked Oligosaccharides of the Extracellular Regions of Fcγ Receptor IIIb Expressed in Baby Hamster Kidney Cells

Cited by 1 publication

References 30 publications

Site-specific glycosylation mapping of Fc gamma receptor IIIb from neutrophils of health donors

Site-specific glycosylation mapping of Fc gamma receptor IIIb from neutrophils of health donors

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