Monoglucosylated glycans in the secreted human complement component C3: implications for protein biosynthesis and structure.

Crispin MD; Ritchie GE; Critchley AJ; Morgan BP; Wilson IA; Dwek RA; Sim RB; Rudd PM

doi:10.1016/j.febslet.2004.04.045

Monoglucosylated glycans in the secreted human complement component C3: implications for protein biosynthesis and structure.

Sim RB ,

Affiliations

1. Department of Biochemistry, Oxford Glycobiology Institute, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Authors
Crispin MD¹
(1 author)

ORCIDs linked to this article

FEBS Letters, 01 May 2004, 566(1-3):270-274
https://doi.org/10.1016/j.febslet.2004.04.045 PMID: 15147907

Abstract

The monoglucosylated oligomannose N-linked oligosaccharide (Glc(1)Man(9)GlcNAc(2)) is a retention signal for the calnexin-calreticulin quality control pathway in the endoplasmic reticulum. We report here the presence of such monoglucosylated N-glycans on the human complement serum glycoprotein C3. This finding represents the first report of monoglucosylated glycans on a human serum glycoprotein from non-diseased individuals. The presence of the glucose moiety in 5% of the human C3 glycoprotein suggests that this glycosylation site is sequestered within the protein and is consistent with previous studies identifying a cryptic conglutinin binding site on C3 that becomes exposed upon its conversion to iC3b.

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