Truncated N-glycans affect protein folding in the ER of CHO-derived mutant cell lines without preventing calnexin binding.

doi:10.1093/glycob/10.1.77

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Article

Truncated N-glycans affect protein folding in the ER of CHO-derived mutant cell lines without preventing calnexin binding.

Glycobiology - 1 Jan 2000

Ermonval M, Duvet S, Zonneveld D, Cacan R, Buttin G, Braakman I

Abstract excerpt

The involvement of N-glycans in the folding of influenza virus hemagglutinin (HA) was analyzed in two CHO-derived glycosylation mutants exhibiting a thermosensitive defect for secretion of human placental alkaline phosphatase. Truncated Man(5)GlcNAc(2)oligosaccharides with one or three glucose residues are attached to proteins of the MadIA214 and B3F7AP2-1 mutant cells, respectively. Newly synthesized proteins...

Topics

Animals
CHO Cells
Calcium-Binding Proteins
Calnexin
Cricetinae
Endoplasmic Reticulum
Glycosylation
Hemagglutinin Glycoproteins, Influenza Virus
Humans
Mannose
Mutation
Polysaccharides
Protein Binding
Protein Folding

Source

Open in PubMed

Identifiers

PMID: 10570226
DOI: 10.1093/glycob/10.1.77

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