Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity.

Lec13 cells, a variant Chinese hamster ovary cell line, were used to produce human IgG1 that were deficient in fucose attached to the Asn(297)-linked carbohydrate but were otherwise similar to that found in IgG1 produced in normal Chinese hamster ovary cell lines and from human serum. Lack of fucose on the IgG1 had no effect on binding to human FcgammaRI, C1q, or the neonatal Fc receptor. Although no change in affinity was found for the His(131) polymorphic form of human FcgammaRIIA, a slight improvement in binding was evident for FcgammaRIIB and the Arg(131) FcgammaRIIA polymorphic form.