Hybrid myeloma cells which secrete heterodimetric IgG: A model to study the N‐linked glycan

Abstract

Fundamental questions remain unanswered regarding ihc elTec! of ihe acceptor polypeplidcslruclure on the fine structure of the A'-linkcd glycan of glycoprotcins and conversely, the effect of the glycan structure of IgG on Ihe function and slruelure of the protein. The construction of myeloma hybrids capable of secreting multiple IgG which differ with regard to the tine structure of their /V-linked oligosaccharides would be a valuable model for studying these questions. P3X63Ag8 secretes an IgGi which possesses an oligosaccharide at Asn^'*'' that differs in fine strueture from the analogous glycan of the igGjb secreted by Sp2/HLBu. Fusion hybrids of these cells secrete parental IgGj. and to a lesser degree IgGjb. as well as a heterodimeric IgG containing both ihe 7i and Y2h chains. The oiigosaecharide of each chain is identical in structure to the appropriate parental IgG. Such cells allow for the analysis of acceptor properties that inffuence glycan fine structure, as well as the role of glycan structure on the stability of the IgG.