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

• Published in: Immunology and cell biology Vol. 69; no. 3; pp. 151 - 157
• Main Authors: LEE, S‐O., PORETZ, R. D.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 22-12-2017
• ISSN: 0818-9641; 1440-1711
• DOI: 10.1038/icb.1991.23

Summary
Fundamental questions remain unanswered regarding the effect of the acceptor polypeptide structure on the fine structure of the N‐linked glycan of glycoproteins and conversely, the effect of the glycan structure of IgG on the function and structure of the protein. The construction of myeloma hybrids capable of secreting multiple IgG which differ with regard to the fine structure of their N‐linked oligosaccharides would be a valuable model for studying these questions. P3X63Ag8 secretes an IgG1 which possesses an oligosaccharide at Asn297 that differs in fine structure from the analogous glycan of the IgG2b secreted by Sp2/HLBu. Fusion hybrids of these cells secrete parental IgG1, and to a lesser degree IgG2b, as well as a heterodimeric IgG containing both the γ1 and γ2b chains. The oligosaccharide of each chain is identical in structure to the appropriate parental IgG. Such cells allow for the analysis of acceptor properties that influence glycan fine structure, as well as the role of glycan structure on the stability of the IgG.