Premium
Hybrid myeloma cells which secrete heterodimetric IgG: A model to study the N ‐linked glycan
Author(s) -
LEE SO.,
PORETZ R. D.
Publication year - 1991
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1038/icb.1991.23
Subject(s) - glycan , glycoprotein , secretion , chemistry , oligosaccharide , biology , biochemistry
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 IgG 1 which possesses an oligosaccharide at Asn 297 that differs in fine structure from the analogous glycan of the IgG 2b secreted by Sp2/HLBu. Fusion hybrids of these cells secrete parental IgG 1 , and to a lesser degree IgG 2b , as well as a heterodimeric IgG containing both the γ 1 and γ 2b 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.