Differential expression of Galalpha1,3Gal epitope in polymeric and monomeric IgM secreted by mouse myeloma cells deficient in alpha2, 6-sialyltransferase

Glycobiology
D SmilovichF Serafini-Cessi

Abstract

IgM are glycoproteins secreted by plasma cells as (mu2L2)5+J or (mu2L2)6 polymers. In most species, mu- and J-chains bear five and one N -glycans, respectively. Here we compare the terminal glycosylation patterns of 4-hydroxy-3-nitrophenylacetyl (NP)-specific IgM secreted by transfectants of the J558L mouse myeloma deficient in the alpha2,6 sialyltransferase [alpha2,6ST(N)] or by a hybridoma expressing this enzyme (B1.8 cells). The absence of alpha2,6-sialylation results in an increased addition of alpha1, 3-galactosyl residues to mu- and J-chain N-glycans. Since alpha1, 3-galactosyltransferase (alpha1,3Gal-T) is similarly expressed in the two cell lines, these results indicate that a competition reaction occurs in vivo between alpha2,6ST(N) and alpha1,3Gal-T. In the alpha2,6ST(N) deficient transfectants, mu-chains lacking the C-subterminal Cys575 residue, which are secreted mainly in the form of mu2L2 monomers, are more efficiently capped by alpha1, 3-galactosyl residues, confirming that polymerization significantly reduces the accessibility of mu-chain glycans to the Golgi processing enzymes involved in the biogenesis of antennary sugars. Functional assays indicate that IgM sialylation affects antigen-binding and complement-d...Continue Reading

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Citations

Sep 6, 2001·Biotechnology and Bioengineering·A E HillsD C James
Mar 21, 2001·Biotechnology and Bioengineering·K N BakerD C James
Feb 13, 2001·Biochemical and Biophysical Research Communications·D CavalloneF Serafini-Cessi
Aug 1, 2015·Scientific Reports·Maria Francesca MossutoRoberto Sitia
Apr 3, 2016·Journal of the American Society for Mass Spectrometry·Edward S X MohNicolle H Packer
Oct 23, 2003·The Journal of Biological Chemistry·Daniela CavalloneFranca Serafini-Cessi

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