Characterization of the oligosaccharides from the invariant chain associated with murine Ia antigens

S. J. Swiedler, Gerald Warren Hart, J. H. Freed

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Abstract

The oligosaccharide side chains of the murine invariant chain (I(i)) glycoprotein associated with the Ia antigens have been characterized. Affinity chromatography using a monoclonal antibody column was employed to purify the I-A(k) antigen from lysates of the AKTB-1b B cell lymphoma. The invariant chain isolated by this procedure was subsequently digested with proteases, and the resulting glycopeptides were fractionated by reverse-phase high-pressure liquid chromatography (HPLC). The invariant chain appears to contain two glycosylation sites, both of which carry high-mannose oligosaccharides, each with a restricted size distribution and an average composition of Man6GIcNAc2 as judged by gel filtration and α-mannosidase digestion. These data, together with the observation that the invariant chain cannot be labeled metabolically with 3H-glucosamine, 3H-fucose, or 3H-galactose, allow the conclusion that the murine invariant chain does not contain complex oligosaccharides and is not O-glycosylated during its association with the Ia antigens.

Original languageEnglish (US)
Pages (from-to)352-358
Number of pages7
JournalJournal of Immunology
Volume131
Issue number1
Publication statusPublished - 1983

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ASJC Scopus subject areas

  • Immunology

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