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Recombinant human interleukin-12 is the second example of a C-mannosylated protein

Doucey, Marie-Agnès ; Hess, Daniel ; Blommers, Marcel J.J. ; Hofsteenge, Jan

In: Glycobiology, 1999, vol. 9, no. 5, p. 435-441

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    Titre
    • Recombinant human interleukin-12 is the second example of a C-mannosylated protein
    Auteur
    • Doucey, Marie-Agnès. Friedrich Miescher-Institut, P.O. Box 2543, CH-4002 Basel, Switzerland
    • Hess, Daniel. Friedrich Miescher-Institut, P.O. Box 2543, CH-4002 Basel, Switzerland
    • Blommers, Marcel J.J.. Novartis Pharma AG, P.O. Box, CH-4002 Basel, Switzerland
    • Hofsteenge, Jan. Friedrich Miescher-Institut, P.O. Box 2543, CH-4002 Basel, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Glycobiology, 1999, vol. 9, no. 5, p. 435-441. Oxford University Press
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:304956
    Summary
    The β-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp. In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan. Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319β is (partially) C-mannosylated. This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor. Furthermore, human B-lymphoblastoid cells, which secrete IL-12, were found to contain an enzyme that carries out the C-mannosylation reaction. This shows that nonrecombinant IL-12 is potentially C-mannosylated as well. This is only the second report on a C-mannosylated protein. However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found