Recombinant soluble human CD69 dimer produced in Escherichia coli: Reevaluation of saccharide binding

Robert A. Childs, Christine Galustian, Alexander M. Lawson, Gordon Dougan, Karen Benwell, Gad Frankel, Ten Feizi

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16 Citations (Scopus)


We reevaluate here an earlier report of monosaccharide binding by the C-type lectin-like, leukocyte surface protein CD69 in the form of a recombinant soluble dimer, and we examine polysaccharide binding by the protein. We have expressed in Escherichia coli a new construct of the extracellular part (Q65-K199) of human CD69. We describe the folding in vitro to produce, in good yield, the protein in a soluble, disulphide-linked, dimeric form, and the results of binding experiments with monosaccharides: glucose, galactose, mannose, fucose, N-acetylglucosamine, and N-acetylgalactosamine, linked to bovine serum albumin. Monosaccharide-binding signals are not detectable. Among the polysaccharides, heparin, chondroitin sulphates A, B, and C, fucoidan, and dextran sulphate, CD69 dimer gives a weak binding signal with fucoidan.

Original languageEnglish
Pages (from-to)19-23
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 9 Dec 1999
Externally publishedYes

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