Glycobiology Advance Access originally published online on July 9, 2007
Glycobiology 2007 17(10):1045-1051; doi:10.1093/glycob/cwm075
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Differential structure and activity between human and mouse intelectin-1: Human intelectin-1 is a disulfide-linked trimer, whereas mouse homologue is a monomer
2 Biomedical Sciences, Florida Atlantic University, Boca Raton, FL 33431, USA;
3 404 Palmeto Dr, Caswell Beach, NC 28465, USA;
4 Pathology and Laboratory Medicine
5 Physiology, Brody School of Medicine at East Carolina University, Greenville, NC 27834, USA
1 To whom correspondence should be addressed: Tel: + 81-45-391-5761 ext. 4054; Fax: +81-45-366-3157; e-mail: stsuji{at}gancen.asahi.yokohama.jp
Received on November 21, 2006; revised on June 29, 2007; accepted on July 2, 2007
Human intelectin-1 (hITLN-1) is a 120-kDa lectin recognizing galactofuranosyl residues found in cell walls of various microorganisms but not in mammalian tissues. Although mouse intelectin-1 (mITLN-1) has been identified previously, its biochemical properties and functional characteristics have not been studied. Therefore, we have compared structures and saccharide-binding specificities of hITLN-1 and mITLN-1 using recombinant proteins produced by mammalian cells. Recombinant hITLN-1 is a trimer, disulfide-linked through Cys-31 and Cys-48, and N-glycosylated at Asn-163. Despite 84.9% amino acid identity to hITLN-1, recombinant and intestinal mITLN-1 are unglycosylated 30-kDa monomers. Recombinant hITLN-1, as well as recombinant and intestinal mITLN-1 were purified by Ca2+-dependent adsorption to galactose-Sepharose. In competitive binding studies, hITLN-1 was eluted from galactose-Sepharose by 100 mM 2-deoxygalactose, a galactofuranosyl disaccharide, D-xylose, and both D- and L-ribose. In contrast, mITLN-1 was partially eluted by the galactofuranosyl disaccharide, and only minimally by the other saccharides indicating that the two intelectins have different saccharide-binding specificities. When the N- and C-terminal regions of hITLN-1 were replaced, respectively, with those of mITLN-1, galactose-Sepharose binding was associated with the C-terminal regions. Finally, hITLN-1 binding to galactose-Sepharose was not affected by the substitution of the Cys residues in the N-terminal region that are necessary for oligomer formation, nor was it affected by the removal of the N-linked oligosaccharide at Asn-163. Although both hITLN-1 and mITLN-1 recognize galactofuranosyl residues, our comparative studies, taken together, demonstrate that these intelectins have different quaternary structures and saccharide-binding specificities.
Key words: galactofuranose / galactose / innate immunity / intelectin / lectin
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