Differential structure and activity between human and mouse intelectin-1: Human intelectin-1 is a disulfide-linked trimer, whereas mouse homologue is a monomer
Open Access
- 9 July 2007
- journal article
- research article
- Published by Oxford University Press (OUP) in Glycobiology
- Vol. 17 (10), 1045-1051
- https://doi.org/10.1093/glycob/cwm075
Abstract
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.Keywords
This publication has 37 references indexed in Scilit:
- Dissecting asthma using focused transgenic modeling and functional genomicsJournal of Allergy and Clinical Immunology, 2005
- Identification of Novel Genes in Intestinal Tissue That Are Regulated after Infection with an Intestinal Nematode ParasiteInfection and Immunity, 2005
- The Xenopus laevis cortical granule lectin: cDNA cloning, developmental expression, and identification of the eglectin family of lectinsComparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, 2003
- A unique primary structure, cDNA cloning and function of a galactose‐specific lectin from ascidian plasmaEuropean Journal of Biochemistry, 1999
- Cloning of the Novel Gene Intelectin, Which Is Expressed in Intestinal Paneth Cells in MiceBiochemical and Biophysical Research Communications, 1998
- Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectinsBiochemical Journal, 1995
- Major structural features of the cell wall arabinogalactans of Mycobacterium, Rhodococcus, and Nocardia spp.Carbohydrate Research, 1993
- Complete structure of the cell surface polysaccharide of Streptococcus oralis C104: a 600-MHz NMR studyBiochemistry, 1991
- Subunit structure of a cortical granule lectin involved in the block to polyspermy in Xenopus laevis eggsFEBS Letters, 1986
- The vitelline envelope to fertilization envelope conversion in eggs of Xenopus laevisDevelopmental Biology, 1986