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Glycobiology Advance Access originally published online on November 23, 2006
Glycobiology 2007 17(3):313-323; doi:10.1093/glycob/cwl070
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© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular characterization and oligosaccharide-binding properties of a galectin from the argasid tick Ornithodoros moubata

Xiaohong Huang2,5, Naotoshi Tsuji1,2, Takeharu Miyoshi2, Sachiko Nakamura-Tsuruta3, Jun Hirabayashi3 and Kozo Fujisaki4

2 Laboratory of Parasitic Diseases, National Institute of Animal Health, 3-1-5, Kannondai, Tsukuba, Ibaraki 305-0856, Japan
3 Glycostructure Analysis Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8568, Japan
4 National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido 080-8555, Japan
5 Fujian Center for Disease Control and Prevention, Fuzhou, Fujian 350001, China

1 To whom correspondence should be addressed; Tel and Fax: +81-29-8387749; e-mail: tsujin{at}affrc.go.jp

Received on August 29, 2006; revised on November 10, 2006; accepted on November 13, 2006

The argasid tick Ornithodoros moubata is a vector of various viral and borrelian diseases in animals and humans. We report here molecular characterization and oligosaccharide-binding properties of a novel galectin (OmGalec) from this tick. OmGalec consisted of 333 amino acids with a predicted molecular weight of 37.4 kDa. Its amino acid sequence did not contain a signal peptide or transmembrane domain. It possessed tandem-repeated carbohydrate recognition domains, in which the typical motifs important for carbohydrate affinity were conserved. OmGalec was expressed both transcriptionally and translationally at all stages of the tick life cycle and in multiple organs and was abundant in hemocytes, midguts, and reproductive organs, which are of importance in immunity, interaction with pathogens, and development, respectively, suggesting that OmGalec is a multifunctional molecule. The oligosaccharide affinity profile analyzed by applying an automated frontal affinity chromatography system revealed that rOmGalec showed a general feature of the galectin family, i.e. significant affinity for lactosamine-type disaccharides, Galß1-3(4)Glc(NAc), via recognition of 4-OH and 6-OH of galactose and 3 (4)-OH of Glc(NAc). Its preference for type I saccharides and {alpha}1-3GalNAc-containing oligosaccharides might provide clues for identifying its ligands and its potential multiple functions. Our results may contribute to the elucidation of galectin functions in the development and immunity of arthropods and/or vector and pathogen interaction and provide valuable information for the development of novel tick control strategies.

Key words: frontal affinity chromatography / galectin / ligand–receptor interaction / oligosaccharide affinity / Ornithodoros moubata


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