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Glycobiology Advance Access published online on January 29, 2009
Glycobiology, doi:10.1093/glycob/cwp013
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Capture of heat-killed Mycobacterium bovis bacillus Calmette-Guérin by intelectin-1 deposited on cell surfaces

Shoutaro Tsuji1,2,3, Makiko Yamashita2, Donald R. Hoffman4, Akihito Nishiyama2, Tsutomu Shinohara2, Takashi Ohtsu3 and Yoshimi Shibata2

2 Biomedical Sciences, Florida Atlantic University, Boca Raton, Florida 33431
3 Division of Cancer Therapy, Kanagawa Cancer Center Research Institute, Kanagawa 241–0815, Japan
4 Pathology and Laboratory Medicine, Brody School of Medicine at East Carolina University, Greenville, North Carolina 27834

1 Address correspondence to: Shoutaro Tsuji, Ph.D., Division of Cancer Therapy, Kanagawa Cancer Center Research Institute, 1–1-2 Nakao, Asahi-ku, Yokohama-shi, Kanagawa 241–0815, Japan, Phone: +81–45-391–5761 ext. 4054, FAX: +81–45-366–3157, E-mail: stsuji{at}gancen.asahi.yokohama.jp

Intelectin is an extracellular animal lectin found in chordata. Although human and mouse intelectin-1 recognize galactofuranosyl residues included in cell walls of various microorganisms, the physiological function of mammalian intelectin had been unclear. In this study, we found that human intelectin-1 was a serum protein and bound to Mycobacterium bovis bacillus Calmette-Guérin (BCG). Human intelectin-1-binding to BCG was inhibited by Ca2+-depletion, galactofuranosyl disaccharide, ribose, or xylose, and was dependent on the trimeric structure of human intelectin-1. Although mouse intelectin-1 was monomeric, mouse intelectin-1 bound to BCG. The C-terminal region of mouse intelectin-1 contributed to efficient binding to BCG. Human intelectin-1-transfected cells did not only secrete intelectin-1 into culture supernatant but also express intelectin-1 on the cells. The cell surface intelectin-1 was not a glycosylphosphatidylinositol-anchored membrane protein. Intelectin-1-transfected cells captured BCG more than untransfected cells, and the BCG adherence was inhibited by an inhibitory saccharide of intelectin-1. Intelectin-1-preincubated cells took up BCG more than untreated cells, but adhesion of intelectin-1-bound BCG was the same as that of untreated BCG. Mouse macrophages phagocytosed BCG more efficiently in medium containing mouse intelectin-1 than in control medium. These results indicate that intelectin is a host defense lectin that assists phagocytic clearance of microorganisms.

Key words: galactofuranose / innate immunity / intelectin / lectin / mycobacteria


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