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International Immunology Advance Access originally published online on April 19, 2004
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International Immunology, Vol. 16, No. 6, pp. 819-829, June 2004
© 2004 Japanese Society for Immunology

Functional comparison of the mouse DC-SIGN, SIGNR1, SIGNR3 and Langerin, C-type lectins

Kazuhiko Takahara, Yusuke Yashima, Yoshiki Omatsu, Hideo Yoshida, Yukino Kimura, Young-Sun Kang1, Ralph M. Steinman1, Chae Gyu Park1 and Kayo Inaba

Laboratory of Immunobiology, Department of Animal Development and Physiology, Division of Systemic Life Science, Graduate School of Biostudies, Graduate School of Science, Kyoto University, Kitashirakawa-Oiwake-cho, Sakyo-ku, Kyoto 606-8502, Japan 1 Laboratory of Cellular Physiology and Immunology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA

K. Takahara and Y. Yashima contributed equally to this work.
Correspondence to: K. Inaba; E-mail: kayo{at}lif.kyoto-u.ac.jp
Transmitting editor: H. Karasuyama

The mouse (m) DC-SIGN family consists of several homologous type II transmembrane proteins located in close proximity on chromosome 8 and having a single carboxyl terminal carbohydrate recognition domain. We first used transfected non-macrophage cell lines to compare the polysaccharide and microbial uptake capacities of three of these lectins—DC-SIGN, SIGNR1 and SIGNR3—to another homologue mLangerin. Each molecule shares a potential mannose-recognition EPN-motif in its carbohydrate recognition domain. Using an anti-Tag antibody to follow Tag-labeled transfectants, we found that each molecule could be internalized, although the rates differed. However, mDC-SIGN was unable to take up FITC–dextran, FITC–ovalbumin, zymosan or heat-killed Candida albicans. The other three lectins showed distinct carbohydrate recognition properties, assessed by blocking FITC–dextran uptake at 37°C and by mannan binding activity at 4°C. Furthermore, only SIGNR1 was efficient in mediating the capture by transfected cells of Gram-negative bacteria, such as Escherichia coli and Salmonella typhimurium, while none of the lectins tested were competent to capture Gram-positive bacteria, Staphylococcus aureus. Interestingly, transfectants with SIGNR1 lacking the cytoplasmic domain were capable of binding FITC–zymosan in a manner that was abolished by EDTA or mannan, but not laminarin. In addition, resident peritoneal CD11b+ cells expressing SIGNR1 bound zymosan at 4°C in concert with a laminarin-sensitive receptor. Therefore these homologous C-type lectins have distinct recognition patters for microbes despite similarities in the carbohydrate recognition domains.

Keywords: dendritic cells, macrophage, Gram-negative bacteria, phagocytosis


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