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Infection and Immunity, July 2004, p. 4159-4171, Vol. 72, No. 7
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.7.4159-4171.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Characterization of ß-Glucan Recognition Site on C-Type Lectin, Dectin 1

Yoshiyuki Adachi,1 Takashi Ishii,1 Yoshihiko Ikeda,1 Akiyoshi Hoshino,1 Hiroshi Tamura,2 Jun Aketagawa,2 Shigenori Tanaka,2 and Naohito Ohno1*

Laboratory for Immunopharmacology of Microbial Products, School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji,1 Seikagaku Corporation, Higashiyamato, Tokyo, Japan2

Received 14 February 2004/ Returned for modification 1 March 2004/ Accepted 5 April 2004

Dectin 1 is a mammalian cell surface receptor for (1->3)-ß-D-glucans. Since (1->3)-ß-D-glucans are commonly present on fungal cell walls, it has been suggested that dectin 1 is important for recognizing fungal invasion. In this study we tried to deduce the amino acid residues in dectin 1 responsible for ß-glucan recognition. HEK293 cells transfected with mouse dectin 1 cDNA could bind to a gel-forming (1->3)-ß-D-glucan, schizophyllan (SPG). The binding of SPG to a dectin 1 transfectant was inhibited by pretreatment with other ß-glucans having a (1->3)-ß-D-glucosyl linkage but not by pretreatment with {alpha}-glucans. Dectin 1 has a carbohydrate recognition domain (CRD) consisting of six cysteine residues that are highly conserved in C-type lectins. We prepared 32 point mutants with mutations in the CRD and analyzed their binding to SPG. Mutations at Trp221 and His223 resulted in decreased binding to ß-glucan. Monoclonal antibody 4B2, a dectin- 1 monoclonal antibody which had a blocking effect on the ß-glucan interaction, completely failed to bind the dectin-1 mutant W221A. A mutant with mutations in Trp221 and His223 did not have a collaborative effect on Toll-like receptor 2-mediated cellular activation in response to zymosan. These amino acid residues are distinct from residues in other sugar-recognizing peptide sequences of typical C-type lectins. These results suggest that the amino acid sequence W221-I222-H223 is critical for formation of a ß-glucan binding site in the CRD of dectin 1.

* Corresponding author. Mailing address: Laboratory for Immunopharmacology of Microbial Products, School of Pharmacy, Tokyo University of Pharmacy and Life Science, 1432-1 Horinouchi, Hachioji, Tokyo, 192-0392, Japan. Phone: 81-426-76-5599. Fax: 81-426-76-5570. E-mail: adachiyo{at}ps.toyaku.ac.jp.

Editor: T. R. Kozel

Infection and Immunity, July 2004, p. 4159-4171, Vol. 72, No. 7
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.7.4159-4171.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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