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Characterization ofβ-Glucan RecognitionSite on C-TypeLectin, Dectin 1 Yoshiyuki AdachiTakashi IshiiYoshihiko Ikeda2004 год

Characterization of β-Glucan Recognition Site on C-Type Lectin, Dectin 1
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Аннотация: Dectin 1 is a mammalian cell surface receptor for (1-->3)-beta-d-glucans. Since (1-->3)-beta-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 beta-glucan recognition. HEK293 cells transfected with mouse dectin 1 cDNA could bind to a gel-forming (1-->3)-beta-d-glucan, schizophyllan (SPG). The binding of SPG to a dectin 1 transfectant was inhibited by pretreatment with other beta-glucans having a (1-->3)-beta-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 Trp(221) and His(223) resulted in decreased binding to beta-glucan. Monoclonal antibody 4B2, a dectin- 1 monoclonal antibody which had a blocking effect on the beta-glucan interaction, completely failed to bind the dectin-1 mutant W221A. A mutant with mutations in Trp(221) and His(223) 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 beta-glucan binding site in the CRD of dectin 1.
Год издания: 2004
Авторы: Yoshiyuki Adachi, Takashi Ishii, Yoshihiko Ikeda, Akiyoshi Hoshino, Hiroshi Tamura, Jun Aketagawa, Shigenori Tanaka, Naohito Ohno
Издательство: American Society for Microbiology
Источник: Infection and Immunity
Ключевые слова: Polysaccharides and Plant Cell Walls, Plant-Microbe Interactions and Immunity, Studies on Chitinases and Chitosanases
Другие ссылки: Infection and Immunity (HTML)
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Europe PMC (PubMed Central) (HTML)
PubMed Central (HTML)
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