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Published online August 26, 2009
The Journal of Immunology, 2009, 183, 3800 -3809
Copyright © 2009 by The American Association of Immunologists, Inc.
doi:10.4049/jimmunol.0901526

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Characterization of FIBCD1 as an Acetyl Group-Binding Receptor That Binds Chitin1

Anders Schlosser2,*, Theresa Thomsen*, Jesper B. Moeller*, Ole Nielsen{dagger}, Ida Tornøe*, Jan Mollenhauer*, Søren K. Moestrup{ddagger} and Uffe Holmskov*

* Medical Biotechnology Center and {dagger} Department of Pathology, University of Southern Denmark, Odense, Denmark; and {ddagger} Department of Medical Biochemistry, University of Aarhus, Aarhus, Denmark

Chitin is a highly acetylated compound and the second most abundant biopolymer in the world next to cellulose. Vertebrates are exposed to chitin both through food ingestion and when infected with parasites, and fungi and chitin modulate the immune response in different directions. We have identified a novel homotetrameric 55-kDa type II transmembrane protein encoded by the FIBCD1 gene and highly expressed in the gastrointestinal tract. The ectodomain of FIBCD1 is characterized by a coiled-coil region, a polycationic region and C-terminal fibrinogen-related domain that by disulfide linkage assembles the protein into tetramers. Functional analysis showed a high-affinity and calcium-dependent binding of acetylated components to the fibrinogen domain, and a function in endocytosis was demonstrated. Screening for ligands revealed that the FIBCD1 is a high-affinity receptor for chitin and chitin fragments. FIBCD1 may play an important role in controlling the exposure of intestine to chitin and chitin fragments, which is of great relevance for the immune defense against parasites and fungi and for immune response modulation.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 This work was supported by the Novo Nordic Foundation, Fonden til Lægevidenskabens Fremme, and the Lundbeck Foundation.

2 Address correspondence and reprint requests to Dr. Anders Schlosser, Medical Biotechnology Center, University of Southern Denmark, Odense, Denmark. E-mail address: aschlosser{at}health.sdu.dk

3 Abbreviations used in this paper: PAMP, pathogen-associated molecular pattern; AMCase, acidic mammalian chitinase; CHO, Chinese hamster ovary; BS3, bis(sulfosuccinimidyl)suberate; GlcNAc, N-acetylglucosamine; LTA, lipoteichoic acid; TL5A, tachylectin 5A; WGA, wheat germ agglutinin.







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