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* Medical Biotechnology Center and
Department of Pathology, University of Southern Denmark, Odense, Denmark; and
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.
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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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