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J Biol Chem, Vol. 275, Issue 7, 4995-5002, February 18, 2000

A Pattern-recognition Protein for -1,3-Glucan
THE BINDING DOMAIN AND THE cDNA CLONING OF -1,3-GLUCAN RECOGNITION PROTEIN FROM THE SILKWORM, BOMBYX MORI^*

Masanori Ochiai and Masaaki Ashida

From the Institute of Low Temperature Science, Hokkaido University, Sapporo 060-0819, Japan

The -1,3-glucan recognition protein (GRP) has strong specific affinity for -1,3-glucan, a component of the fungal cell wall. Its interaction with -1,3-glucan initiates the activation of the prophenoloxidase cascade, which is an important defense system in invertebrates of many species. We cloned the cDNA of the GRP of the silkworm Bombyx mori. The GRP mRNA transcript was constitutively expressed in the hemocytes, fat body, and epithelial cells of the naive silkworm. At the same time, a bacterial or yeast challenge was indicated to intensify the transcription. Comparison of the deduced amino acid sequence with known sequences revealed that the GRP contained a region (Thr²⁶⁴ to Pro³⁸⁶) displaying significant similarity to the catalytic regions of bacterial -1,3-glucanases and much higher similarity to the glucanase-like regions of Gram-negative bacteria-binding proteins found in the silkworm B. mori and the mosquito Anopheles gambiae. The region (Thr²⁶⁴ to Pro³⁸⁶) of the GRP, however, was demonstrated not to have appreciable affinity for -1,3-glucan. A recombinant peptide corresponding to an N-terminal region (Tyr¹ to Ala¹⁰²) of the GRP bound strongly to -1,3-glucan. These results indicate that the binding domain of the GRP for -1,3-glucan is located in the N-terminal region. Glucanases and the current pattern-recognition proteins that contain a glucanase-like region seem to have a common origin in their molecular evolution.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AB026441.

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