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A Novel Gene, CBP1, Encoding a Putative Extracellular Chitin-Binding Protein, May Play an Important Role in the Hydrophobic Surface Sensing of Magnaporthe grisea During Appressorium Differentiation

May 2002 , Volume 15 , Number  5
Pages  437 - 444

Takashi Kamakura , 1 Syuichi Yamaguchi , 2 Ken-ichiro Saitoh , 2 Tohru Teraoka , 2 and Isamu Yamaguchi 1

1Microbial Toxicology Laboratory, RIKEN Institute, Wako, Saitama 351-0198 Japan; 2Tokyo University of Agriculture and Technology, Fuchu, Tokyo 183-8509 Japan


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Accepted 3 January 2002.

The conidial germ tube of the rice blast fungus, Magnaporthe grisea, differentiates a specialized cell, an appressorium, required for penetration into the host plant. Formation of the appressorium is also observed on artificial solid substrata such as polycarbonate. A novel emerging germ tube-specific gene, CBP1 (chitin-binding protein), was found in a cDNA subtractive differential library. CBP1 coded for a putative extracellular protein (signal peptide) with two similar chitin-binding domains at both ends of a central domain with homology to fungal chitin deacetylases and with a C-terminus domain rich in Ser/Thr related extracellular matrix protein such as agglutinin. The consensus sequence of the chitin-binding domain found in CBP1 has never been reported in fungi and is similar to the chitin-binding motif in plant lectins and plant chitinases classes I and IV. CBP1 was disrupted in order to identify its function. Null mutants of CBP1 failed to differentiate appressoria normally on artificial surface but succeeded in normally differentiating appressoria on the plant leaf surface. Since the null mutant Cbp1- showed abnormal appressorium differentiation only on artificial surfaces and was sensitive to the chemical inducers, CBP1 seemed to play an important role in the recognition of physical factors on solid surfaces.



© 2002 The American Phytopathological Society