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moflp1,encoding a novel fungal fasciclin-like protein,is involved in conidiation and pathogenicity in Magnaporthe oryzae

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Journal of Zhejiang University-Science B(Biomedicine & Biotechnology) 2009年第6期10卷 434-444页

作者： Tong-bao LIU Guo-qing CHEN Hang MIN Fu-cheng LIN State Key Laboratory for Rice Biology Biotechnology Institute Zhejiang University Hangzhou 310029 China College of Life Sciences Zhejiang University Hangzhou 310058 China

Fasciclin family proteins have been identified as cell adhesion molecules in various organisms. In this study, a novel Magnaporthe oryzae fasciclin-like protein encoding gene, named moflp1, was isolated from a subtractive suppressive cDNA library and functionally analyzed. Sequence analysis showed that the moflp1 gene contains an open reading frame (ORF) of 1050 nucleotides encoding 349 amino acids with a calculated molecular weight of 35.85 kDa and a pI of 7.76. The deduced moflp1 protein contains a 17-amino acid secretion signal sequence and an 18-amino acid sequence with the characteristics of a glycosylphosphotidylinositol (GPI) anchor additional signal at its N- and C-terminuses, respectively. Potential N-glycosylation sites and domains involving cell adhesion were also identified in moflp1. Sequence analysis and subcellular localization by the expression of moflp1-GFP fusion construct in M. oryzae indicated that the moflp1 protein is probably localized on the vacuole membrane. Two moflp1 null mutants generated by targeted gene disruption exhibited marked reduction of conidiation, conidial adhesion, appressorium turgor, and pathogenicity. Our results indicate that fasciclin proteins play important roles in fungal de-velopment and pathogenicity in M. oryzae.

关键词： Magnaporthe oryzae Fasciclin moflp1 Cellular localization Conidiation Pathogenicity

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