Open AccessThe Magnaporthe grisea snodprot1 homolog, MSP1, is required for virulence
Author(s) -
Jeong Jun Seop,
Mitchell Thomas K.,
Dean Ralph A.
Publication year - 2007
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2007.00796.x
Subject(s) - magnaporthe grisea , appressorium , biology , virulence , magnaporthe , mutant , fungus , microbiology and biotechnology , gene , transformation (genetics) , effector , western blot , southern blot , genetics , oryza sativa , botany
Secreted proteins play central roles in plant–microbe interactions acting as signals, toxins, and effectors. One important group of small secreted proteins is the snodprot1 family, members of which have demonstrated phytotoxic properties. A split‐marker transformation system was applied for gene deletion of the snodprot1 homolog, MSP 1, in the rice blast fungus Magnaporthe grisea . msp 1 mutants were phenotypically indistinguishable from wild type and elaborated apparently normal appressoria. However, the deletion mutants were greatly reduced in virulence primarily due to impaired growth in planta . Western blot analysis showed that the protein was secreted and not associated with the fungal cell wall. When purified MSP1 protein was applied to wounded leaf tissue, no apparent phytotoxic effects were noted. This is the first report to the authors' knowledge that directly implicates a snodprot1 protein as a virulence factor.