Abstract
BackgroundGPI-anchoring is a prevalent Glycosylphosphatidylinositol modification process of posttranslational protein and is necessary for cell wall integrity in eukaryotes. To date, the function of GPI anchored-related protein remains unknown in phytopathogenic fungi.ResultsWe here characterized the functions of MoPer1, a homolog of Saccharomyces cerevisiae ScPer1, from the rice blast fungus Magnaporthe oryzae. Transcriptional analysis demonstrated that MoPER1 was significantly upregulated during conidiation and infection. We found that the ∆Moper1 mutant was defective in conidiation and appressoria formation, and MoPer1 was involved in osmotic stress response and maintaining the cell wall integrity. Pathogenicity assays indicated that deletion of MoPEP1 significant reduction in virulence. Microscopic examination of the lesions revealed that the invasive hyphae of ∆Moper1 mutants were mostly restricted to the primary infected leaf sheath cells.ConclusionsOur results indicated that MoPer1 is necessary for growth, conidiogenesis, and pathogenicity of the fungus. Our study facilitated to deep elucidate the pathogenic molecular mechanism of M. oryzae, and also provided a very helpful reference value for developing effective fungicide pointed at as the gene for target.
Highlights
The fungal cell wall play important roles in maintaining cell integrity during polarized growth (Klis et al, 2002)
Transformants carrying the MoPER1 gene exhibited better growth on medium containing 20 μg/ml calcofluor white (CFW) compared to the ΔScper1 mutant, and was similar to wild type BY4741 strain (Additional file 1: Figure S1), suggesting that MoPer1 is a functional paralog of ScPer1
The phase-specific expression of MoPER1 was quantified by quantitative real-time polymerase chain reaction, with the synthesis of cDNA from each sample including infectious growth, vegetative growth and conidia
Summary
The fungal cell wall play important roles in maintaining cell integrity during polarized growth (Klis et al, 2002). Part of the cell wall protein must be anchored by glycosylphosphatidylinositol (GPI) after translated, and bound to the cell wall to perform its normal biological function (Bernard and Latge, 2001; Bowman and Free, 2006; Free, 2013). Deletion of the BST1 gene delays the formation of GPI-anchored proteins (Tanaka et al, 2004; Fujita et al, 2006b). Biological function of the Per is similar to Bst, which is necessary for the maturation of GPI-anchored proteins and loss of these two genes caused defects to the integrity of cell wall. GPI-anchoring is a prevalent Glycosylphosphatidylinositol modification process of posttranslational protein and is necessary for cell wall integrity in eukaryotes. The function of GPI anchored-related protein remains unknown in phytopathogenic fungi
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