The N-mannosyltransferase MoAlg9 plays important roles in the development and pathogenicity of Magnaporthe oryzae
文献类型： 外文期刊
作者： Zhang, Shulin 1 ; Wang, Yu 1 ; Hu, Jinmei 1 ; Cui, Xinyue 1 ; Kang, Xiaoru 1 ; Zhao, Wei 3 ; Pan, Yuemin 1 ;
作者机构： 1.Anhui Agr Univ, Coll Plant Protect, Dept Plant Pathol, Hefei 230036, Peoples R China
2.Anhui Agr Univ, Anhui Prov Key Lab Crop Integrated Pest Management, Hefei 230036, Peoples R China
3.Anhui Acad Agr Sci, Inst Plant Protect & Agroprod Safety, Hefei 230031, Peoples R China
关键词： glycosylation; N-mannosyltransferase; Alg9; pathogenicity; rice blast; Magnaporthe oryzae
期刊名称：JOURNAL OF INTEGRATIVE AGRICULTURE （ 影响因子：4.4； 五年影响因子：4.8 ）
ISSN： 2095-3119
年卷期： 2025 年 24 卷 6 期
页码：
收录情况： SCI
摘要： Magnaporthe oryzae is the causal agent of rice blast. Glycosylation plays key roles in vegetative growth, development, and infection of M. oryzae. However, several glycosylation-related genes have not been characterized. In this study, we identified a Glyco_transf_22 domain-containing protein, MoAlg9, and found that MoAlg9 is localized to the endoplasmic reticulum (ER). Deletion of MoALG9 significantly affected conidial production, normal appressorium formation, responses to stressors, and pathogenicity of M. oryzae. We also found that the Delta Moalg9 mutant was defective in glycogen utilization, appressorial penetration, and invasive growth in host cells. Moreover, we further demonstrated that MoALG9 regulates the transcription of several target genes involved in conidiation, appressorium formation, and cell wall integrity. In addition, we found that the Glyco_transf_22 domain is essential for normal MoAlg9 function and localization. We also provide evidence that MoAlg9 is involved in N-glycosylation pathway in M. oryzae. Taken together, these results show that MoAlg9 is important for conidiation, appressorium formation, maintenance of cell wall integrity, and the pathogenesis of M. oryzae.
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