Proteomics Analysis Reveals the Molecular Mechanism of MoPer1 Regulating the Development and Pathogenicity of Magnaporthe oryzae
Glycosylphosphatidylinositol (GPI) anchoring the protein GPI modification post-transcriptionally is commonly seen. In our previous study, MoPer1, a GPI anchoring essential factor, has a critical effect on Magnaporthe oryzae growth, pathogenicity, and conidiogenesis, but its molecular mechanism is n...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2022-06-01
|
| Series: | Frontiers in Cellular and Infection Microbiology |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/fcimb.2022.926771/full |
| _version_ | 1811333890966552576 |
|---|---|
| author | Yue Chen Yue Chen Xiyang Wu Xiyang Wu Chunyan Chen Qiang Huang Chenggang Li Xin Zhang Xinqiu Tan Xinqiu Tan Deyong Zhang Deyong Zhang Yong Liu Yong Liu |
| author_facet | Yue Chen Yue Chen Xiyang Wu Xiyang Wu Chunyan Chen Qiang Huang Chenggang Li Xin Zhang Xinqiu Tan Xinqiu Tan Deyong Zhang Deyong Zhang Yong Liu Yong Liu |
| author_sort | Yue Chen |
| collection | DOAJ |
| description | Glycosylphosphatidylinositol (GPI) anchoring the protein GPI modification post-transcriptionally is commonly seen. In our previous study, MoPer1, a GPI anchoring essential factor, has a critical effect on Magnaporthe oryzae growth, pathogenicity, and conidiogenesis, but its molecular mechanism is not clear. Here, we extracted the glycoproteins from the ΔMoper1 mutant and wild-type Guy11 to analyze their differential levels by quantitative proteomic analysis of TMT markers. After background subtraction, a total of 431 proteins, with significant changes in expression, were successfully identified, and these differential proteins were involved in biological regulation, as well as cellular process and metabolic process, binding, catalytic activity, and other aspects. Moreover, we found that MoPer1 regulates the expression of 14 proteins involved in growth, development, and pathogenicity of M. oryzae. The above findings shed light on MoPer1’s underlying mechanism in regulating growth, development, and pathogenicity of M. oryzae. |
| first_indexed | 2024-04-13T16:59:37Z |
| format | Article |
| id | doaj.art-80f06910db4d4148a63a8238d2856697 |
| institution | Directory Open Access Journal |
| issn | 2235-2988 |
| language | English |
| last_indexed | 2024-04-13T16:59:37Z |
| publishDate | 2022-06-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cellular and Infection Microbiology |
| spelling | doaj.art-80f06910db4d4148a63a8238d28566972022-12-22T02:38:43ZengFrontiers Media S.A.Frontiers in Cellular and Infection Microbiology2235-29882022-06-011210.3389/fcimb.2022.926771926771Proteomics Analysis Reveals the Molecular Mechanism of MoPer1 Regulating the Development and Pathogenicity of Magnaporthe oryzaeYue Chen0Yue Chen1Xiyang Wu2Xiyang Wu3Chunyan Chen4Qiang Huang5Chenggang Li6Xin Zhang7Xinqiu Tan8Xinqiu Tan9Deyong Zhang10Deyong Zhang11Yong Liu12Yong Liu13State Key Laboratory of Hybrid Rice and Institute of Plant Protection, Hunan Academy of Agricultural Sciences, Changsha, ChinaLong Ping Branch, Graduate School of Hunan University, Changsha, ChinaState Key Laboratory of Hybrid Rice and Institute of Plant Protection, Hunan Academy of Agricultural Sciences, Changsha, ChinaLong Ping Branch, Graduate School of Hunan University, Changsha, ChinaCollege of Plant Protection, Hunan Agricultural University, Changsha, ChinaCollege of Plant Protection, Hunan Agricultural University, Changsha, ChinaState Key Laboratory of Hybrid Rice and Institute of Plant Protection, Hunan Academy of Agricultural Sciences, Changsha, ChinaState Key Laboratory of Hybrid Rice and Institute of Plant Protection, Hunan Academy of Agricultural Sciences, Changsha, ChinaState Key Laboratory of Hybrid Rice and Institute of Plant Protection, Hunan Academy of Agricultural Sciences, Changsha, ChinaLong Ping Branch, Graduate School of Hunan University, Changsha, ChinaState Key Laboratory of Hybrid Rice and Institute of Plant Protection, Hunan Academy of Agricultural Sciences, Changsha, ChinaLong Ping Branch, Graduate School of Hunan University, Changsha, ChinaState Key Laboratory of Hybrid Rice and Institute of Plant Protection, Hunan Academy of Agricultural Sciences, Changsha, ChinaLong Ping Branch, Graduate School of Hunan University, Changsha, ChinaGlycosylphosphatidylinositol (GPI) anchoring the protein GPI modification post-transcriptionally is commonly seen. In our previous study, MoPer1, a GPI anchoring essential factor, has a critical effect on Magnaporthe oryzae growth, pathogenicity, and conidiogenesis, but its molecular mechanism is not clear. Here, we extracted the glycoproteins from the ΔMoper1 mutant and wild-type Guy11 to analyze their differential levels by quantitative proteomic analysis of TMT markers. After background subtraction, a total of 431 proteins, with significant changes in expression, were successfully identified, and these differential proteins were involved in biological regulation, as well as cellular process and metabolic process, binding, catalytic activity, and other aspects. Moreover, we found that MoPer1 regulates the expression of 14 proteins involved in growth, development, and pathogenicity of M. oryzae. The above findings shed light on MoPer1’s underlying mechanism in regulating growth, development, and pathogenicity of M. oryzae.https://www.frontiersin.org/articles/10.3389/fcimb.2022.926771/fullMoPer1proteomicsdifferentially expressed proteinspathogenic proteinqRT-PCR validation |
| spellingShingle | Yue Chen Yue Chen Xiyang Wu Xiyang Wu Chunyan Chen Qiang Huang Chenggang Li Xin Zhang Xinqiu Tan Xinqiu Tan Deyong Zhang Deyong Zhang Yong Liu Yong Liu Proteomics Analysis Reveals the Molecular Mechanism of MoPer1 Regulating the Development and Pathogenicity of Magnaporthe oryzae Frontiers in Cellular and Infection Microbiology MoPer1 proteomics differentially expressed proteins pathogenic protein qRT-PCR validation |
| title | Proteomics Analysis Reveals the Molecular Mechanism of MoPer1 Regulating the Development and Pathogenicity of Magnaporthe oryzae |
| title_full | Proteomics Analysis Reveals the Molecular Mechanism of MoPer1 Regulating the Development and Pathogenicity of Magnaporthe oryzae |
| title_fullStr | Proteomics Analysis Reveals the Molecular Mechanism of MoPer1 Regulating the Development and Pathogenicity of Magnaporthe oryzae |
| title_full_unstemmed | Proteomics Analysis Reveals the Molecular Mechanism of MoPer1 Regulating the Development and Pathogenicity of Magnaporthe oryzae |
| title_short | Proteomics Analysis Reveals the Molecular Mechanism of MoPer1 Regulating the Development and Pathogenicity of Magnaporthe oryzae |
| title_sort | proteomics analysis reveals the molecular mechanism of moper1 regulating the development and pathogenicity of magnaporthe oryzae |
| topic | MoPer1 proteomics differentially expressed proteins pathogenic protein qRT-PCR validation |
| url | https://www.frontiersin.org/articles/10.3389/fcimb.2022.926771/full |
| work_keys_str_mv | AT yuechen proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT yuechen proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT xiyangwu proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT xiyangwu proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT chunyanchen proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT qianghuang proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT chenggangli proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT xinzhang proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT xinqiutan proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT xinqiutan proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT deyongzhang proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT deyongzhang proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT yongliu proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae AT yongliu proteomicsanalysisrevealsthemolecularmechanismofmoper1regulatingthedevelopmentandpathogenicityofmagnaportheoryzae |