The Bursaphelenchus xylophilus effector BxML1 targets the cyclophilin protein (CyP) to promote parasitism and virulence in pine
Abstract Background Bursaphelenchus xylophilus is the causal agent of pine wilt disease (PWD) that has caused enormous ecological and economic losses in China. The mechanism in the interaction between nematodes and pine remains unclear. Plant parasitic nematodes (PPNs) secrete effectors into host pl...
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BMC
2022-04-01
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Series: | BMC Plant Biology |
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Online Access: | https://doi.org/10.1186/s12870-022-03567-z |
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author | Yan Zhang Tong-Yue Wen Xiao-Qin Wu Long-Jiao Hu Yi-Jun Qiu Lin Rui |
author_facet | Yan Zhang Tong-Yue Wen Xiao-Qin Wu Long-Jiao Hu Yi-Jun Qiu Lin Rui |
author_sort | Yan Zhang |
collection | DOAJ |
description | Abstract Background Bursaphelenchus xylophilus is the causal agent of pine wilt disease (PWD) that has caused enormous ecological and economic losses in China. The mechanism in the interaction between nematodes and pine remains unclear. Plant parasitic nematodes (PPNs) secrete effectors into host plant tissues. However, it is poorly studied that role of effector in the infection of pine wood nematode (PWN). Results We cloned, characterized and functionally validated the B. xylophilus effector BxML1, containing an MD-2-related lipid-recognition (ML) domain. This protein inhibits immune responses triggered by the molecular pattern BxCDP1 of B. xylophilus. An insitu hybridization assay demonstrated that BxML1 was expressed mainly in the dorsal glands and intestine of B. xylophilus. Subcellular localization analysis showed the presence of BxML1 in the cytoplasm and nucleus. Furthermore, number of B. xylophilus and morbidity of pine were significantly reduced in Pinus thunbergii infected with B. xylophilus when BxML was silenced. Using yeast two-hybrid (Y2H) and coimmunoprecipitation (CoIP) assays, we found that the BxML1 interacts with cyclophilin protein PtCyP1 in P. thunbergii. Conclusions This study illustrated that BxML1 plays a critical role in the B. xylophilus–plant interaction and virulence of B. xylophilus. |
first_indexed | 2024-04-14T06:42:43Z |
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issn | 1471-2229 |
language | English |
last_indexed | 2024-04-14T06:42:43Z |
publishDate | 2022-04-01 |
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series | BMC Plant Biology |
spelling | doaj.art-3b13519f791e4f6ab1bc1bfabc27dd0c2022-12-22T02:07:17ZengBMCBMC Plant Biology1471-22292022-04-0122111310.1186/s12870-022-03567-zThe Bursaphelenchus xylophilus effector BxML1 targets the cyclophilin protein (CyP) to promote parasitism and virulence in pineYan Zhang0Tong-Yue Wen1Xiao-Qin Wu2Long-Jiao Hu3Yi-Jun Qiu4Lin Rui5Co-Innovation Center for Sustainable Forestry in Southern China, College of Forestry, Nanjing Forestry UniversityCo-Innovation Center for Sustainable Forestry in Southern China, College of Forestry, Nanjing Forestry UniversityCo-Innovation Center for Sustainable Forestry in Southern China, College of Forestry, Nanjing Forestry UniversityCo-Innovation Center for Sustainable Forestry in Southern China, College of Forestry, Nanjing Forestry UniversityCo-Innovation Center for Sustainable Forestry in Southern China, College of Forestry, Nanjing Forestry UniversityCo-Innovation Center for Sustainable Forestry in Southern China, College of Forestry, Nanjing Forestry UniversityAbstract Background Bursaphelenchus xylophilus is the causal agent of pine wilt disease (PWD) that has caused enormous ecological and economic losses in China. The mechanism in the interaction between nematodes and pine remains unclear. Plant parasitic nematodes (PPNs) secrete effectors into host plant tissues. However, it is poorly studied that role of effector in the infection of pine wood nematode (PWN). Results We cloned, characterized and functionally validated the B. xylophilus effector BxML1, containing an MD-2-related lipid-recognition (ML) domain. This protein inhibits immune responses triggered by the molecular pattern BxCDP1 of B. xylophilus. An insitu hybridization assay demonstrated that BxML1 was expressed mainly in the dorsal glands and intestine of B. xylophilus. Subcellular localization analysis showed the presence of BxML1 in the cytoplasm and nucleus. Furthermore, number of B. xylophilus and morbidity of pine were significantly reduced in Pinus thunbergii infected with B. xylophilus when BxML was silenced. Using yeast two-hybrid (Y2H) and coimmunoprecipitation (CoIP) assays, we found that the BxML1 interacts with cyclophilin protein PtCyP1 in P. thunbergii. Conclusions This study illustrated that BxML1 plays a critical role in the B. xylophilus–plant interaction and virulence of B. xylophilus.https://doi.org/10.1186/s12870-022-03567-zBursaphelenchus xylophilusEffectorMD-2-related lipid-recognition domain proteinCyclophilin proteinPinus thunbergii |
spellingShingle | Yan Zhang Tong-Yue Wen Xiao-Qin Wu Long-Jiao Hu Yi-Jun Qiu Lin Rui The Bursaphelenchus xylophilus effector BxML1 targets the cyclophilin protein (CyP) to promote parasitism and virulence in pine BMC Plant Biology Bursaphelenchus xylophilus Effector MD-2-related lipid-recognition domain protein Cyclophilin protein Pinus thunbergii |
title | The Bursaphelenchus xylophilus effector BxML1 targets the cyclophilin protein (CyP) to promote parasitism and virulence in pine |
title_full | The Bursaphelenchus xylophilus effector BxML1 targets the cyclophilin protein (CyP) to promote parasitism and virulence in pine |
title_fullStr | The Bursaphelenchus xylophilus effector BxML1 targets the cyclophilin protein (CyP) to promote parasitism and virulence in pine |
title_full_unstemmed | The Bursaphelenchus xylophilus effector BxML1 targets the cyclophilin protein (CyP) to promote parasitism and virulence in pine |
title_short | The Bursaphelenchus xylophilus effector BxML1 targets the cyclophilin protein (CyP) to promote parasitism and virulence in pine |
title_sort | bursaphelenchus xylophilus effector bxml1 targets the cyclophilin protein cyp to promote parasitism and virulence in pine |
topic | Bursaphelenchus xylophilus Effector MD-2-related lipid-recognition domain protein Cyclophilin protein Pinus thunbergii |
url | https://doi.org/10.1186/s12870-022-03567-z |
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