Plant cell walls are a critical site where plants and pathogens continuously struggle for physiological domi-nance.Here we show that dynamic remodeling of pectin methylesterification of plant cell walls is a compo-nen...Plant cell walls are a critical site where plants and pathogens continuously struggle for physiological domi-nance.Here we show that dynamic remodeling of pectin methylesterification of plant cell walls is a compo-nent of the physiological and co-evolutionary struggles between hosts and pathogens.A pectin methyles-terase(PsPME1)secreted by Phytophthora sojae decreases the degree of pectin methylesterification,thus synergizing with an endo-polygalacturonase(PsPG1)to weaken plant cell walls.To counter PsPME1-mediated susceptibility,a plant-derived pectin methylesterase inhibitor protein,GmPMl1,protects pectin to maintain a high methylesterification status.GmPMl1 protects plant cell walls from enzymatic degrada-tion by inhibiting both soybean and P.sojae pectin methylesterases during infection.However,constitutive expression of GmPMl1 disrupted the trade-off between host growth and defense responses.We therefore used AlphaFold structure tools to design a modified form of GmPMI1(GmPMI1R)that specifically targets and inhibits pectin methylesterases secreted from pathogens but notfrom plants.Transient expression of GmPMi1R enhanced plant resistance to oomycete and fungal pathogens.In summary,our work highlights the biochemical modification of the cell wall as an important focal point in the physiological and co-evolutionary conflict between hosts and microbes,providing an important proof of concept that Al-driven structure-based tools can accelerate the development of new strategies for plant protection.展开更多
Plants secrete defense molecules into the extracellular space (the apoplast) to combat attacking microbes. However, the mechanisms by which successful pathogens subvert plant apoplastic immunity remain poorly understo...Plants secrete defense molecules into the extracellular space (the apoplast) to combat attacking microbes. However, the mechanisms by which successful pathogens subvert plant apoplastic immunity remain poorly understood. In this study, we show that PsAvh240, a membrane-localized effector of the soybean pathogen Phytophthora sojae, promotes P. sojae infection in soybean hairy roots. We found that PsAvh240 interacts with the soybean-resistant aspartic protease GmAP1 in planta and suppresses the secretion of GmAP1 into the apoplast. By solving its crystal structure we revealed that PsAvh240 contain six a helices and two WY motifs. The first two a helices of PsAvh240 are responsible for its plasma membrane-localization and are required for PsAvh240's interaction with GmAP1. The second WY motifs of two PsAvh240 molecules form a handshake arrangement resulting in a handshake-like dimer. This dimerization is required for the effector's repression of GmAP1 secretion. Taken together, these data reveal that PsAvh240 localizes at the plasma membrane to interfere with GmAP1 secretion, which represents an effective mechanism by which effector proteins suppress plant apoplastic immunity.展开更多
基金supported bythe National Key Research and Development Program of China(2022YFF1001500)the National Natural Science Foundation of China(32102172)and(31721004)+1 种基金the China National Postdoctoral Program for Innovative Talents(BX2021130)the China Postdoctoral Science Foundation(2021M700074).
文摘Plant cell walls are a critical site where plants and pathogens continuously struggle for physiological domi-nance.Here we show that dynamic remodeling of pectin methylesterification of plant cell walls is a compo-nent of the physiological and co-evolutionary struggles between hosts and pathogens.A pectin methyles-terase(PsPME1)secreted by Phytophthora sojae decreases the degree of pectin methylesterification,thus synergizing with an endo-polygalacturonase(PsPG1)to weaken plant cell walls.To counter PsPME1-mediated susceptibility,a plant-derived pectin methylesterase inhibitor protein,GmPMl1,protects pectin to maintain a high methylesterification status.GmPMl1 protects plant cell walls from enzymatic degrada-tion by inhibiting both soybean and P.sojae pectin methylesterases during infection.However,constitutive expression of GmPMl1 disrupted the trade-off between host growth and defense responses.We therefore used AlphaFold structure tools to design a modified form of GmPMI1(GmPMI1R)that specifically targets and inhibits pectin methylesterases secreted from pathogens but notfrom plants.Transient expression of GmPMi1R enhanced plant resistance to oomycete and fungal pathogens.In summary,our work highlights the biochemical modification of the cell wall as an important focal point in the physiological and co-evolutionary conflict between hosts and microbes,providing an important proof of concept that Al-driven structure-based tools can accelerate the development of new strategies for plant protection.
基金supported by grants to Yuanchao Wang from the China National Funds for Innovative Research Groups(31721004)the key program of the National Natural Science Foundation of China(31430073)+2 种基金the Chinese Modern Agricultural Industry Technology System(CARS-004-PS14)the National Key R&D Program of China(SQ2018YFD020042)Research in the W.X.laboratory is supported by the Chinese Thousand Talents Plan and the Chinese Academy of Sciences.B.G.is supported by the Postgraduate Research&Practice Innovation Program of Jiangsu Province(KYCX18.0662).
文摘Plants secrete defense molecules into the extracellular space (the apoplast) to combat attacking microbes. However, the mechanisms by which successful pathogens subvert plant apoplastic immunity remain poorly understood. In this study, we show that PsAvh240, a membrane-localized effector of the soybean pathogen Phytophthora sojae, promotes P. sojae infection in soybean hairy roots. We found that PsAvh240 interacts with the soybean-resistant aspartic protease GmAP1 in planta and suppresses the secretion of GmAP1 into the apoplast. By solving its crystal structure we revealed that PsAvh240 contain six a helices and two WY motifs. The first two a helices of PsAvh240 are responsible for its plasma membrane-localization and are required for PsAvh240's interaction with GmAP1. The second WY motifs of two PsAvh240 molecules form a handshake arrangement resulting in a handshake-like dimer. This dimerization is required for the effector's repression of GmAP1 secretion. Taken together, these data reveal that PsAvh240 localizes at the plasma membrane to interfere with GmAP1 secretion, which represents an effective mechanism by which effector proteins suppress plant apoplastic immunity.
