Phytopathogens secrete effectors to promote colonization of their host plants.These effectors modulate host immune responses by interfering with various pathways,but little is known about their biochemical activities....Phytopathogens secrete effectors to promote colonization of their host plants.These effectors modulate host immune responses by interfering with various pathways,but little is known about their biochemical activities.Several recent reports indicate that some phytopathogen effectors have Nudix hydrolase activity,including Avr3b from Phytophthora sojae(Dong et al.,2011),AvrM14 from Melampsora lini (McCombe et al.,2023),and RipN from Ralstonia solanacearum (Sun et al.,2019).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 by grants from the National Key Research and Development Program of China (2022YFF1001500)National Natural Science Foundation of China (31721004, 32202261)Natural Science Foundation of Jiangsu Province (BK20210156)。
文摘Phytopathogens secrete effectors to promote colonization of their host plants.These effectors modulate host immune responses by interfering with various pathways,but little is known about their biochemical activities.Several recent reports indicate that some phytopathogen effectors have Nudix hydrolase activity,including Avr3b from Phytophthora sojae(Dong et al.,2011),AvrM14 from Melampsora lini (McCombe et al.,2023),and RipN from Ralstonia solanacearum (Sun et al.,2019).
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.
