Structural highlights
Publication Abstract from PubMedPlants secrete defence molecules into the extracellular space (the apoplast) to combat attacking microbes. Thus far, the mechanisms by which successful pathogens subvert plant apoplastic immunity remain poorly known. In this study, we show that PsAvh240, a membrane-localised effector of the soybean pathogen Phytophthora sojae, promote P. sojae infection in the soybean hairy roots. PsAvh240 interacts with a soybean resistant aspartic protease GmAP1 in planta and suppresses the secretion of GmAP1 to the apoplast. The crystal structure reveals that PsAvh240 comprises six alpha-helices and two WY motifs. The first two alpha-helices of PsAvh240 are responsible for plasma membrane localisation of the effector, which are required for PsAvh240 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 revealed that PsAvh240 localises at the plasma membrane to interfere with GmAP1 secretion, which presents an effective mechanism by which effector proteins suppress plant apoplastic immunity. Phytophthora sojae effector PsAvh240 inhibits a host aspartic protease secretion to promote infection.,Guo B, Wang H, Yang B, Jiang W, Jing M, Li H, Xia Y, Xu Y, Hu Q, Wang F, Yu F, Wang Y, Ye W, Dong S, Xing W, Wang Y Mol Plant. 2019 Jan 28. pii: S1674-2052(19)30023-1. doi:, 10.1016/j.molp.2019.01.017. PMID:30703565[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 10:30, 18 March 2021.