Remorins are plant-specific membrane-associated proteins and were proposed to play crucial roles in plant-pathogen interactions.However,little is known about how pathogens counter remorin-mediated host responses.In this study,by quantitative whole-proteome analysis we found that the remorin protein (NbREM1) is downregulated early in Rice stripe virus (RSV) infection.We further discovered that the tuover of NbREM1 is regulated by S-acylation modification and its degradation is mediated mainly through the autophagy pathway.Interestingly,RSV can interfere with the S-acylation of NbREM1,which is required to negatively regulate RSV infection by restricting virus cell-to-cell trafficking.The disruption of NbREM1 S-acylation affects its targeting to the plasma membrane microdomain,and the resulting accumulation of non-targeted NbREM1 is subjected to autophagic degradation,causing downregulation of NbREM1.Moreover,we found that RSV-encoded movement protein,NSvc4,alone can interfere with NbREM1 S-acylation through binding with the C-terminal domain of NbREM1 the S-acylation of OsREM1.4,the homologous remorin of NbREM1,and thus remorin-mediated defense against RSV in rice,the original host of RSV,indicating that downregulation of the remorin protein level by interfering with its S-acylation is a common strategy adopted by RSV to overcome remorin-mediated inhibition of virus movement.