Rice Stripe Virus Interferes with S-acylation of Remorin and Induces Its Autophagic Degradation to Facilitate Virus Infection

Remorins are plant-specific membrane-associated proteins, and were proposed to play crucial roles in plant-pathogen interactions. However, little is known about pathogens’ counter-response to remorin-mediated regulation. Here, we find the remorin protein (NbREM1) is down-regulated early in Rice stripe virus (RSV) infection by quantitative whole-proteome analysis. We demonstrate that the turnover of NbREM1 is regulated by the S-acylation modification and can enter the autophagy pathway for degradation. We further show that RSV can interfere with the S-acylation of NbREM1, that is required for negatively regulates RSV infection by restricting virus cell-to-cell trafficking. The interference of NbREM1 S-acylation affects the targeting of NbREM1 to the plasma membrane microdomain, and the resulting accumulation of non-targeted NbREM1 is subjected to the autophagic degradation, causing down-regulation of NbREM1. In addition, we find the RSV-encoded NSvc4 protein alone can interfere with NbREM1 S-acylation through binding with the C-terminal domain of NbREM1. Moreover, we reveal a same counter-response of NSvc4 to the homologous remorin (OsREM1.4) from Oryza sativa, the original host of RSV, indicating down-regulating remorin protein level by interfering its S-acylation is a common strategy that RSV has adopted to overcome remorin mediated inhibition of virus movement.