A redundant chloroplast protein is co-opted by potyvirids as the scaffold protein to mediate viral intercellular movement complex assembly

Abstract

For viruses in the family Potyviridae (potyvirids), three virus-encoded proteins (P3N-PIPO, CI and CP) and several host components are known to coordinately regulate viral cell-to-cell movement. Here, we found that HCPro2 encoded by areca palm necrotic ring spot virus is involved in the intercellular movement, which could be functionally complemented by its counterpart HCPro from a potyvirus. The affinity purification and mass spectrum analysis identified several viral factors (including CI and CP) and a variety of host proteins that physically associate with HCPro2. We demonstrated that HCPro2 interacts with either CI or CP in planta, and the three form plasmodesmata (PD)-localized interactive complex in viral infection. Further, we screened HCPro2-associating host proteins, and identified a common host protein RbCS that mediates the interactions of HCPro2-CI, HCPro2-CP and CI-CP among the complex. Knockdown of NbRbCS simultaneously impairs the interactions of HCPro2-CI, HCPro2-CP and CI-CP, and significantly attenuates the intercellular movement and systemic infection for ANRSV and other three tested potyvirids. This study highlights that a nucleus-encoded chloroplast-targeted protein is hijacked by potyvirids as the scaffold protein to mediate the assembly of viral intercellular movement complex to promote viral infection.