Formation of complexes at plasmodesmata for potyvirus intercellular movement is mediated by the viral protein P3N-PIPO.
Intercellular transport of viruses through cytoplasmic connections, termed plasmodesmata (PD), is essential for systemic infection in plants by viruses. Previous genetic and ultrastructural data revealed that the potyvirus cyclindrical inclusion (CI) protein is directly involved in cell-to-cell movement, likely through the formation of conical structures anchored to and extended through PD. In this study, we demonstrate that plasmodesmatal localization of CI in N. benthamiana leaf cells is modulated by the recently discovered potyviral protein, P3N-PIPO, in a CI:P3N-PIPO ratio-dependent manner. We show that P3N-PIPO is a PD-located protein that physically interacts with CI in planta. The early secretory pathway, rather than the actomyosin motility system, is required for the delivery of P3N-PIPO and CI to PD. Moreover, CI mutations that disrupt virus cell-to-cell movement compromise PD-localization capacity. These data suggest that the CI and P3N-PIPO complex coordinates the formation of PD-associated structures that facilitate the intercellular movement of potyviruses in infected plants.
Wei
Taiyun
T
Southern Crop Protection and Food Research Centre, Agriculture and Agri-Food Canada, London, Ontario, Canada.
Zhang
Changwei
C
Hong
Jian
J
Xiong
Ruyi
R
Kasschau
Kristin D
KD
Zhou
Xueping
X
Carrington
James C
JC
Wang
Aiming
A
D000205:Actomyosin / Q000378:metabolism; D002450:Cell Communication; D002465:Cell Movement; D004279:DNA, Viral / Q000235:genetics; D031425:Plasmodesmata / Q000502:physiology*; D017800:Potyvirus / Q000302:isolation & purification / Q000502:physiology*; D012231:Rhizobium / Q000235:genetics; D014026:Nicotiana / Q000821:virology*; D019562:Viral Load; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D014779:Virus Replication
D004279:DNA, Viral; D014764:Viral Proteins; D000205:Actomyosin