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The bipartite begomoviruses (Geminiviridae family),which are DNA viruses that replicate in the nucleus of infected cells,encode the nuclear shuttle protein (NSP) to facilitate the translocation of viral DNA from the nucleus to the cytoplasm via nuclear pores.This intracellular trafficking of NSP-DNA complexes is accessorized by the NSP-interacting guanosine triphosphatase (NIG) at the cytosolic side.Here,we report the nuclear redistribution of NIG by AtWWP1,a WW domain-containing protein that forms immune nuclear bodies (NBs) against begomoviruses.We demonstrated that AtWWP1 relocates NIG from the cytoplasm to the nucleus where it is confined to AtWWP1-NBs,suggesting that the NIG-AtWWP1 interaction may interfere with the NIG pro-viral function associated with its cytosolic localization.Consistent with this assumption,loss of AtWWP1 function cuased plants more susceptible to begomovirus infection,whereas overexpression of AtWWP1 enhanced plant resistance to begomovirus.Furthermore,we found that a mutant version of AtWWP1 defective for NB formation was no longer capable of interacting with and relocating NIG to the nucleus and lost its immune function against begomovirus.The antiviral function of AtWWP1-NBs,however,could be antagonized by viral infection that induced either the disruption or a decrease in the number of AtWWP1-NBs.Collectively,these results led us to propose that AtWWP1 organizes nuclear structures into nuclear foci,which provide intrinsic immunity against begomovirus infection.