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Plumeria pudica, known as bridal bouquet, exhibiting characteristic symptoms of orthotospovirus infection were found in different localities in Brazil. Symptoms were restricted to leaves of the middle and lower thirds of a few branches of each plant. Electron microscopy, molecular analyses, and complete genome sequencing identified the orthotospovirus as groundnut ringspot virus (GRSV),member of the species Orthotospovirus arachianuli. The virus was poorly transmitted mechanically to P. pudica. Reverse transcription polymerase chain reaction (RT-PCR) and reverse transcription quantitative polymerase chain reaction (RT-qPCR) analyses performed using total RNA extracted from leaf blades, primary veins, petioles, and regions of petiole insertion on branches indicated the presence of GRSV, predominantly in the symptomatic leaf blades. Symptomatic branches propagate vegetatively, often resulting in plants expressing GRSV symptoms. In contrast, vegetative propagation of the asymptomatic branches of infected plants predominantly generates plants without GRSV symptoms. The resistance of P. pudica plants to GRSV infection, restricted systemic viral movement, and expression of symptoms in infected plants suggest that this orthotospovirus does not threaten this ornamental plant. [ABSTRACT FROM AUTHOR]

The movement of some plant RNA viruses is mediated by triple gene block (TGB) proteins, which cooperate to transfer the viral genome from cell to cell through plasmodesmata. Here, we investigated the function of the TGB proteins of cowpea mild mottle virus (CPMMV; genus Carlavirus , family Betaflexiviridae), which causes severe damage to soybean production. Subcellular localization experiments demonstrated that TGBp1 and TGBp3 were localized to the endoplasmic reticulum (ER), plasmodesmata (PD) and nucleus in Nicotiana benthamiana leaves. TGBp2 was unusually localized to PD. In protein interaction assays TGBp2 significantly enhanced the interaction between TGBp3 and TGBp1. Interaction assays using deletion mutants showed that the C-terminal transmembrane (TM) domain of TGBp2 is critical for its localization to PD and for its interaction with TGBp1 and TGBp3. [ABSTRACT FROM AUTHOR]