Abstract
p2 of rice stripe virus may translocate from the nucleus to the cytoplasm and recruit nucleolar functions to promote virus systemic movement. Cajal bodies (CBs) are nuclear components associated with the nucleolus, which play a major role in plant virus infection. Coilin, a marker protein of CBs, is essential for CB formation and function. Coilin contains three domains, the N-terminal, the center, and the C-terminal fragments. Using yeast two-hybrid, colocalization, and bimolecular fluorescence complementation (BiFC) approaches, we show that p2 interacts with the full-length of Arabidopsis thaliana coilin (Atcoilin), the center and C-terminal domain of Atcoilin in the nucleus. Moreover, the N-terminal is indispensable for Atcoilin to interact with Cajal bodies.
Highlights
Plant viruses invade plants by infecting host cell to complete replication
Coilin has low homology in amino acid sequences in different species, but coilin of different organisms demonstrate a high level of structural similarity, such that their functionalities may be localized into three main domains, the N-terminal, the center, and C- terminal regions; the N- and Cterminal are conserved [21, 22]
The results show that p2 of Rice stripe virus (RSV) binds with the full-length of Atcoilin in the nucleus, targeting to the nucleoli and Cajal bodies (Figure 3(a))
Summary
Plant viruses invade plants by infecting host cell to complete replication. The replicated viruses infect more cells to cause virus diseases. Coilin serves to increase virus pathogenicity; Groundnut rosette virus (GRV) ORF3 protein hijacks CBs as vehicles to enter the nucleolus in virus systemic infection [4, 5]; herpes simplex virus 1 and adenoviruses relocalize coilin and other CB components around viral replication centers [2]. Fibrillarin is a major nucleolus protein, localized in nucleolus and CBs; CBs are often physically and functionally associated with the nucleolus to play a significant role in modulating some virus infections [1, 2], for example, GRV finished its systemic infection via a mechanism involving the reorganization of CBs and their fusion with the nucleolus [4]. The results indicated that p2 interacts with the full-length Atcoilin, the center and C-terminal domains of Atcoilin in the nucleus, but not interacts with the N-terminal domain
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