Abstract
The spread of Tomato yellow leaf curl virus (TYLCV) was accompanied by the formation of coat protein (CP) aggregates of increasing size in the cytoplasm and nucleus of infected tomato (Solanum lycopersicum) cells. In order to better understand the TYLCV-host interaction, we investigated the properties and the subcellular accumulation pattern of the non-structural viral protein V2. CP and V2 are the only sense-oriented genes on the virus circular single-stranded DNA genome. Similar to CP, V2 localized to cytoplasmic aggregates of increasing size and as infection progressed was also found in nuclei, where it co-localized with CP. V2 was associated with viral genomic DNA molecules, suggesting that V2 functions as a DNA shuttling protein. The formation and the 26S proteasome-mediated degradation of V2 aggregates were dependent on the integrity of the actin and microtubule cytoskeleton. We propose that the cytoskeleton-dependent formation and growth of V2 aggregates play an important role during TYLCV infection, and that microtubules and actin filaments are important for the delivery of V2 to the 26S proteasome.
Highlights
Many plant and animal viruses induce the formation of insoluble aggregates/inclusion bodies inside infected cells
TGBp3 is recruited to these vesicles[8] and these complexes are later found in a large perinuclear aggregate named X-body, which serves as a viral replication site similar to animal VFs9
Actin filaments and associated myosin motor proteins are important for Tobacco mosaic virus (TMV) and facilitate the transport of the viral MP and MP-containing viral replication complexes (VRCs) along the endoplasmic reticulum (ER) to the plasmodesmata (PD)[3,4,6]
Summary
Many plant and animal viruses induce the formation of insoluble aggregates/inclusion bodies inside infected cells. These structures usually contain viral and host proteins, and can vary in location, size, content and biological function[1,2]. The formation of virus-induced structures inside the infected cell, such as replication complexes, viral factories (VFs), and inclusion bodies, often depends on trafficking of host and viral proteins along the cytoskeleton. These structures can recruit host components associated with defenses against infection and cell stress. Inhibition of the proteasome in sink leaves leads to the formation of a single large aggregate per cell, resembling the mammalian aggresome[14]
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