Abstract
Most plant reoviruses encode a type of nonstructural protein that assembles tubular structures to package virions for viral spread in planthopper or leafhopper vectors. These tubules are propelled by actin filaments and facilitate viruses to overcome transmission barriers in insect vectors. This is known as actin-based tubule motility (ABTM), in which insect proteins, especially actin-associated proteins participate. To better understand the insect components that play a role in the ABTM, the proteins interacting with tubule protein Pns11 of the Rice gall dwarf virus (RGDV) in the leafhopper vector were investigated. We found that gelsolin, an actin-modulating protein, interacted with Pns11 in the yeast-two-hybrid system and Sf9 cells. The interaction and co-localization of gelsolin and Pns11 were also verified in cultured cells and insect bodies of the leafhopper vector. Further, the expression of gelsolin was up-regulated by the RGDV infection both in cultured cells and insects. The knockdown of the gelsolin gene triggered by RNA interference increased viral accumulation, thus increasing the viruliferous rates of the leafhopper vector. This negative association of gelsolin with Pns11 and virus infection revealed that gelsolin negatively affected the ability of the virus to spread by interacting with Pns11 tubules, finally acting to negatively regulate RGDV infection. The results of this study indicate that ABTM is negatively regulated by insects in the coevolution of the insect vector and virus.
Highlights
Plant reoviruses are transmitted by planthopper or leafhopper vectors in a persistent propagative manner (Attoui et al 2012)
We investigated the molecular mechanisms for actin-based tubule motility (ABTM) of Rice gall dwarf virus (RGDV), by combining the yeast two-hybrid assay (Y2H), baculovirus expression system, immunofluorescence assay, and RNA interference (RNAi) technique based on the cultured cells and insect bodies
Pns11 interacts with gelsolin in vitro Because the Pns11 tubule is transmembrane and highly hydrophobic, a membrane protein-specific Yeast two-hybrid assay (Y2H) system, the DUALmembrane system, was utilized to screen the proteins of N. cincticeps interacting with RGDV Pns11
Summary
Plant reoviruses are transmitted by planthopper or leafhopper vectors in a persistent propagative manner (Attoui et al 2012). For the persistent propagative transmission, these viruses exploit actin-based tubule motility (ABTM) to overcome the transmission barriers in insect vectors. In cultured cells derived from insect vectors, these tubules, propelled by actin filaments in filopodia, protrude from the cellular surface, and penetrate neighboring uninfected cells for persistent viral infection (Wei et al 2006; Chen et al 2012; Chen et al 2013; Jia et al 2014; Wei and Li 2016). In. ABTM is mainly conducted by virus-encoded tubular proteins and the actin filament engine. To understand the mechanism of this process, it is essential to investigate the interaction of actin or actin-associated proteins with tubular proteins; it is necessary to study the regulation mechanism of actin in response to viral infection. Previous studies have shown that the specific interaction of these tubular proteins, including RDV (2019) 1:19
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