Location: Wheat, Sorghum and Forage ResearchTitle: Wheat streak mosaic virus coat protein is a determinant for vector transmission by the wheat curl mite
|Tatineni, Satyanarayana - Ts|
|MCMECHAN, ANTHONY - University Of Nebraska|
|HEIN, GARY - University Of Nebraska|
Submitted to: Virology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 10/19/2017
Publication Date: 11/10/2017
Publication URL: https://handle.nal.usda.gov/10113/5863771
Citation: Tatineni, S., McMechan, A.J., Hein, G.L. 2017. Wheat streak mosaic virus coat protein is a determinant for vector transmission by the wheat curl mite. Virology. 514:42-49. https://doi.org/10.1016/j.virol.2017.10.018.
Interpretive Summary: Wheat streak mosaic virus (WSMV) is the causal agent of the most economically important wheat viral disease in the Great Plains region of the USA. WSMV is transmitted by wheat curl mites in growers’ fields. Control of WSMV spread by blocking wheat curl mite transmission provides eco-friendly management of the mosaic disease. Successful interactions between viral and vector proteins are required for effective transmission of viruses by insect vectors. Hence, vector transmission of plant viruses can be prevented by disrupting these interactions. Identification of viral genes involved in vector transmission is a prerequisite to examining interactions between viral and vector proteins. In this study, the coat protein of WSMV was identified as a determinant for wheat curl mite transmission. These results will facilitate identification of mite proteins involved in interactions with WSMV coat protein, followed by disruption of these interactions by silencing mite genes through RNA-interference technology in transgenic wheat.
Technical Abstract: Wheat streak mosaic virus (WSMV; genus Tritimovirus; family Potyviridae), is transmitted by the wheat curl mite (Aceria tosichella Keifer). The requirement of coat protein (CP) for WSMV transmission by the wheat curl mite was examined using a series of viable deletion and point mutations. Mite transmission of WSMV was completely abolished with deletions comprising CP amino acids 58–100. In contrast, the amino-proximal (amino acids 6–27 and 36–57) and carboxy-terminal (14 amino acids) regions of CP were expendable for mite transmission. Mutation of aspartic acid residues at amino acid positions 289 or 326 (D289A or D326A) at the carboxy-proximal region of CP significantly reduced mite transmission. Remarkably, every wheat plant infected by mutants D289A or D326A through mite transmission but not with in vitro transcripts contained a second-site mutation of R131C and N275H, respectively. Collectively, these data demonstrate for the first time that CP is a determinant for an eriophyid-transmitted plant virus.