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ARS Home » Northeast Area » Ithaca, New York » Robert W. Holley Center for Agriculture & Health » Emerging Pests and Pathogens Research » Research » Publications at this Location » Publication #318563
Title: Proteomic analysis of interaction between a plant virus and its vector insect reveals new functions of hemipteran cuticular protein

Author
item LIU, WENWEN - Chinese Academy Of Agricultural Sciences
item Gray, Stewart
item HUO, YAN - Chinese Academy Of Sciences
item LI, LI - Chinese Academy Of Agricultural Sciences
item WEI, TAIYUN - Fujian Agricultural & Forestry University
item WANG, XIFENG - Chinese Academy Of Agricultural Sciences

Submitted to: Molecular and Cellular Proteomics
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 3/30/2015
Publication Date: 6/19/2015
Citation: Liu, W., Gray, S.M., Huo, Y., Li, L., Wei, T., Wang, X. 2015. Proteomic analysis of interaction between a plant virus and its vector insect reveals new functions of hemipteran cuticular protein. Molecular and Cellular Proteomics. 14(8):2229-2242.

Interpretive Summary: Most plant viruses are transmitted by insect vectors and there are very specific interactions between the insect and the virus that control the efficiency of transmission. While we understand which of the virus proteins are essential for transmission, we know very little about the insect proteins that interact with the virus and allow it to be spread between plant hosts. This study used molecular technologies that identify protein binding partners. In this case insect proteins that bind to the protein that forms the shell of the virus. Five insect proteins were identified that attach to the virus and are likely involved in moving the virus through various tissues of the insect. One insect protein, that is a component of the insect shell, but also is found in insect blood cells, appears to bind virus particles as they move through the insect blood on their way to the salivary glands. Binding virus to insect blood cells appears to facilitate the survival and movement of virus in the blood and prevent the insect immune system from attacking and destroying the virus. If the virus survives to enter the insect salivary glands it can be delivered into new plant hosts when the insect is feeding. Understanding how the virus evades the insect immune system and survives in the insect blood for extended times may provide specific targets to try and disrupt the virus-insect protein interactions and allow the virus to be targeted and destroyed by the insect immune system.

Technical Abstract: Numerous viruses can be transmitted by their corresponding vector insects; however, the molecular mechanisms enabling virus transmission by vector insects have been poorly understood, especially the identity of vector components interacting with the virus. Here, we used the yeast two hybrid system to study proteomic interactions of a plant virus (Rice stripe virus, RSV, genus Tenuivirus) with its vector insect, small brown planthopper (Laodelphax striatellus). Sixty-six proteins of L. striatellus that interacted with the nucleocapsid protein (pc3) of RSV were identified. A virus-insect interaction network, constructed for pc3 and 29 protein homologs of Drosophila melanogaster, suggested that 9 proteins might directly interact with pc3. Of the 66 proteins, five (atlasin, a novel cuticular protein, jagunal, NAC domain protein, and vitellogenin) were most likely to be involved in viral movement, replication and transovarial transmission. This work also provides evidence that the novel cuticular protein, CPR1, from L. striatellus is essential for RSV transmission by its vector insect. CPR1 binds the nucleocapsid protein (pc3) of RSV both in vivo and in vitro and colocalizes with RSV in the hemocytes of L. striatellus. Knockdown of CPR1 transcription using RNA interference resulted in a decrease in the concentration of RSV in the hemolymph, salivary glands and in viral transmission efficiency. These data suggest that CPR1 binds RSV in the insect and stabilizes the viral concentration in the hemolymph, perhaps to protect the virus or to help move the virus to the salivary tissues. Our studies provide direct experimental evidence that viruses can use existing vector proteins to aid their survival in the hemolymph. Identifying these putative vector molecules should lead to a better understanding of the interactions between viruses and vector insects.