Discovery of novel thrips vector proteins that bind to the viral attachment protein of the plant bunyavirus, tomato spotted wilt virus

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Foilsithe in:bioRxiv (Apr 27, 2019), p. n/a
Príomhchruthaitheoir: Badillo-Vargas, Ismael E
Rannpháirtithe: Chen, Yuting, Martin, Kathleen M, Rotenberg, Dorith, Whitfield, Anna E
Foilsithe / Cruthaithe:
Cold Spring Harbor Laboratory Press
Ábhair:
Rochtain ar líne:Citation/Abstract
Full text outside of ProQuest
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LEADER 00000nab a2200000uu 4500
001 2111029863
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022 |a 2692-8205 
024 7 |a 10.1101/416560  |2 doi 
035 |a 2111029863 
045 0 |b d20190427 
100 1 |a Badillo-Vargas, Ismael E 
245 1 |a Discovery of novel thrips vector proteins that bind to the viral attachment protein of the plant bunyavirus, tomato spotted wilt virus 
260 |b Cold Spring Harbor Laboratory Press  |c Apr 27, 2019 
513 |a Working Paper 
520 3 |a The plant-pathogenic virus, tomato spotted wilt virus (TSWV), encodes a structural glycoprotein (GN) that, like with other bunyavirus/vector interactions, serves a role in viral attachment and possibly entry into arthropod vector host cells. It is well documented that Frankliniella occidentalis is one of seven competent thrips vectors of TSWV transmission to plant hosts, however, the insect molecules that interact with viral proteins, such as GN, during infection and dissemination in thrips vector tissues are unknown. The goals of this project were to identify TSWV-interacting proteins (TIPs) that interact directly with TSWV GNand to localize expression of these proteins in relation to virus in thrips tissues of principle importance along the route of dissemination. We report here the identification of six TIPs from first instar larvae (L1), the most acquisition-efficient developmental stage of the thrips vector. Sequence analyses of these TIPs revealed homology to proteins associated with the infection cycle of other vector-borne viruses. Immunolocalization of the TIPs in L1s revealed robust expression in the midgut and salivary glands of F. occidentalis, the tissues most important during virus infection, replication and plant-inoculation. The TIPs and GN interactions were validated using protein-protein interaction assays. Two of the thrips proteins, endocuticle structural glycoprotein and cyclophilin, were found to be consistent interactors with GN. These newly discovered thrips protein-GN interactions are essential towards better understanding of transmission of persistent propagative plant viruses by their vectors, as well as for developing new strategies of insect pest management and virus resistance in plants. 
653 |a Infections 
653 |a Plant viruses 
653 |a Disease resistance 
653 |a Disease transmission 
653 |a Larvae 
653 |a Salivary gland 
653 |a Inoculation 
653 |a Viruses 
653 |a Pest control 
653 |a Midgut 
653 |a Wilt 
653 |a Vectors 
653 |a Homology 
653 |a Proteins 
653 |a Protein interaction 
653 |a Virus attachment 
700 1 |a Chen, Yuting 
700 1 |a Martin, Kathleen M 
700 1 |a Rotenberg, Dorith 
700 1 |a Whitfield, Anna E 
773 0 |t bioRxiv  |g (Apr 27, 2019), p. n/a 
786 0 |d ProQuest  |t Biological Science Database 
856 4 1 |3 Citation/Abstract  |u https://www.proquest.com/docview/2111029863/abstract/embedded/75I98GEZK8WCJMPQ?source=fedsrch 
856 4 0 |3 Full text outside of ProQuest  |u https://www.biorxiv.org/content/10.1101/416560v2