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PLoS Pathog


Title:Chemosensory protein regulates the behavioural response of Frankliniella intonsa and Frankliniella occidentalis to tomato zonate spot virus-Infected pepper (Capsicum annuum)
Author(s):Li H; Chen Y; Lu C; Tian H; Lin S; Wang L; Linghu T; Zheng X; Wei H; Fan X; Chen Y;
Address:"State Key Laboratory of Ecological Pest Control for Fujian and Taiwan Crops, Institute of Plant Protection, Fujian Academy of Agricultural Sciences, Fuzhou, China. Fujian Key Laboratory for Monitoring and Integrated Management of Crop Pests, Fuzhou Scientific Observing and Experimental Station of Crop Pests of Ministry of Agriculture, Fujian Engineering Research Center for Green Pest Management, Fuzhou, China. Fujian Agriculture and Forestry University, Fuzhou, China. Institute of Biotechnology and Germplasm Resources, Yunnan Academy of Agricultural Sciences, Kunming, China"
Journal Title:PLoS Pathog
Year:2023
Volume:20230508
Issue:5
Page Number:e1011380 -
DOI: 10.1371/journal.ppat.1011380
ISSN/ISBN:1553-7374 (Electronic) 1553-7366 (Print) 1553-7366 (Linking)
Abstract:"Many herbivorous insects rely on plant volatiles to locate their host plants. Vector-borne viral infections induce changes in plant volatiles, which render infected plants more attractive to insect vectors. However, the detailed mechanisms underlying the olfactory responses of insect vectors induced by the volatiles produced by virus-infected plants are poorly understood. Here, we show that volatiles emitted by pepper (Capsicum annuum) plants infected with tomato zonate spot virus (TZSV), particularly the volatile cis-3-hexenal, which is recognized by chemosensory protein 1 of the thrips Frankliniella intonsa (FintCSP1), are more attractive to F. intonsa than the volatiles emitted by non-infected pepper plants. FintCSP1 is highly abundant in the antenna of F. intonsa. Silencing of FintCSP1 significantly decreased electroantennogram responses of F. intonsa antennae to cis-3-hexenal and impaired thrips' responses to TZSV-infected pepper plants and cis-3-hexenal, as assessed using a Y-tube olfactometer. Three-dimensional model predictions indicated that FintCSP1 consists of seven alpha-helixes and two disulfide bridges. Molecular docking analysis suggested that cis-3-hexenal is positioned deep inside the binding pocket of FintCSP1 and binds to residues of the protein. We combined site-directed mutagenesis and fluorescence binding assays and identified three hydrophilic residues, Lys26, Thr28, and Glu67, of FintCSP1 as being critical for cis-3-hexenal binding. Furthermore, CSP of F. occidentalis (FoccCSP) is also a key olfactory protein involved in modulating the behaviour of F. occidentalis to TZSV-infected pepper. This study revealed the specific binding characteristics of CSPs to cis-3-hexenal and confirmed the general hypothesis that virus infections induce changes in host volatiles, which can be recognized by the olfactory proteins of the insect vector to enhance vector attraction and this may facilitate viral spread and transmission"
Keywords:Animals *Thysanoptera/physiology *Solanum lycopersicum *Capsicum Molecular Docking Simulation *Plant Viruses;
Notes:"MedlineLi, Heng Chen, Yixin Lu, Chengcong Tian, Houjun Lin, Shuo Wang, Liang Linghu, Tingting Zheng, Xue Wei, Hui Fan, Xiaojing Chen, Yong eng Research Support, Non-U.S. Gov't 2023/05/08 PLoS Pathog. 2023 May 8; 19(5):e1011380. doi: 10.1371/journal.ppat.1011380. eCollection 2023 May"

 
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