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Arbovirus suppression of a lectin protein-mediated broad-spectrum resistance enhances herbivorous vector performance and viral transmission
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Arbovirus suppression of a lectin protein-mediated broad-spectrum resistance enhances herbivorous vector performance and viral transmission
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Journal Article
Arbovirus suppression of a lectin protein-mediated broad-spectrum resistance enhances herbivorous vector performance and viral transmission
2025
Overview
Arboviruses often employ various strategies to manipulate the behavior of herbivorous vectors and host plants, thereby enhancing their transmission and infection. In this study, we identify a plant lectin protein, OsChtBL1, which possesses chitin-binding activity and specifically accumulates on the stylets of insect vectors. This binding creates a feeding barrier that reduces the vectors’ efficiency in acquiring and transmitting the virus. However, the rice stripe virus, a devastating pathogen in rice, counteracts this defense by utilizing a viral protein to recruit an E3 ubiquitin ligase, leading to the degradation of OsChtBL1. This degradation facilitates vector feeding and enhances viral transmission. Our findings provide insights into how arbovirus-infected host plants improve the performance of herbivorous vectors and offer deeper understanding of the complex interactions among arboviruses, vectors, and host plants.
Yang et al. demonstrate that the rice lectin OsChtBL1 accumulates in the food canal of insect vectors, creating a barrier that hinders feeding and reduces rice stripe virus (RSV) transmission. RSV counters this by using its P2 protein to recruit the host E3 ubiquitin ligase OsRING18, leading to OsChtBL1 degradation.
