Arbovirus suppression of a lectin protein-mediated broad-spectrum resistance enhances herbivorous vector performance and viral transmission.

Abstract

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.