ABSTRACT: Trichogramma dendrolimi is one of most successfully industrialized Trichogramma species for agricultural and forestry pest control. Despite extensive research enhancing our understanding of the physiological and behavioral traits of T. dendrolimi, the exploration of the molecular mechanisms governing parasitism in this species is hindered by the absence of functional analysis of its venom proteins. Here, we used artificial host eggs , filled with 1× phosphate-buffered saline (PBS) buffer in parafilm membrane, to replicate the natural oviposition behavior of wasps for the extraction of authentic venom components from T. dendrolimi. We integrated the proteome of venom proteins obtained through artificial host eggAHEs and the transcriptome of the VA venom apparatus to identify the venom protein of T. dendrolimi. A total of 649 putative venom proteins were identified, with the majority being hydrolases, oxidoreductases, proteasomes, transferases, protease inhibitors, isomerases, ligases, and lyases. Among these, hydrolases, particularly serine proteases, were the most abundant protein group in T. dendrolimi venom.A total of 649 putative venom proteins were identified, predominantly comprising hydrolases, oxidoreductases, proteasomes, transferases, protease inhibitors, isomerases, ligases, and lyases, with hydrolases, especially serine proteases, standing out as the predominant protein group in T. dendrolimi venom.
Ying Hu 
