Abstract
The ubiquitin–proteasome system (UPS) is an essential protagonist in host–pathogen interactions. Among the three classes of enzymes in the UPS, ubiquitin-conjugating enzyme E2 plays a dual role in viral pathogenesis; however, the role of insect E2s in interactions with plant viruses is unclear. Twenty E2-encoding genes in Laodelphax striatellus, the small brown planthopper, were identified and classified into 17 groups by transcriptomic and phylogenetic analysis. Full-length cDNAs of four LstrE2s (LstrE2 A/E/G2/H) were obtained by rapid-amplification of cDNA ends (RACE-PCR) analysis. Expression of the four LstrE2s showed tissue- and development-specific patterns. RT-qPCR analyses revealed that Rice stripe viruse (RSV) infection increased the level of LstrE2 A/E/G2/H. Further study indicated that repression of LstrE2 E via RNAi caused significant increases in the expression of RSV coat protein mRNA and protein levels. These findings suggest that LstrE2 E inhibits RSV accumulation in the planthopper body. Understanding the function of LstrE2 E in RSV accumulation may ultimately result in the development of novel antiviral strategies.
Highlights
Ubiquitin (Ub) and ubiquitin-like (Ubl) proteins are highly-conserved molecules that generally contain around 100 amino acids that can be covalently attached to protein substrates through a versatile and reversible modification known as ubiquitination [1,2,3]
More than 42.94 million clean reads were obtained from each transcriptome candidates of ubiquitin-conjugating enzyme (E2) were screened with a BLASTx algorithm-based search and over 60.9% mapped to the small brown planthopper genome (Table S2)
These results indicated that repression of LstrE2 E facilitated Rice stripe viruse (RSV) accumulation in the
Summary
Ubiquitin (Ub) and ubiquitin-like (Ubl) proteins are highly-conserved molecules that generally contain around 100 amino acids that can be covalently attached to protein substrates through a versatile and reversible modification known as ubiquitination [1,2,3]. E2 carries the activated Ub/Ubl from the Ub/Ubl-E1 thioester to E3 or occasionally completes the conjugation of Ub/Ubl to target proteins in the absence of E3 [4,8]. During this modification, E2 determines the processivity and topology of polyubiquitin chain formation, which regulates the fate, function, and interaction of target proteins [9,10].
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