This page has only limited features, please log in for full access.
Background: Infestation by tea green leafhoppers, Empoasca (Matsumurasca) onukii , could cause a series of biochemical changes in tea leaves. As a typical cell-rupture feeder, E. onukii secretes proteases while probing with its stylet into the tender shoots of tea plants ( Camellia sinensis ). This study identified and analyzed proteases specifically expressed in the salivary gland (SG) and gut of E. onukii through enzymatic activity assays, complemented with an integrated analysis of transcriptome and proteome data.Results: In total, 129 contigs representing seven types of putative proteases were identified. Transcript abundance of digestive proteases and enzymatic activity assays showed that cathepsin B-like protease, cathepsin L-like protease, and serine proteases (trypsin- and chymotrypsin-like protease) were highly abundant in the gut while moderately abundant in the SG. The abundance pattern of digestive proteases in the SG and gut of E. onukii differed from that of other hemipterans including Nilaparvata lugens , Laodelphax striatellus , Acyrthosiphum pisum , Halyomorpha halys and Nephotettix cincticeps . Phylogenetic analysis showed that aminopeptidase N-like proteins and serine proteases abundant in the SG or gut of hemipterans were distributed to two distinct clusters.Conclusions: Altogether, this study provide insightful information on the digestive system of E. onukii and observed different patterns of proteases abundant in the SG and gut of E. onukii , in comparison with other five hemipteran species. These results will be beneficial in understanding the interaction between tea plants and E. onukii .
Ensi Shao; Yujuan Song; Yaomin Wang; Yichen Liao; Yufei Luo; Sijun Liu; Xiong Guan; Zhipeng Huang. Transcriptomic and proteomic analysis of putative digestive proteases in the salivary gland and gut of Empoasca (Matsumurasca) onukii Matsuda. 2020, 1 .
AMA StyleEnsi Shao, Yujuan Song, Yaomin Wang, Yichen Liao, Yufei Luo, Sijun Liu, Xiong Guan, Zhipeng Huang. Transcriptomic and proteomic analysis of putative digestive proteases in the salivary gland and gut of Empoasca (Matsumurasca) onukii Matsuda. . 2020; ():1.
Chicago/Turabian StyleEnsi Shao; Yujuan Song; Yaomin Wang; Yichen Liao; Yufei Luo; Sijun Liu; Xiong Guan; Zhipeng Huang. 2020. "Transcriptomic and proteomic analysis of putative digestive proteases in the salivary gland and gut of Empoasca (Matsumurasca) onukii Matsuda." , no. : 1.
Background: Infestation by tea green leafhoppers, Empoasca (Matsumurasca) onukii, could cause a series of biochemical changes in tea leaves. As a typical cell-rupture feeder, E. onukii secretes proteases while probing with its stylet into the tender shoots of tea plants (Camellia sinensis). This study identified and analyzed proteases specifically expressed in the salivary gland (SG) and gut of E. onukii through enzymatic activity assays, complemented with an integrated analysis of transcriptome and proteome data.Results: In total, 129 contigs representing seven types of putative proteases were identified. Transcript abundance of digestive proteases and enzymatic activity assays showed that cathepsin B, cathepsin L, and serine proteases (trypsin and chymotrypsin) were highly abundant in the gut while moderately abundant in the SG. The abundance pattern of digestive proteases in the SG and gut of E. onukii differed from that of other hemipterans including Nilaparvata lugens, Laodelphax striatellus, Nephotettix cincticeps and Acyrthosiphum pisum. Phylogenetic analysis showed that aminopeptidase N-like proteins and serine proteases abundant in the SG or gut of hemipterans were distributed to two distinct clusters. Conclusions: Altogether, this study provide insightful information on the digestive system of E. onukii and observed different patterns of proteases abundant in the SG and gut of E. onukii, in comparison with other five hemipteran species. These results will be beneficial in understanding the interaction between tea plants and E. onukii.
Ensi Shao; Yujuan Song; Yaomin Wang; Yichen Liao; Yufei Luo; Sijun Liu; Xiong Guan; Zhipeng Huang. Transcriptomic and proteomic analysis of putative digestive proteases in the salivary gland and gut of Empoasca(Matsumurasca) onukii Matsuda. 2020, 1 .
AMA StyleEnsi Shao, Yujuan Song, Yaomin Wang, Yichen Liao, Yufei Luo, Sijun Liu, Xiong Guan, Zhipeng Huang. Transcriptomic and proteomic analysis of putative digestive proteases in the salivary gland and gut of Empoasca(Matsumurasca) onukii Matsuda. . 2020; ():1.
Chicago/Turabian StyleEnsi Shao; Yujuan Song; Yaomin Wang; Yichen Liao; Yufei Luo; Sijun Liu; Xiong Guan; Zhipeng Huang. 2020. "Transcriptomic and proteomic analysis of putative digestive proteases in the salivary gland and gut of Empoasca(Matsumurasca) onukii Matsuda." , no. : 1.
Bacillus thuringiensis (Bt) Vip3A proteins are important insecticidal proteins used for control of lepidopteran insects. However, the mode of action of Vip3A toxin is still unclear. In this study, the amino acid residue S164 in Vip3Aa was identified to be critical for the toxicity in Spodoptera litura. Results from substitution mutations of the S164 indicate that the insecticidal activity of Vip3Aa correlated with the formation of a >240 kDa complex of the toxin upon proteolytic activation. The >240 kDa complex was found to be composed of the 19 kDa and the 65 kDa fragments of Vip3Aa. Substitution of the S164 in Vip3Aa protein with Ala or Pro resulted in loss of the >240 kDa complex and loss of toxicity in Spodoptera litura. In contrast, substitution of S164 with Thr did not affect the >240 kDa complex formation, and the toxicity of the mutant was only reduced by 35%. Therefore, the results from this study indicated that formation of the >240 kDa complex correlates with the toxicity of Vip3Aa in insects and the residue S164 is important for the formation of the complex.
Ensi Shao; Aishan Zhang; Yaqi Yan; Yaomin Wang; Xinyi Jia; Li Sha; Xiong Guan; Ping Wang; Zhipeng Huang. Oligomer Formation and Insecticidal Activity of Bacillus thuringiensis Vip3Aa Toxin. Toxins 2020, 12, 274 .
AMA StyleEnsi Shao, Aishan Zhang, Yaqi Yan, Yaomin Wang, Xinyi Jia, Li Sha, Xiong Guan, Ping Wang, Zhipeng Huang. Oligomer Formation and Insecticidal Activity of Bacillus thuringiensis Vip3Aa Toxin. Toxins. 2020; 12 (4):274.
Chicago/Turabian StyleEnsi Shao; Aishan Zhang; Yaqi Yan; Yaomin Wang; Xinyi Jia; Li Sha; Xiong Guan; Ping Wang; Zhipeng Huang. 2020. "Oligomer Formation and Insecticidal Activity of Bacillus thuringiensis Vip3Aa Toxin." Toxins 12, no. 4: 274.