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学者姓名：黄志鹏
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Abstract ：
Uridine diphosphate-glycosyltransferases (UGTs) catalyze sugar conjugation of endogenous and exogenous molecules in insects. In this study, 45 putative UGT genes in 11 families were identified from the genome of S. litura. Exposure to Bt toxins in 5th-instar larvae of the WT strain led to a significant upregulation of midgut UGT40 expression, particularly of SlUGT40D20, SlUGT40D22, and SlUGT40F25. This upregulation was not observed following exposure to chemical pesticides. Knockout of the UGT genes SlUGT40D20 and SlUGT40D22 in S. litura (mutant strains SlUGT40D20-KO and SlUGT40D22-KO) via CRISPR/Cas9-mediated mutagenesis increased susceptibility of S. litura to Bacillus thuringiensis (Bt) insecticidal proteins. However, in comparison with the wild-type (WT) strain, the mutants did not change susceptibility to chemical pesticides. Observations of 5thinstar larval midgut by electron microscopy revealed severe damage to the midgut epithelium caused by Cry1Ac toxin at 10 mu g/g in the SlUGT40D20-KO strain compared to the WT. SDS-PAGE and LC MS/MS analyses identified a specific protein band corresponding to putative proteoglycans in the peritrophic matrix of the WT strain, which was absent in the SlUGT40D20-KO strain. Our study suggests an inverse correlation between expression of some UGTs and the susceptibility of S. litura larvae to some Bt toxins.
Keyword ：
Bt toxin Bt toxin CRISPR/Cas9 CRISPR/Cas9 Midgut Midgut Spodoptera litura Spodoptera litura UDP-Glycosyltransferases UDP-Glycosyltransferases
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| GB/T 7714 | Shao, Ensi , Wang, Can , Zheng, Wenhui et al. Knockout of two uridine diphosphate-glycosyltransferase genes increases the susceptibility of Spodoptera litura to Bacillus thuringiensis toxins [J]. | INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY , 2024 , 175 . |
| MLA | Shao, Ensi et al. "Knockout of two uridine diphosphate-glycosyltransferase genes increases the susceptibility of Spodoptera litura to Bacillus thuringiensis toxins" . | INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY 175 (2024) . |
| APA | Shao, Ensi , Wang, Can , Zheng, Wenhui , Ma, Yige , Wang, Shanshan , Sha, Li et al. Knockout of two uridine diphosphate-glycosyltransferase genes increases the susceptibility of Spodoptera litura to Bacillus thuringiensis toxins . | INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY , 2024 , 175 . |
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The applications of alginate lyase are diverse, but efficient commercial enzymes are still unavailable. In this study, a novel alginate lyase with high activity was obtained from the marine bacteria Vibrio sp. Ni1. The ORF of the algB gene has 1824 bp, encoding 607 amino acids. Homology analysis shows that AlgB belongs to the PL7 family. There are two catalytic domains with the typical region of QIH found in AlgB. The purified recombinant enzyme of AlgB shows highest activity at 35 degrees C, pH 8.0, and 50 mmol/L Tris-HCl without any metal ions. Only K+ slightly enhances the activity, while Fe2+ and Cu2+ strongly inhibit the activity. The AlgB preferred polyM as substrate. The end products of enzymatic mixture are DP2 and DP3, without any metal ion to assist them. This enzyme has good industrial application prospects.
Keyword ：
alginate alginate alginate lyase alginate lyase oligosaccharide oligosaccharide PL7 PL7 product distribution product distribution Vibrio Vibrio
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| GB/T 7714 | Sha, Li , Huang, Minghai , Huang, Xiaonan et al. Cloning and Characterization of a Novel Endo-Type Metal-Independent Alginate Lyase from the Marine Bacteria Vibrio sp. Ni1 [J]. | MARINE DRUGS , 2022 , 20 (8) . |
| MLA | Sha, Li et al. "Cloning and Characterization of a Novel Endo-Type Metal-Independent Alginate Lyase from the Marine Bacteria Vibrio sp. Ni1" . | MARINE DRUGS 20 . 8 (2022) . |
| APA | Sha, Li , Huang, Minghai , Huang, Xiaonan , Huang, Yongtong , Shao, Ensi , Guan, Xiong et al. Cloning and Characterization of a Novel Endo-Type Metal-Independent Alginate Lyase from the Marine Bacteria Vibrio sp. Ni1 . | MARINE DRUGS , 2022 , 20 (8) . |
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Spodoptera litura is one of the most destructive lepidopteran insects of cabbages and cauliflowers in the world. Cry1 and Vip3 toxins from Bacillus thuringiensis have been reported to show toxicity in multiple lepidopteran insects. Binding of toxic molecules to specific receptors on the midgut epithelial cells is known to be a key step in the action mode of Bt toxins. Aminopeptidase N (APN) -like proteins have been reported to be binding sites of multiple Cry toxins in the midgut of Cry susceptible insects. In the present study, we identified six midgut APNs by analysis of the genome and midgut transcriptome of S. litura. CRISPR/Cas9 mediated gene-knockout system was utilized to mutate the GPI-anchor signal peptide at the C terminus of SlAPN1. SlAPN1 was verified to be removed from the midgut brush border membrane vesicles of a homozygous knockout strain of S. litura (SlAPN1-KO). Bioassay results indicated that susceptibility of the SlAPN1-KO strain to Cry1Aa, Cry1Ac, Cry1Ca, and Vip3Aa toxins was close to that of the wild-type strain of S. litura. RT-qPCR results showed that the transcriptional level of SlAPN2-6 was not up-regulated after knockout of the SlAPN1. Results in this study indicated that the SlAPN1 did not play a critical role in the pathway of toxicity of Cry1Aa, Cry1Ac, Cry1Ca, and Vip3Aa toxins in S. litura.
Keyword ：
aminopeptidase N aminopeptidase N Cas9 Cas9 CRISPR CRISPR Cry1 Cry1 Spodoptera litura Spodoptera litura Vip3Aa Vip3Aa
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| GB/T 7714 | Wang, Can , Deng, Zhimin , Yuan, Jin et al. Removal of an Aminopeptidase N From Midgut Brush Border Does Not Affect Susceptibility of Spodoptera litura (Lepidoptera: Noctuidae) Larvae to Four Insecticidal Proteins of Bacillus thuringiensis (Bacillales: Bacillaceae) [J]. | JOURNAL OF ECONOMIC ENTOMOLOGY , 2022 , 116 (1) : 223-232 . |
| MLA | Wang, Can et al. "Removal of an Aminopeptidase N From Midgut Brush Border Does Not Affect Susceptibility of Spodoptera litura (Lepidoptera: Noctuidae) Larvae to Four Insecticidal Proteins of Bacillus thuringiensis (Bacillales: Bacillaceae)" . | JOURNAL OF ECONOMIC ENTOMOLOGY 116 . 1 (2022) : 223-232 . |
| APA | Wang, Can , Deng, Zhimin , Yuan, Jin , Xu, Kexin , Sha, Li , Guan, Xiong et al. Removal of an Aminopeptidase N From Midgut Brush Border Does Not Affect Susceptibility of Spodoptera litura (Lepidoptera: Noctuidae) Larvae to Four Insecticidal Proteins of Bacillus thuringiensis (Bacillales: Bacillaceae) . | JOURNAL OF ECONOMIC ENTOMOLOGY , 2022 , 116 (1) , 223-232 . |
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Background Infestation by tea green leafhoppers (Empoasca (Matsumurasca) onukii) can cause a series of biochemical changes in tea leaves. As a typical cell-rupture feeder, E. onukii secretes proteases while using its stylet to probe the tender shoots of tea plants (Camellia sinensis). This study identified and analyzed proteases expressed specifically in the salivary gland (SG) and gut of E. onukii through enzymatic activity assays complemented with an integrated analysis of transcriptomic and proteomic 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 but 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 formed two distinct clusters. Conclusions Altogether, this study provides insightful information on the digestive system of E. onukii. Compared to five other hemipteran species, we observed different patterns of proteases abundant in the SG and gut of E. onukii. These results will be beneficial in understanding the interaction between tea plants and E. onukii.
Keyword ：
Enzymatic activity Enzymatic activity Gut Gut Proteomics Proteomics RNA-Seq RNA-Seq Salivary gland Salivary gland Tea green leafhopper Tea green leafhopper
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| GB/T 7714 | Shao, Ensi , Song, Yujuan , Wang, Yaomin et al. Transcriptomic and proteomic analysis of putative digestive proteases in the salivary gland and gut of Empoasca (Matsumurasca) onukii Matsuda [J]. | BMC GENOMICS , 2021 , 22 (1) . |
| MLA | Shao, Ensi et al. "Transcriptomic and proteomic analysis of putative digestive proteases in the salivary gland and gut of Empoasca (Matsumurasca) onukii Matsuda" . | BMC GENOMICS 22 . 1 (2021) . |
| APA | Shao, Ensi , Song, Yujuan , Wang, Yaomin , Liao, Yichen , Luo, Yufei , Liu, Sijun et al. Transcriptomic and proteomic analysis of putative digestive proteases in the salivary gland and gut of Empoasca (Matsumurasca) onukii Matsuda . | BMC GENOMICS , 2021 , 22 (1) . |
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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.
Keyword ：
Bacillus thuringiensis Bacillus thuringiensis site-directed mutagenesis site-directed mutagenesis Spodoptera litura Spodoptera litura Vip3A Vip3A
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| GB/T 7714 | Shao, Ensi , Zhang, Aishan , Yan, Yaqi et al. Oligomer Formation and Insecticidal Activity of Bacillus thuringiensis Vip3Aa Toxin [J]. | TOXINS , 2020 , 12 (4) . |
| MLA | Shao, Ensi et al. "Oligomer Formation and Insecticidal Activity of Bacillus thuringiensis Vip3Aa Toxin" . | TOXINS 12 . 4 (2020) . |
| APA | Shao, Ensi , Zhang, Aishan , Yan, Yaqi , Wang, Yaomin , Jia, Xinyi , Sha, Li et al. Oligomer Formation and Insecticidal Activity of Bacillus thuringiensis Vip3Aa Toxin . | TOXINS , 2020 , 12 (4) . |
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The brown planthopper (BPH) Nilaparvata lugens is one of the most destructive insect pests in the rice fields of Asia. Like other hemipteran insects, BPH is not susceptible to Cry toxins of Bacillus thuringiensis (Bt) or transgenic rice carrying Bt cry genes. Lack of Cry receptors in the midgut is one of the main reasons that BPH is not susceptible to the Cry toxins. The main Cry-binding proteins (CBPs) of the susceptible insects are cadherin, aminopeptidase N (APN), and alkaline phosphatase (ALP). In this study, we analyzed and validated de novo assembled transcripts from transcriptome sequencing data of BPH to identify and characterize homologs of cadherin, APN, and ALP. We then compared the cadherin-, APN-, and ALP-like proteins of BPH to previously reported CBPs to identify their homologs in BPH. The sequence analysis revealed that at least one cadherin, one APN, and two ALPs of BPH contained homologous functional domains identified from the Cry-binding cadherin, APN, and ALP, respectively. Quantitative real-time polymerase chain reaction used to verify the expression level of each putative Cry receptor homolog in the BPH midgut indicated that the CBPs homologous APN and ALP were expressed at high or medium-high levels while the cadherin was expressed at a low level. These results suggest that homologs of CBPs exist in the midgut of BPH. However, differences in key motifs of CBPs, which are functional in interacting with Cry toxins, may be responsible for insusceptibility of BPH to Cry toxins.
Keyword ：
alkaline phosphatase alkaline phosphatase aminopeptidase N aminopeptidase N brown planthopper brown planthopper cadherin cadherin de novo assembly de novo assembly
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| GB/T 7714 | Shao, Ensi , Lin, Li , Liu, Sijun et al. Analysis of Homologs of Cry-toxin Receptor-Related Proteins in the Midgut of a Non-Bt Target, Nilaparvata lugens (Stal) (Hemiptera: Delphacidae) [J]. | JOURNAL OF INSECT SCIENCE , 2018 , 18 (1) . |
| MLA | Shao, Ensi et al. "Analysis of Homologs of Cry-toxin Receptor-Related Proteins in the Midgut of a Non-Bt Target, Nilaparvata lugens (Stal) (Hemiptera: Delphacidae)" . | JOURNAL OF INSECT SCIENCE 18 . 1 (2018) . |
| APA | Shao, Ensi , Lin, Li , Liu, Sijun , Zhang, Jiao , Chen, Xuelin , Sha, Li et al. Analysis of Homologs of Cry-toxin Receptor-Related Proteins in the Midgut of a Non-Bt Target, Nilaparvata lugens (Stal) (Hemiptera: Delphacidae) . | JOURNAL OF INSECT SCIENCE , 2018 , 18 (1) . |
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Bacillus thuringiensis (Bt) and transgenic crops carrying cry genes are widely used in the management of lepidopteran and coleopteran pests. However, almost none of the Cry toxins have insecticidal properties against sap-sucking insects, such as planthoppers, leafhoppers and aphids. To understand the low insecticidal activity of Cry1Ac toxin on sap-sucking insects, we investigated two critical steps in the Bt-intoxication cascade: the proteolytic processing of Cry1Ac toxin by gut proteases, and the binding of Cry1Ac to brush border membrane vesicles (BBMV) of Nilaparvata lugens. Proteolytic processing of Cry1Ac protoxin by N.lugens gut proteases resulted in an approximate to 65kDa product, similar to the expected size of the trypsin-activated Cry1Ac toxin. In addition, activation of cysteine proteases in N.lugens gut increased the efficiency of proteolytic activities in the processing of Cry1Ac. However, feeding N.lugens nymphs with either Cry1Ac protoxin or trypsin-activated Cry1Ac toxin resulted in low mortalities. The LC50 of Cry1Ac protoxin and trypsin-activated Cry1Ac was 198.92 and 450.18g/mL, respectively. In vitro binding analysis of BBMV with the pre-activated Cry1Ac showed that Cry1Ac toxin could specifically bind to the BBMV. However, binding competition with 500-fold molar excess GalNAc (N-acetyl-d-galactosamine) suggested that the binding was not mediated by GalNAc-like glycoproteins. These results indicate that Cry1Ac toxin could be successfully processed by the treatment of N.lugens gut proteases. However, the binding of Cry1Ac toxin to the midgut brush border membrane was not mediated by GalNAc-like glycoprotein. This may be responsible for the low susceptibility of N.lugens to Cry1Ac.
Keyword ：
BBMV BBMV binding assay binding assay Brown planthopper Brown planthopper Cry1Ac Cry1Ac gut proteases gut proteases
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| GB/T 7714 | Shao, Ensi , Chen, Chen , Chen, Hanze et al. In vitro hydrolysis of Bacillus thuringiensis Cry1Ac toxin by gut proteases of Nilaparvata lugens (Stal) and binding assays of Cry1Ac toxin with brush border membrane of N.lugens midgut [J]. | BIOCONTROL SCIENCE AND TECHNOLOGY , 2018 , 28 (5) : 446-458 . |
| MLA | Shao, Ensi et al. "In vitro hydrolysis of Bacillus thuringiensis Cry1Ac toxin by gut proteases of Nilaparvata lugens (Stal) and binding assays of Cry1Ac toxin with brush border membrane of N.lugens midgut" . | BIOCONTROL SCIENCE AND TECHNOLOGY 28 . 5 (2018) : 446-458 . |
| APA | Shao, Ensi , Chen, Chen , Chen, Hanze , Liu, Sijun , Lin, Li , Wang, Yaomin et al. In vitro hydrolysis of Bacillus thuringiensis Cry1Ac toxin by gut proteases of Nilaparvata lugens (Stal) and binding assays of Cry1Ac toxin with brush border membrane of N.lugens midgut . | BIOCONTROL SCIENCE AND TECHNOLOGY , 2018 , 28 (5) , 446-458 . |
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本发明提供了一种松墨天牛低龄幼虫的人工饲料及其制备方法，包括：木屑45～60份、韧皮部粉末85～110份、蔗糖35～45份、干酵母20～30份、麸皮45～70份、琼脂25～35份、苯甲酸钠3.5～4.0份、山梨酸1.5～2.0份、虾壳粉8~15份、250～350份蒸馏水。所采用的制备方法能够很好的控制饲料的理化性质，操作简单，适合实验室条件下的制备和幼虫的生长所需。采用本配方饲养Ⅰ、Ⅱ龄的松墨天牛幼虫，与其它人工饲料饲养的幼虫相比，生长快，活性强，个体大，利于幼虫的后续生长和传代饲养。可实现在人为控制环境条件下调控松墨天牛的生长，做到同时保有不同龄期、虫态松墨天牛，为实验提供长期稳定的天牛种群。
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| GB/T 7714 | 吴松青 , 夏枫 , 张飞萍 et al. 一种松墨天牛低龄幼虫的人工饲料及其制备方法 : CN201710324582.2[P]. | 2017-05-10 . |
| MLA | 吴松青 et al. "一种松墨天牛低龄幼虫的人工饲料及其制备方法" : CN201710324582.2. | 2017-05-10 . |
| APA | 吴松青 , 夏枫 , 张飞萍 , 梁光红 , 胡霞 , 王荣 et al. 一种松墨天牛低龄幼虫的人工饲料及其制备方法 : CN201710324582.2. | 2017-05-10 . |
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本发明公开了一种人工养殖松墨天牛的方法，用于实验室条件下饲养繁殖松墨天牛。所述方法包括：(1)松墨天牛亚成熟个体的人工饲养；(2)松墨天牛人工产房的配备；(3)松墨天牛性成熟个体的人工配对饲养及诱导繁殖；(4)松墨天牛各龄期幼虫人工饲料的制备；(5)松墨天牛初生幼虫的分离获取；(6)松墨天牛幼虫转入人工饲料的后续培养；(7)松墨天牛蛹期及羽化管理。本发明采用的人工养殖松墨天牛的方法，在实验室条件下构建出一套适用于人工培养各生长阶段的松墨天牛的体系，在减少松材消耗的同时，显著提高松墨天牛各生长阶段的成活率，排除季节对松墨天牛生长繁殖的影响，缩短松墨天牛的生长周期，形成稳定的实验虫源。
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| GB/T 7714 | 吴松青 , 夏枫 , 张飞萍 et al. 一种人工养殖松墨天牛的方法 : CN201710324580.3[P]. | 2017-05-10 . |
| MLA | 吴松青 et al. "一种人工养殖松墨天牛的方法" : CN201710324580.3. | 2017-05-10 . |
| APA | 吴松青 , 夏枫 , 张飞萍 , 梁光红 , 胡霞 , 王荣 et al. 一种人工养殖松墨天牛的方法 : CN201710324580.3. | 2017-05-10 . |
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Bacillus thuringiensis var. israelensis (Bti) is highly pathogenic to mosquito larvae and is widely used for mosquito control. Its mosquitocidal activity however is relatively low compared to many chemical insecticides. The detoxification mechanisms in the mosquito, among other things, might neutralize the Bti activity, resulting in resistance or tolerance. We tested whether or not the detoxification mechanisms against chemical insecticides might also operate against Bti, rendering it less effective. We targeted four enzymes in Aedes aegypti larvae involved in detoxification with inhibitors that have been used in resistance studies in chemical insecticides and assayed their effects on Bti toxicity. Results revealed that phenylmethanesulphonyl fluoride (PMSF), diethyl maleate, phenobarbital (PB), and piperonyl butoxide (PBO) altered Bti toxicity to various degrees. PMSF is a serine protease inhibitor that prevents Bti digestion and improves Bti activity. PB that induces several detoxifying enzymes had two different effects depending on the method of treatment. Mortality was higher when treatment with PB was discontinuous (149%) whereas with continuous treatment it was lower (101%). PBO, a typical cytochrome P450 inhibitor, increased Bti effect (159%). The combination of discontinuous pretreatment of larvae with PB followed by PBO had a synergistic effect and showed increased activity (146%). It appears that the mechanism for Bti resistance in mosquitoes is similar to that of chemical insecticides. Our studies indicate that we may be able to increase Bti activity by inhibiting some of the detoxification systems as active as broad spectrum chemical insecticides.
Keyword ：
Aedes aegypti Aedes aegypti Bacillus thuringiensis Bacillus thuringiensis Bti Bti enzyme activity enzyme activity inhibitor inhibitor tolerance tolerance
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| GB/T 7714 | Hu, Xiaohua , Guo, Yajie , Wu, Songqing et al. Effect of proteolytic and detoxification enzyme inhibitors on Bacillus thuringiensis var. israelensis tolerance in the mosquito Aedes aegypti [J]. | BIOCONTROL SCIENCE AND TECHNOLOGY , 2017 , 27 (2) : 169-179 . |
| MLA | Hu, Xiaohua et al. "Effect of proteolytic and detoxification enzyme inhibitors on Bacillus thuringiensis var. israelensis tolerance in the mosquito Aedes aegypti" . | BIOCONTROL SCIENCE AND TECHNOLOGY 27 . 2 (2017) : 169-179 . |
| APA | Hu, Xiaohua , Guo, Yajie , Wu, Songqing , Liu, Zhaoxia , Fu, Tao , Shao, Ensi et al. Effect of proteolytic and detoxification enzyme inhibitors on Bacillus thuringiensis var. israelensis tolerance in the mosquito Aedes aegypti . | BIOCONTROL SCIENCE AND TECHNOLOGY , 2017 , 27 (2) , 169-179 . |
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