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学者姓名：邵恩斯
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Abstract ：
Pearl millet is a major cereal crop that feeds more than 90 million people worldwide in arid and semi-arid regions. The stalk phenotypes of Poaceous grasses are critical for their productivity and stress tolerance; however, the molecular mechanisms governing stalk development in pearl millet remain to be deciphered. In this study, we spatiotemporally measured 19 transcriptomes for stalk internodes of four different early developmental stages. Data analysis of the transcriptomes defined four developmental zones on the stalks and identified 12 specific gene sets with specific expression patterns across the zones. Using weighted gene co-expression network analysis (WGCNA), we found that two co-expression modules together with candidate genes were involved in stalk elongation and the thickening of pearl millet. Among the elongation-related candidate genes, we established by SELEX that a MYB-family transcription factor PMF7G02448 can bind to the promoters of three cell wall synthases genes (CesAs). In summary, these findings provide insights into stalk development and offer potential targets for future genetic improvement in pearl millet.
Keyword ：
gene expression gene expression genetic improvement genetic improvement pearl millet pearl millet stalk development stalk development transcriptome analysis transcriptome analysis
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| GB/T 7714 | Mao, Fei , Luo, Lin , Ma, Nana et al. A Spatiotemporal Transcriptome Reveals Stalk Development in Pearl Millet [J]. | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES , 2024 , 25 (18) . |
| MLA | Mao, Fei et al. "A Spatiotemporal Transcriptome Reveals Stalk Development in Pearl Millet" . | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 25 . 18 (2024) . |
| APA | Mao, Fei , Luo, Lin , Ma, Nana , Qu, Qi , Chen, Hao , Yi, Chao et al. A Spatiotemporal Transcriptome Reveals Stalk Development in Pearl Millet . | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES , 2024 , 25 (18) . |
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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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Bacillus thuringiensis Vip3 toxins form a tetrameric structure crucial for their insecticidal activity. Each Vip3Aa monomer comprises five domains. Interaction of the first four alpha-helices in domain I with the target cellular membrane was proposed to be a key step before pore formation. In this study, four N-terminal alpha-helix-deleted truncations of Vip3Aa were produced and, it was found that they lost both liposome permeability and insecticidal activity against Spodoptera litura. To further probe the role of domain I in membrane permeation, the full-length domain I and the fragments of N-terminal alpha-helix-truncated domain I were fused to green fluorescent protein (GFP), respectively. Only the fusion carrying the full-length domain I exhibited permeability against artificial liposomes. In addition, seven Vip3Aa-Cry1Ac fusions were also constructed by combination of alpha-helices from Vip3Aa domains I and II with the domains II and III of Cry1Ac. Five of the seven combinations were determined to show membrane permeability in artificial liposomes. However, none of the Vip3Aa-Cry1Ac combinations exhibited insecticidal activity due to the significant reduction in proteolytic stability. These results indicated that the N-terminal helix alpha 1 in the Vip3Aa domain I is essential for both insecticidal activity and liposome permeability and that domain I of Vip3Aa preserved a high liposome permeability independently from domains II-V.
Keyword ：
Cry1Ac Cry1Ac domain exchange domain exchange insecticidal activity insecticidal activity membrane permeability membrane permeability Vip3Aa Vip3Aa
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| GB/T 7714 | Shao, Ensi , Huang, Hanye , Yuan, Jin et al. N-Terminal α-Helices in Domain I of Bacillus thuringiensis Vip3Aa Play Crucial Roles in Disruption of Liposomal Membrane [J]. | TOXINS , 2024 , 16 (2) . |
| MLA | Shao, Ensi et al. "N-Terminal α-Helices in Domain I of Bacillus thuringiensis Vip3Aa Play Crucial Roles in Disruption of Liposomal Membrane" . | TOXINS 16 . 2 (2024) . |
| APA | Shao, Ensi , Huang, Hanye , Yuan, Jin , Yan, Yaqi , Ou, Luru , Chen, Xiankun et al. N-Terminal α-Helices in Domain I of Bacillus thuringiensis Vip3Aa Play Crucial Roles in Disruption of Liposomal Membrane . | TOXINS , 2024 , 16 (2) . |
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Giant reed (Arundo donax) is widely distributed across the globe and is considered an important energy crop. This study presents the first comprehensive analysis of the chloroplast genome of giant reed, revealing detailed characteristics of this species' chloroplast genome. The chloroplast genome has a total length of 137,153 bp, containing 84 protein-coding genes, 38 tRNA genes, and 8 rRNA genes, with a GC content of 39%. Functional analysis indicates that a total of 45 photosynthesis-related genes and 78 self-replication-related genes were identified, which may be closely associated with its adaptability and growth characteristics. Phylogenetic analysis confirmed that Arundo donax cv. Lvzhou No.1 belongs to the Arundionideae clade and occupies a distinct evolutionary position compared to other Arundo species. The findings of this study not only enhance our understanding of the giant reed genome but also provide valuable genetic resources for its application in biotechnology, bioenergy crop development, and ecological restoration.
Keyword ：
Arundionideae Arundionideae Arundo donax Arundo donax chloroplast genome chloroplast genome phylogenetic analysis phylogenetic analysis
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| GB/T 7714 | Luo, Lin , Qu, Qi , Lin, Hui et al. Exploring the Evolutionary History and Phylogenetic Relationships of Giant Reed (Arundo donax) through Comprehensive Analysis of Its Chloroplast Genome [J]. | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES , 2024 , 25 (14) . |
| MLA | Luo, Lin et al. "Exploring the Evolutionary History and Phylogenetic Relationships of Giant Reed (Arundo donax) through Comprehensive Analysis of Its Chloroplast Genome" . | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 25 . 14 (2024) . |
| APA | Luo, Lin , Qu, Qi , Lin, Hui , Chen, Jiaming , Lin, Zhanxi , Shao, Ensi et al. Exploring the Evolutionary History and Phylogenetic Relationships of Giant Reed (Arundo donax) through Comprehensive Analysis of Its Chloroplast Genome . | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES , 2024 , 25 (14) . |
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| GB/T 7714 | Luo, Lin , Lin, Dongmei , Li, Jinhui et al. EGDB: A comprehensive multi-omics database for energy grasses and the epigenomic atlas of pearl millet [J]. | IMETA , 2024 , 4 (1) . |
| MLA | Luo, Lin et al. "EGDB: A comprehensive multi-omics database for energy grasses and the epigenomic atlas of pearl millet" . | IMETA 4 . 1 (2024) . |
| APA | Luo, Lin , Lin, Dongmei , Li, Jinhui , Chen, Hao , Qu, Qi , Zhang, Lin et al. EGDB: A comprehensive multi-omics database for energy grasses and the epigenomic atlas of pearl millet . | IMETA , 2024 , 4 (1) . |
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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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【目的】氨肽酶N(aminopeptidase N, APN)是昆虫消化系统中重要的蛋白酶。本研究旨在对在褐飞虱Nilaparvata lugens中肠中两个具有较高转录水平的apn基因(nlapn1和nlapn4)在中肠上皮细胞上的表达及其蛋白功能特性进行鉴定与分析。【方法】利用最大似然法进行褐飞虱NLAPN1和NLAPN4的系统进化分析;利用Western blot分析NLAPN1及NLAPN4在中肠刷状缘膜囊泡(brush border membrane vesicles, BBMVs)中的定位;利用LC-ESI-MS/MS技术对Western blot定位的NLAPN1及NLAPN4进行鉴定。在果蝇Drosophila S2细胞内分别表达两个NLAPN蛋白,并利用Western blot及免疫荧光定位技术对NLAPN1与NLAPN4进行S2细胞内的定位;分别以L-亮氨酸对硝基苯胺(leucine-p-NA)、L-丙氨酸4-硝基苯胺盐酸盐(Ala-p-NA)、L-甲硫氨酸对硝基苯胺盐酸盐(Met-p-NA)和L-赖氨酸对硝基苯胺二氢溴酸盐(Lys-p-NA)为底物测定NLAPN1和NLAPN4的酶活性。【结果】系统进化树分析结果显示,褐飞虱NLAPN1及NLAPN4与其他半翅目昆虫肠道中高表达的APN分在了同一分支中。Western blot及LC-ESI-MS/MS质谱分析结果证明NLAPN1与NLAPN4均存在于褐飞虱中肠刷状缘膜囊泡中,分子量约为160 kD。Western blot及免疫荧光定位结果显示,两个NLAPN蛋白均位于S2细胞膜上,而C端缺失糖基磷脂酰肌醇(glycosylphosphatidylinositol, GPI)锚定位点的NLAPN4lackG蛋白分布在细胞质中。酶活性测定结果显示,以L-丙氨酸4-硝基苯胺盐酸盐及L-赖氨酸对硝基苯胺二氢溴酸盐为底物时NLAPN1和NLAPN4都具有一定的酶活性,而以L-亮氨酸对硝基苯胺为底物时NLAPN1有极高的酶活性(>60 U/mg)。【结论】NLAPN1与NLAPN4是褐飞虱中肠上皮细胞膜上高表达的两个膜结合APN蛋白,且都通过C端的GPI锚定附着在细胞膜上。NLAPN1与NLAPN4与鳞翅目、鞘翅目、双翅目等昆虫中肠膜结合APN有着近似的蛋白结构与酶学特性。膜结合APN在褐飞虱中肠中的生理生化功能及其与外源病原物的互作机制还有待进一步深入研究。
Keyword ：
S2细胞 S2细胞 中肠 中肠 氨肽酶N 氨肽酶N 膜结合蛋白 膜结合蛋白 褐飞虱 褐飞虱 酶活性 酶活性
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| GB/T 7714 | 林莉 , 余小强 , 关雄 et al. 褐飞虱中肠两种氨肽酶N的鉴定及蛋白特性分析 [J]. | 昆虫学报 , 2021 , 64 (07) : 771-780 . |
| MLA | 林莉 et al. "褐飞虱中肠两种氨肽酶N的鉴定及蛋白特性分析" . | 昆虫学报 64 . 07 (2021) : 771-780 . |
| APA | 林莉 , 余小强 , 关雄 , 邵恩斯 . 褐飞虱中肠两种氨肽酶N的鉴定及蛋白特性分析 . | 昆虫学报 , 2021 , 64 (07) , 771-780 . |
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Keyword ：
diluted sulfuric acid treatment diluted sulfuric acid treatment hot water treatment hot water treatment reducing sugar reducing sugar sodium hydroxide treatment sodium hydroxide treatment Spent Juncao Substrate Spent Juncao Substrate
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| GB/T 7714 | Huang, Chenyan , Wu, Xuan , Xiong, Yueting et al. Conversion of spent Juncao Substrate into reducing sugar using a one-step method [J]. | ENERGY SOURCES PART A-RECOVERY UTILIZATION AND ENVIRONMENTAL EFFECTS , 2020 , 46 (1) : 15506-15518 . |
| MLA | Huang, Chenyan et al. "Conversion of spent Juncao Substrate into reducing sugar using a one-step method" . | ENERGY SOURCES PART A-RECOVERY UTILIZATION AND ENVIRONMENTAL EFFECTS 46 . 1 (2020) : 15506-15518 . |
| APA | Huang, Chenyan , Wu, Xuan , Xiong, Yueting , Rebeca, Carballar Lejarazu , Zhang, Jun , Zhang, Shiying et al. Conversion of spent Juncao Substrate into reducing sugar using a one-step method . | ENERGY SOURCES PART A-RECOVERY UTILIZATION AND ENVIRONMENTAL EFFECTS , 2020 , 46 (1) , 15506-15518 . |
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