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- 저자 : Lei Hea (검색결과 2 건)
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Lei Hea,Huan Yu,Cun-Yi Xu,Ying Zhao,Fu-Xiang Yang,Ya-Dong Guo,Guo-Hua Huang 한국응용곤충학회 2019 Journal of Asia-Pacific Entomology Vol.22 No.2
Insect chitinases are necessary hydrolytic enzymes for chitin degradation, insect molting and metamorphosis. In this study, five chitinases encoded in the genome of Spodoptera exigua (SeCHIT7, SeCHIT11, SeCHIT12, SeCHIT13 and SeCHIT14) were identified by reverse transcription PCR. Phylogenetic analysis indicated that SeCHIT7 belonged to Group III, and SeCHIT11/12/13/14 belonged to Group VIII. Real-time quantitative PCR analyses showed that SeCHIT7 had an extensive transcription at the fourth- and fifth-instar larval and pupal stages, while SeCHIT11 had the highest transcription level at the egg stage, and the transcription of SeCHIT12 increased by over 1000 times from pre-pupal to pupal stage. Tissue-specific analyses showed that these three SeCHITs (SeCHIT7, SeCHIT11 and SeCHIT12) were mainly transcribed in the midgut and fat body. Chitinase activity assays suggested that the activity had a lower level at the egg stage and peaked at the pupal stage. The activities were increased by 9.4 times from egg to first-instar larval stage. Tissue specificity analysis showed that the highest activity was observed in the fat body, followed by hemolymph and cuticle of the pre-pupal stage. Overall, these results provided valid information for further research on the biological function and regulation of chitinases in S. exigua.
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Huan Yu,Lei Hea,Yi-Yi Ou-Yang,Guo-Hua Huang 한국응용곤충학회 2018 Journal of Asia-Pacific Entomology Vol.21 No.3
Antibodies, which are wildly used in molecular researches, are proteins secreted by plasma cells that can specifically recognize specific antigens. To obtain a stable reference antibodies are important for protein analysis. In this study, a capable glyceraldehyde phosphate dehydrogenase (GAPDH) antiserum against most noctuid larval protein samples was prepared. Firstly, the full-length gapdh was amplified from Spodoptera exigua larvae to construct the prokaryotic expression vector. The purified His-tag fused GAPDH protein was used to immunize rabbits for the antiserum preparation. Protein samples extracted from 11 insect species distributed across seven families and three orders were used to perform the Western bolt analysis. The bright specific bands were detected in S. exigua, S. litura, Helicoverpa armigera, and Mythimna seperata protein samples, indicating that this antiserum may be capable of detecting noctuid larval encoded GAPDH. Further immunofluorescence identification of H. armigera and S. exigua paraffin section slides with GAPDH antiserum exhibited an identical cytostained image. The GAPDH antiserum prepared in this study is useful and efficient as reference antibodies in studies involving noctuid larval protein samples in other related fields.
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