Protein Engineering of Novel Proteinase Inhibitors and Their Effects on the Growth of Spodoptera exigua Larvae.
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- INANAGA Hideko
- Laboratory of Biochemistry Faculty of Agriculture, Graduate School, Kyushu University
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- KOBAYASI Daiki
- Laboratory of Biochemistry Faculty of Agriculture, Graduate School, Kyushu University
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- KOUZUMA Yoshiaki
- Laboratory of Biochemistry Faculty of Agriculture, Graduate School, Kyushu University
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- AOKI-YASUNAGA Chisa
- Institute of Biological Control, Faculty of Agriculture, Graduate School, Kyushu University
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- IIYAMA Kazuhiro
- Institute of Biological Control, Faculty of Agriculture, Graduate School, Kyushu University
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- KIMURA Makoto
- Laboratory of Biochemistry Faculty of Agriculture, Graduate School, Kyushu University
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Abstract
Novel types of proteinase inhibitors with multi-inhibitory activities were generated by replacement of phytocystatin domains in sunflower multi-cystatin (SMC) by the serine proteinase inhibitor BGIT from bitter gourd seeds. Two chimeric inhibitors SMC-T3 and SMC-T23, in which the third domain in SMC and the second and third domains in SMC were replaced by BGIT, acquired trypsin inhibitory activity (Ki: 1.46 × 10-7 M and 1.75 × 10-7 M), retaining inhibitory activity toward papain (Ki: 4.5 × 10 -8 M and 1.52 × 10-7 M), respectively. We compared the chimeric inhibitors and the recombinant SMC (r-SMC) in relation to their effects on the growth of larval Spodoptera exigua. When the second instar larvae were reared on a diet containing rSMC, SMC-T3, or SMC-T23 for ten days, a significant reduction in weight gain was observed. Mean weights for rSMC, SMC-T3, and SMC-T23 were 43 mg, 32 mg, and 43 mg, respectively, as compared with that (60 mg) for the absence of the inhibitor. In contrast, BGIT had little effect on the growth of the S. exigua larvae. This result indicated that the chimeric inhibitor SMC-T3 with two phytocystatin domains and one serine proteinase inhibitor domain is an efficient inhibitor of proteinases in the S. exigua larvae. Therefore, this novel type of proteinase inhibitor with multi-inhibitory activities may represent a promising protein for successful application to a transgenic plant with insect resistance.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 65 (10), 2259-2264, 2001
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390282681453347328
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- NII Article ID
- 110002693269
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- NII Book ID
- AA10824164
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- COI
- 1:CAS:528:DC%2BD3MXotFanu7o%3D
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 5969319
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- PubMed
- 11758918
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed