INSECT PROTEASES, PLANT PROTEASE INHIBITORS, AND POSSIBLE PEST CONTROL
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Abstract Since the first observation that plants contained protease inhibitors, as identified by their ability to inhibit vertebrate enzymes, it has been postulated that the presence of these substances was related to their phytoprotective abilities. However the following assumptions (1) that phytophagous insects use trypsin, and (2) that ingested inhibitors disrupt digestive proteolysis in insects, have not been adequately tested. Identification of non-tryptic enzymes, cathepsin B, D, and H in phytophagous Coleoptera and unique trypsin-like enzymes in Lepidoptera, indicates insect proteases may differ from their vertebrate counterparts. Putative inhibitor proteins inhibited vertebrate trypsin and chymotrypsin in vitro but had no effect on the trypsin- or chymotrypsin-like activity from the insect midgut. Feeding experiments with the European corn borer, Ostrinia nubilalis (Hübner), indicate that ingestion of inhibitors may not disrupt digestive proteolysis in vivo and the vertebrate trypsin inhibitor in corn may be ineffective as a phytoprotective strategy for this insect. Limitations and implications of ingested inhibitors for future pest control may depend on the origin of the inhibitor, as well as the insect's response.Keywords:
Proteolysis
Ostrinia
Protease inhibitor (pharmacology)
Trypsin inhibitor
Trypsin inhibitor
Protease inhibitor (pharmacology)
Cysteine protease
Serine Proteinase Inhibitors
Serpin
MASP1
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Protease inhibitor (pharmacology)
Trypsin inhibitor
Pepsin
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국내에서 생산된 감자 중 세풍, 남서, 수미, 조풍 및 대서의 5가지 품종에 대하여 단백질 profile 및 아미노산 조성을 분석하였다. 총 질소함량은 1.27～1.64%이었으며, 남서가 높았고 수미가 낮게 나타났다. 아미노산 조성은 품종 간에 유의적인 차이가 있었다. 한편, 주요 감자 단백질은 papatin(40 kDa), trypsin inhibitor(20 kDa) 및 protease inhibitor(15 kDa)이었으며, 이들의 함량은 각각 22.16～25.81%, 25.22～20.91% 및 14.12～25.23%이었다. Papatin 함량은 조풍, 세풍, 수미감자가 높은 함량을 보인 반면, trypsin inhibitor는 조풍감자가 5.22%로 가장 낮은 함량을 보였다. Protease inhibitors인 20 kDa와 15 kDa를 합한 값은 24.7～35.0%이었으며, 세풍이 가장 적었고 조풍에 가장 많이 함유되어 있었다.
Trypsin inhibitor
Protease inhibitor (pharmacology)
Amino Acid Analysis
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Objective To establish an detecting method for protease inhibitors,especially for low-molecular-weight inhibitors.Methods Inhibitor samples were separated on a gelatin-SDS-PAGE in a Tris-Tricine buffer system.After electrophoresis,the gel was incubated with the target proteases to hydrolyze the background gelatin.The inhibitor bands,which were undigested by the target proteases,were stained.Results Low-molecular-weight inhibitor(pepstatin A) and larger inhibitor(soybean Bowman-Birk inhibitor) were demonstrated by this method and showed clear blue inhibitor bands in the white background.By this method,a trypsin inhibitor was detected from the seeds of Albizzia kalkora(Roxb.) Prain.Conclusion This method not only fit for inhibitors with different molecular mass,but fits for inhibitors with various species.Moreover,the trypsin inhibitor found in Albizzia kalkora is important for further research and overall exploration.
Tricine
Gelatin
Trypsin inhibitor
Protease inhibitor (pharmacology)
Bromelain
Molecular mass
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Ostrinia
European corn borer
Bacillus thuringiensis
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Plant protease inhibitors (PIs) are elements of a common plant defense mechanism induced in response to herbivores. The fall armyworm, Spodoptera frugiperda, a highly polyphagous lepidopteran pest, responds to various PIs in its diet by expressing genes encoding trypsins. This raises the question of whether the PI-induced trypsins are also inhibited by other PIs, which we posed as the hypothesis that Inga laurina trypsin inhibitor (ILTI) inhibits PI-induced trypsins in S. frugiperda. In the process of testing our hypothesis, we compared its properties with those of selected PIs, soybean Kunitz trypsin inhibitor (SKTI), Inga vera trypsin inhibitor (IVTI), Adenanthera pavonina trypsin inhibitor (ApTI), and Entada acaciifolia trypsin inhibitor (EATI). We report that ILTI is more effective in inhibiting the induced S. frugiperda trypsins than SKTI and the other PIs, which supports our hypothesis. ILTI may be more appropriate than SKTI for studies regarding adaptive mechanisms to dietary PIs.
Protease inhibitor (pharmacology)
Trypsin inhibitor
Fall armyworm
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Protease inhibitors of the Bowman-Birk (BBI) family are commonly found in plants and animals where they play a protective role against invading pathogens. Here, we report an atomic resolution (1Å) crystal structure of a peptide inhibitor isolated from a skin secretion of a Chinese bamboo odorous frog Huia versabilis (HV-BBI) in complex with trypsin. HV-BBI shares significant similarities in sequence with a previously described inhibitor from a diskless-fingered odorous frog Odorrana graham (ORB). However, the latter is characterized by more than a 16,000 fold higher Ki against trypsin than HV-BBI. Comparative analysis of trypsin cocrystal structures of HV-BBI and ORB and additionally that of Sunflower Trypsin Inhibitor (SFTI-1) together with accessory information on the affinities of inhibitor variants allowed us to pinpoint the inhibitor moiety responsible for the observed large difference in activity and also to define the extent of modifications permissible within the common protease-binding loop scaffold of BBI inhibitors. We suggest that modifications outside of the inhibitory loop permit the evolution of specificity toward different enzymes characterized by trypsin-like specificity. Proteins 2015; 83:582–589. © 2014 Wiley Periodicals, Inc.
Protease inhibitor (pharmacology)
Trypsin inhibitor
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Protease inhibitor (pharmacology)
Trypsin inhibitor
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Endopeptidase
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Ostrinia
Crambidae
European corn borer
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Protease inhibitor (pharmacology)
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