Serine protease inhibitors in plants: nature’s arsenal crafted for insect predators

Jamal, Farrukh; Pandey, Prabhash Kumar; Singh, Diksha; Khan, M. Firoze

doi:10.1007/s11101-012-9231-y

Cited by 89 publications

(71 citation statements)

References 235 publications

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“…Similar to our findings, corn meal has shown an inhibitory effect on alkaline proteases (specifically on trypsin) (Jamal et al 2012). As proteases inhibitors were detected in kernel oil palm meal (KOPM), their presence may explain partly the growth reduction found with O. aureus when fed KOPM at 10 % or higher levels (Iluyemi et al 2010).…”

Section: Alkaline Proteolytic Activitysupporting

confidence: 88%

In vitro digestibility and proteases inhibitory effect of several feedstuffs for Parachromis dovii juveniles and P. dovii hybrid larvae

Chavarría¹,

Álvarez‐González

Brais-Medina³

et al. 2016

Fish Physiol Biochem

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Parachromis dovii, a native cichlid from Costa Rica, is highly appreciated for its size and flesh quality. Further, P. dovii easily accept inert feed from the beginning of exogenous feeding; however, its growth is low compared to live food. For this reason, evaluation of several feedstuffs using two in vitro techniques was done. The quantification of the in vitro inhibitory effect of seven plant ingredients on the alkaline protease activity was done using enzymatic extracts from larvae samples of 6, 15, 22 and 30 days after hatching (DAH). The in vitro alkaline digestibility assays were run for six protein sources (from animal and plant origin) using the enzymatic extract from larvae 30 DAH. Independent of fish age, all plant feedstuffs reduced alkaline digestive proteases activity; however, the wheat flour (14.1 % at 6 DAH, 33.4 % at 15 DAH) and broken rice meal (51.6 % at 22 DAH) showed the lowest inhibition percentage of alkaline digestive activity, whereas the highest inhibition percentage was found with soybean and palm kernel meals (92.5 % at 30 DAH and 87.4 %, respectively) (P < 0.05). The alkaline proteases inhibition percentage of feedstuffs varied during larvae ontogeny. From six protein dietary sources tested, tankage and fish meal presented the highest in vitro digestibility values, 113.9 and 74.9 %, respectively. Contrary, the lowest digestibility was found for blood and soybean meals (38.07 and 19.82 %, respectively).

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Section: Alkaline Proteolytic Activitysupporting

confidence: 88%

In vitro digestibility and proteases inhibitory effect of several feedstuffs for Parachromis dovii juveniles and P. dovii hybrid larvae

Chavarría¹,

Álvarez‐González

Brais-Medina³

et al. 2016

Fish Physiol Biochem

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“…PIs are widely distributed in plant seeds, where they act as antinutritional agents, especially in insects where they inhibit midgut proteinases [7, 8] by reacting with cognate enzymes and binding in a canonical fashion to catalytic sites [9]. The presence of an exposed loop in all canonical inhibitors simulates a rapid binding and a slow dissociation mechanism [10].…”

Section: Introductionmentioning

confidence: 99%

A Nonhost Peptidase Inhibitor of ~14 kDa fromButea monosperma(Lam.) Taub. Seeds Affects Negatively the Growth and Developmental Physiology ofHelicoverpa armigera

Pandey

Singh

et al. 2014

Biochemistry Research International

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Helicoverpa armigera is one of the major devastating pests of crop plants. In this context a serine peptidase inhibitor purified from the seeds of Butea monosperma was evaluated for its effect on developmental physiology of H. armigera larvae. B. monosperma peptidase inhibitor on 12% denaturing polyacrylamide gel electrophoresis exhibited a single protein band of ~14 kDa with or without reduction. In vitro studies towards total gut proteolytic enzymes of H. armigera and bovine trypsin indicated measurable inhibitory activity. B. monosperma peptidase inhibitor dose for 50% mortality and weight reduction by 50% were 0.5% w/w and 0.10% w/w, respectively. The IC50 of B. monosperma peptidase inhibitor against total H. armigera gut proteinases activity was 2.0 µg/mL. The larval feeding assays suggested B. monosperma peptidase inhibitor to be toxic as reflected by its retarded growth and development, consequently affecting fertility and fecundity of pest and prolonging the larval-pupal duration of the insect life cycle of H. armigera. Supplementing B. monosperma peptidase inhibitor in artificial diet at 0.1% w/w, both the efficiencies of conversion of ingested as well as digested food were downregulated, whereas approximate digestibility and metabolic cost were enhanced. The efficacy of Butea monosperma peptidase inhibitor against progressive growth and development of H. armigera suggest its usefulness in insect pest management of food crops.

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“…Ekspresinya diinduksi oleh respon pelukaan atau serangan hama dan patogen. Pada tanaman, inhibitor ini efektif dalam menekan proses metabolisme dalam percernaan hama serangga pertanian serta ramah lingkungan dan berkelanjutan (Jamal et al, 2013).…”

Section: Identifikasi Domain Dan Familiunclassified

Identifikasi famili gen putatif penyandi protease inhibitor dengan pendekatan in silico komparatif pada genom Hevea brasiliensis Muell. Arg (Identification of putative gene family encoding protease inhibitors by in silico comparative analysis in Hevea brasiliensis Muell. Arg genome)

Martiansyah¹,

Putranto²,

Khumaida³

2017

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Protease inhibitors (PIs) are small proteins that form complexes with proteases and inhibits their proteolytic activity. Its potential application as an antimicrobial agent has been studied. Most of PIs' molecule size is around 8-22 kDa depending on their protein families.To date, on the basis of sequence homologies of inhibitor domains, PIs have been classified into 48 families in all organisms. In plant, more than 13 families of PIs have been identified but they were not widely identified in the rubber tree (Hevea brasiliensis Muell.Arg). In the present study, 40 putative HbPI genes, designated as HbPI01 to HbPI36, were identified from whole-genome sequence of rubber tree clone Reyan 7-33-97 using 7453 scaffolds available online in NCBI with the accession code: LVXX01000000. Multiple sequence alignment using MUSCLE algorithm discovered seven conserved motifs (Motifs I-VII) among HbPIs. Phylogenetic analysis of 50 and 36 PI amino acid residues of 32 scaffolds containing putative PI genes from Arabidopsis thaliana and H. brasiliensis showed three clusters (families): LTP-I, SERPIN and LTP-II. LTP-I has 23 putative HbPI genes (HbPI05 to HbPI27) and 12 AtPI genes. SERPIN, a family member of serine protease inhibitor group, has 11 putative HbPI genes (HbPI01 to HbPI04 and HbPI28 to HbPI34) and 22 AtPI genes. LTP-II has 2 putative HbPI genes (HbPI35 to HbPI36) and 16 AtPI genes. In conclusion, this work provides valuable information for further functional characterization of HbPI genes in H. brasiliensis.[Key words: protease inhibitor, genome-wide, scaffold, in silico, Hevea brasiliensis]. AbstrakProtease inhibitor (PI) merupakan protein yang membentuk kompleks dengan protease dan menghambat aktivitas proteolitik dari enzim tersebut. Potensi penggunaan protease inhibitor sebagai agensia antimikroba telah diketahui. Kebanyakan PI memiliki ukuran molekul sekitar 8-22 kDa bergantung pada familinya. Saat ini, PI dapat diklasifikasikan menjadi 48 famili di seluruh organisme berdasarkan kemiripan sekuen dari domain inhibitornya. Pada tanaman, lebih dari 13 famili PI telah diketahui tetapi pada tanaman karet (Hevea brasiliensis Muell.Arg) belum diidentifikasi. Pada penelitian ini, sebanyak 40 gen putatif penyandi PI (HbPI01 hingga HbPI36) telah berhasil diidentifikasi dari 7453 scaffold genom utuh tanaman karet klon Reyan 7-33-97 yang tersedia secara daring dengan kode aksesi LVXX01000000. Penjajaran sekuen menggunakan algoritma MUSCLE memper-lihatkan tujuh konservasi motif (Motif I-VIII) pada famili gen putatif HbPIs. Analisis pohon filogenetik dari tanaman Arabidopsis thaliana dan H. brasiliensis sebanyak 50 dan 36 sekuen residu asam amino dari 32 scaffold yang mengandung gen putatif PI menunjukkan adanya tiga klaster besar, yaitu famili LTP-I, SERPIN dan LTP-II. LTP-I terdiri dari 23 gen putatif HbPI (HbPI05 hingga HbPI27) dan 12 gen AtPI. SERPIN yang merupakan anggota kelas protease inhibitor serin terdiri dari 11 gen putatif HbPI (HbPI01hingga HbPI04 dan HbPI28 hingga HbPI34) dan 22 gen AtPI. LTP-II terdiri dari 2 gen putatif HbPI (HbPI35 hingga HbPI36) dan 16 gen AtPIs. Penelitian ini menghasilkan informasi penting untuk melakukan karakterisasi fungsional lebih mendalam pada gen HbPI tanaman karet ke depannya.[Kata kunci: protease inhibitor, genome-wide,scaffold, in silico, Hevea brasiliensis].

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Serine protease inhibitors in plants: nature’s arsenal crafted for insect predators

Cited by 89 publications

References 235 publications

In vitro digestibility and proteases inhibitory effect of several feedstuffs for Parachromis dovii juveniles and P. dovii hybrid larvae

In vitro digestibility and proteases inhibitory effect of several feedstuffs for Parachromis dovii juveniles and P. dovii hybrid larvae

A Nonhost Peptidase Inhibitor of ~14 kDa fromButea monosperma(Lam.) Taub. Seeds Affects Negatively the Growth and Developmental Physiology ofHelicoverpa armigera

Identifikasi famili gen putatif penyandi protease inhibitor dengan pendekatan in silico komparatif pada genom Hevea brasiliensis Muell. Arg (Identification of putative gene family encoding protease inhibitors by in silico comparative analysis in Hevea brasiliensis Muell. Arg genome)

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