ArticleThe protein journal2005
Molecular cloning and expression of an alpha-amylase inhibitor from rye with potential for controlling insect pests.
Article in The protein journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 28 citations in OpenAlex.
- Exploring Plant α-Amylase Inhibitors: Mechanisms and Potential Application for Insect Pest Control.Biotechnology journal · 2025Review
- Life Table Parameters and Digestive Enzyme Activity ofInsects · 2022Article
- Structure, Function and Protein Engineering of Cereal-Type Inhibitors Acting on Amylolytic Enzymes.Frontiers in molecular biosciences · 2022Review
- Midgut Genes Knockdown by Oral dsRNA Administration Produces a Lethal Effect on Cotton Boll Weevil.Neotropical entomology · 2021Article
- Transgenic Cotton Plants Expressing Cry1Ia12 Toxin Confer Resistance to Fall Armyworm (Spodoptera frugiperda) and Cotton Boll Weevil (Anthonomus grandis).Frontiers in plant science · 2016Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alpha-amylase inhibitors have important roles in plant defense mechanisms, particularly against insects, and several of these inhibitors have been expressed in different crops to increase their resistance to particular insects. In this work, we report the cloning and expression of a gene encoding for a new alpha-amylase inhibitor (BIII) from rye (Secale cereale) seeds. The BIII gene contains 354 nucleotides that encode for 118 amino acids sequence. A 313 bp fragment of the gene was expressed in Escherichia coli and resulted in a functional inhibitor that reduced the activity of alpha-amylases of larvae of the coleopteran pests Acanthoscelides obtectus, Zabrotess subfasciatus and Anthonomus grandis. In contrast, the inhibitor did not inhibit the activity of porcine pancreatic alpha-amylase. Although the amino acid sequence of BIII showed high identity with those of bifunctional inhibitors, the recombinant protein was unable to inhibit trypsin-like serine proteinases. The effects of recombinant BIII were evaluated in vivo against A. grandis. When first instar larvae were reared on an artificial diet containing four different concentrations of BIII, a reduction in larval weight and a mortality of 83% were observed at the highest concentration.
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