Literature DB >> 11856298

Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases.

Octávio L Franco1, Daniel J Rigden, Francislete R Melo, Maria F Grossi-De-Sá.   

Abstract

Insect pests and pathogens (fungi, bacteria and viruses) are responsible for severe crop losses. Insects feed directly on the plant tissues, while the pathogens lead to damage or death of the plant. Plants have evolved a certain degree of resistance through the production of defence compounds, which may be aproteic, e.g. antibiotics, alkaloids, terpenes, cyanogenic glucosides or proteic, e.g. chitinases, beta-1,3-glucanases, lectins, arcelins, vicilins, systemins and enzyme inhibitors. The enzyme inhibitors impede digestion through their action on insect gut digestive alpha-amylases and proteinases, which play a key role in the digestion of plant starch and proteins. The natural defences of crop plants may be improved through the use of transgenic technology. Current research in the area focuses particularly on weevils as these are highly dependent on starch for their energy supply. Six different alpha-amylase inhibitor classes, lectin-like, knottin-like, cereal-type, Kunitz-like, gamma-purothionin-like and thaumatin-like could be used in pest control. These classes of inhibitors show remarkable structural variety leading to different modes of inhibition and different specificity profiles against diverse alpha-amylases. Specificity of inhibition is an important issue as the introduced inhibitor must not adversely affect the plant's own alpha-amylases, nor the nutritional value of the crop. Of particular interest are some bifunctional inhibitors with additional favourable properties, such as proteinase inhibitory activity or chitinase activity. The area has benefited from the recent determination of many structures of alpha-amylases, inhibitors and complexes. These structures highlight the remarkable variety in structural modes of alpha-amylase inhibition. The continuing discovery of new classes of alpha-amylase inhibitor ensures that exciting discoveries remain to be made. In this review, we summarize existing knowledge of insect alpha-amylases, plant alpha-amylase inhibitors and their interaction. Positive results recently obtained for transgenic plants and future prospects in the area are reviewed.

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Year:  2002        PMID: 11856298     DOI: 10.1046/j.0014-2956.2001.02656.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  65 in total

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Journal:  J Mol Evol       Date:  2006-05-25       Impact factor: 2.395

2.  Genomic and functional characterization of coleopteran insect-specific α-amylase inhibitor gene from Amaranthus species.

Authors:  Amey J Bhide; Sonal M Channale; Yashpal Yadav; Kabita Bhattacharjee; Pankaj K Pawar; V L Maheshwari; Vidya S Gupta; Sureshkumar Ramasamy; Ashok P Giri
Journal:  Plant Mol Biol       Date:  2017-04-12       Impact factor: 4.076

Review 3.  The superfamily of thaumatin-like proteins: its origin, evolution, and expression towards biological function.

Authors:  Jun-Jun Liu; Rona Sturrock; Abul K M Ekramoddoullah
Journal:  Plant Cell Rep       Date:  2010-03-05       Impact factor: 4.570

4.  Templating α-amylase peptide inhibitors with organotin compounds.

Authors:  Fernando Porcelli; Cristina Olivieri; Larry R Masterson; Yi Wang; Gianluigi Veglia
Journal:  J Biol Inorg Chem       Date:  2011-07-07       Impact factor: 3.358

5.  The starch-bound alpha-amylase/trypsin-inhibitors in Avena.

Authors:  Laura Gazza; Gloria Gazzelloni; Federica Taddei; Arianna Latini; Vera Muccilli; Michela Alfieri; Salvatore Conti; Rita Redaelli; Norberto E Pogna
Journal:  Mol Genet Genomics       Date:  2016-08-05       Impact factor: 3.291

6.  Effect of betulin-containing extract from birch tree bark on α-amylase activity in vitro and on weight gain of broiler chickens in vivo.

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7.  Protein:Carbohydrate Ratios in the Diet of Gypsy Moth Lymantria dispar Affect its Ability to Tolerate Tannins.

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Journal:  J Chem Ecol       Date:  2020-02-14       Impact factor: 2.626

8.  Digestion-related proteins in the tobacco hornworm, Manduca sexta.

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Journal:  Insect Biochem Mol Biol       Date:  2020-08-27       Impact factor: 4.714

9.  Purification of a novel α-amylase inhibitor from local Himalayan bean (Phaseolus vulgaris) seeds with activity towards bruchid pests and human salivary amylase.

Authors:  Mridu Gupta; Pratima Sharma; Amarjit K Nath
Journal:  J Food Sci Technol       Date:  2012-02-09       Impact factor: 2.701

Review 10.  Protease inhibitors from plants with antimicrobial activity.

Authors:  Jin-Young Kim; Seong-Cheol Park; Indeok Hwang; Hyeonsook Cheong; Jae-Woon Nah; Kyung-Soo Hahm; Yoonkyung Park
Journal:  Int J Mol Sci       Date:  2009-06-23       Impact factor: 6.208

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