Inhibitory specificity and insecticidal selectivity of alpha-amylase inhibitor from Phaseolus vulgaris
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
15649508
DOI
10.1016/j.phytochem.2004.11.001
PII: S0031-9422(04)00589-8
Knihovny.cz E-zdroje
- MeSH
- alfa-amylasy antagonisté a inhibitory MeSH
- Caenorhabditis elegans enzymologie MeSH
- fazol chemie MeSH
- Helix (hlemýždi) enzymologie MeSH
- hmyz enzymologie MeSH
- houby enzymologie MeSH
- insekticidy chemie farmakologie MeSH
- molekulární modely MeSH
- molekulární sekvence - údaje MeSH
- Oligochaeta enzymologie MeSH
- rostlinné lektiny chemie farmakologie MeSH
- roztoči enzymologie MeSH
- sekvence aminokyselin MeSH
- substrátová specifita MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- alfa-amylasy MeSH
- alpha-amylase inhibitor, Phaseolus vulgaris MeSH Prohlížeč
- insekticidy MeSH
- rostlinné lektiny MeSH
The primary structure and proteolytic processing of the alpha-amylase isoinhibitor alpha AI-1 from common bean (Phaseolus vulgaris cv. Magna) was determined by protein chemistry techniques. The inhibitory specificity of alphaAI-1 was screened with a panel of the digestive alpha-amylases from 30 species of insects, mites, gastropod, annelid worm, nematode and fungal phytopathogens with a focus on agricultural pests and important model species. This in vitro analysis showed a selective inhibition of alpha-amylases from three orders of insect (Coleoptera, Hymenoptera and Diptera) and an inhibition of alpha-amylases of the annelid worm. The inhibitory potential of alphaAI-1 against several alpha-amylases was found to be modulated by pH. To understand how alphaAI-1 discriminates among closely related alpha-amylases, the sequences of the alpha-amylases sensitive, respectively, insensitive to alphaAI-1 were compared, and the critical determinants were localized on the spatial alpha-amylase model. Based on the in vitro analysis of the inhibitory specificity of alphaAI-1, the in vivo activity of the ingested alphaAI-1 was demonstrated by suppression of the development of the insect larvae that expressed the sensitive digestive alpha-amylases. The first comprehensive mapping of alphaAI-1 specificity significantly broadens the spectrum of targets that can be regulated by alpha-amylase inhibitors of plant origin, and points to potential application of these protein insecticides in plant biotechnologies.
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