TAILIEUCHUNG - Báo cáo khoa học: Characterization of a high-affinity binding site for the pea albumin 1b entomotoxin in the weevil Sitophilus

The toxicity of the pea albumin 1b (PA1b), a 37 amino-acid peptide extracted from pea seeds, for cereal weevils (Sito-philus oryzae, Sitophilus granariusandSitophilus zeamais) was recently mechanism of action of this new entomotoxin is still unknown and potentially involves a target protein in the insect work describes the characterization of a high-affinity binding site for PA1b in a microsomal fraction PA1b was labeled to a high specific radioactivity ( CiÆmmol )1 )using 125 I, and the iodinated ligand was found to be biologically of this ligand to the microsomal fraction ofS. . | Eur. J. Biochem. 270 2429-2435 2003 FEBS 2003 doi Characterization of a high-affinity binding site for the pea albumin 1b entomotoxin in the weevil Sitophilus Frederic Gressent Isabelle Rahioui and Yvan Rahbe UMR 0203 INRA INSA de Lyon BF2I Biologie Fonctionnelle Insectes et Interactions INSA Batiment Louis Pasteur Villeurbanne France The toxicity of the pea albumin 1b PA1b a 37 amino-acid peptide extracted from pea seeds for cereal weevils Sitophilus oryzae Sitophilus granarius and Sitophilus zeamais was recently discovered. The mcchnnism of cciion fl this new entomotoxin is still unknown and potentially involves a target protein in the insect tissues. ThÍS work describes the characterization of a high-affinity binding site for PA1b in a microsomal fraction of Sitophilus spp. 6 11 1 . Purified PA1b was labeled to a high specific radioactivity c. 900 Ci-mmol-1 using 125I and the iodinated ligand was found to be biologically active. Binding of thís i g rmd to the microsomal fraction of S. oryzae extract was found to be saturable and reversible with an affinity Kd of DM and a high maximal binding capacity Bmax of 40 pmol-mg-1 of protein. A bindíng she díspkiyíng simitar ct a Llctel isiis. s was detectable in the five susceptible weevils strains tested as well as in the pea aphid or in the fruit fly. However no binding activity was detectable in extracts from four S. oryzae strains previously shown to be resistant to the toxin through a recessive monogenic mechanism. Therefore. we suggest that this binding site might be involved in the mechanism of action of PA1b. Keywords binding site pea albumin 1b Sitophilus cystine-knot leginsulin. The cereal weevils Sitophilus oryzae Sitophilus granarius and Sitophilus zeamais are major pests of stored grains. At present the use of chemical insecticides is the main answer to the damage caused by stored product pests inducing ecotoxicity problems and the occurrence of resistance within insect .

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