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Mechanism of entomotoxicity of the plant lectin from Hippeastrum hybrid (Amaryllis) in Spodoptera littoralis larvae.
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Plant lectins have received a lot of attention because of their insecticidal properties. When orally administered in artificial diet or in transgenic plants, lectins provoke a wide range of detrimental effects, including alteration of the digestive enzyme machinery, fecundity drop, reduced feeding,
X-ray structure solution of amaryllis lectin by molecular replacement with only 4% of the total diffracting matter.
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It is often the case that analogous proteins from different species crystallize in a different form. These structures can usually be easily solved by the molecular-replacement (MR) technique, as the protein folding is very often conserved. However, the results from MR become more uncertain as the
Crystallization and preliminary X-ray studies on the mannose-specific lectin from Amaryllis bulbs.
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Affinity-purified amaryllis lectin was used to grow single crystals using the hanging-drop method. The space group was found to be C2 with unit-cell dimensions a = 73.4 (1), b = 100.3 (1), c = 62.2 (1) A and beta = 137.3 (2) degrees. Data to 2.25 A resolution have been recorded and solution of the
Carbohydrate-binding specificity of the daffodil (Narcissus pseudonarcissus) and amaryllis (Hippeastrum hybr.) bulb lectins.
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The carbohydrate binding specificity of the daffodil (Narcissus pseudonarcissus; NPA) and amaryllis (Hippeastrum hybr.; HHA) lectins, isolated from extracts of their bulbs by affinity chromatography on immobilized mannose, was studied by quantitative precipitation, sugar hapten inhibition, and
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