1,720,977 research outputs found
Protease inhibitor gene transfer as a tool for an ecological and sustainable plant defence strategy
No full textEvolution of the nad3-rps12 gene cluster in angiosperm mitochondria: Comparison of edited and unedited sequences
No full textIdentification of isoformic genes coding for the allergenic lipid transfer protein (LTP) in plants
No full textAnalysis by phage display selection and site-directed retromutagenesis of the Mustard Trypsin Inhibitor 2 reactive site
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Characterization of the spinach Lhcb1 multigene family and its regulatory regions: possible involvement in environmental adaptation
No full textApplication of a genome walking method for the study of the spinach Lhcb1 multigene family
No full textMapping of 5' and 3'-ends of sunflower mitochondrial nad6 mRNAs reveals a very complex transcription pattern which includes primary transcripts lacking 5'-UTR
No full textCloning and characterization of maize chitinase A: a tough allergenic molecule. Gene diffusion among different maize races
No full textOverview of plant chitinases identified as food allergens
No full textFood allergies are induced by proteins belonging to a limited number of families. Unfortunately, relationships between protein structure and capacity to induce the immune response have not been completely clarified yet, which precludes possible improvements in the diagnosis, prevention, and therapy of allergies. Plant chitinases constitute a good example of food allergenic proteins for which structural analysis of allergenicity has only been carried out partially. In plants, there are at least five structural classes of chitinases plus a number of chitinase-related polypeptides. Their allergenicity has been mostly investigated for chitinases of class I, due to both their higher prevalence among plant chitinases and by the high structural similarity between their substrate-binding domain and hevein, a well-known allergen present in the latex of rubber trees. Even if allergenic molecules have been identified for at least three other classes of plant chitinases, the involvement of the different structural motifs in the allergenicity of molecules has been disregarded so far. In this review, we provide a structurally based catalog of plant chitinases investigated for allergenicity, which could be a useful base for further studies aimed at better clarifying the structure-allergenicity relationships for this protein family
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