Non-specific lipid transfer proteins (nsLTPs) are small proteins abundant in plants, which function in transferring phospholipids and galactolipids across the membrane. nsLTPs also play a key role in plant resistance to biotic and abiotic stresses, growth and development, as well as in sexual reproduction, seed development, and germination. In addition, these proteins have previously been identified as food allergens. In the present study, we carried out a molecular and functional comparative characterisation of 25 sequences of nsLTPs of lupin legumes and other species. Extensive analysis was carried out; including comparison of databases, phylogeny, physical–chemical properties, functional properties of post-translational modifications, protein structure conservation, 2-D and 3D modelling, functional interaction analysis, and allergenicity including identification of IgE, T-cell, and B-cell binding epitopes. The results indicated that particular structural features of nsLTPs are essential to the functionality of these proteins, high level of structural stability and conservation. Information about different functional interactions between nsLTPs and ligands showed that nsLTPs can accommodate several of them with different structure; and that the relationship between structure and allergenicity was investigated through the identification of epitopes susceptible of being involved in cross-reactivity between species of the Fabaceae family.
Food allergies due to eating habits, pollution, and other factors are a growing problem in Western nations as well as developing countries. Symptoms of food allergies include changes in the respiratory and digestive systems. Legumes are a potential solution to the enormous demands for healthy, nutritive, and sustainable food. However, legumes also contain families of proteins that can cause food allergies. Some of these legumes include peanut, pea, chickpea, soy, and lupine. It has been shown that processing can alter the allergenicity of legumes since thermic and enzymatic resistance can affect these properties. Cross-reactivity (CR) is an allergy feature of some allergen proteins when the immune system recognizes part of the common share sequences (epitopes) in these allergic proteins. The research about molecular allergy includes comparisons of immunoglobulin E (IgE) and T-cell epitopes, assessment of three-dimensional structure and comparison of secondary structure elements, post-transduction modifications analysis by bioinformatic approach, and post-transduction modifications affecting epitopes properties may facilitate molecular tools to predict protein allergic behavior establishing prevention measurements that could promote the use of legumes and other seeds. This chapter provides an overview of the structural features of the main allergen proteins from legumes and their allergenic potential.
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