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J Biomol Struct Dyn


Title:Herbivory-inducible lipid-transfer proteins (LTPs) of Cicer arietinum as potential human allergens
Author(s):Negi H; Saxena H; Singh IK; Singh A;
Address:"Department of Botany, Hans Raj College, University of Delhi, Delhi, India. Department of Biological Sciences, University of South Carolina, Columbia, SC, USA. Institute of Plant Breeding, Genetics and Genomics, University of Georgia, Griffin, GA, USA. Department of Zoology, Deshbandhu College, University of Delhi, New Delhi, India. J C Bose Centre for Plant Genomics, Hansraj College, University of Delhi, Delhi, India. Delhi School of Climate Change and Sustainability, Institution of Eminence, Maharishi Karnad Bhawan, University of Delhi, Delhi, India"
Journal Title:J Biomol Struct Dyn
Year:2023
Volume:20230126
Issue:
Page Number:1 - 17
DOI: 10.1080/07391102.2023.2169353
ISSN/ISBN:1538-0254 (Electronic) 0739-1102 (Linking)
Abstract:"Lipid-transfer proteins (LTPs) are lipid-binding small proteins, ubiquitously distributed amongst plant kingdom. Apart from their involvement in plant defense, it has also been discovered that they induce allergic reactions in humans. A plethora of LTPs have been identified in vegetables, fruits, pollens, nuts, and latex, among which Pru p 3, a LTP allergen from peach fruit, is extensively studied and exhibits cross-reactivity with potential allergens from different species. In Cicer arietinum, a family of LTPs (CaLTPs) has been identified and their importance in plant defense during Helicoverpa armigera-infestation has been recognized. However, the determination of the allergenicity potential of CaLTPs has not been attempted. In this study, we aim to decipher the allergenicity potential of defense-related CaLTPs. The allergenicity potential prediction, and identification of B-cell epitope binding regions showed that the CaLTPs had conserved domains and B-cell epitopes in the same regions as Prup3 (a marker allergen for LTPs). Using molecular docking and simulations, we observed that the CaLTPs successfully interacted with the Immunoglobin E(IgE)with docking energies ranging from -315.5 to -268.4 and the structures were stabilized within 10 ns of simulation. Through this study, we intend to embellish our present knowledge and understanding of the sensitization and allergenicity potential of CaLTPs.Communicated by Ramaswamy H. Sarma"
Keywords:Helicoverpa armigera Lipid-transfer proteins (LTPs) allergenicity potential chickpea human allergens;
Notes:"PublisherNegi, Harshita Saxena, Harshita Singh, Indrakant K Singh, Archana eng England 2023/01/28 J Biomol Struct Dyn. 2023 Jan 26:1-17. doi: 10.1080/07391102.2023.2169353"

 
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