ArticleFoods (Basel, Switzerland)2021
Mapping B-Cell Epitopes for Nonspecific Lipid Transfer Proteins of Legumes Consumed in India and Identification of Critical Residues Responsible for IgE Binding.
Article in Foods (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 1 synthesis or guideline pooled it, 5 citations in OpenAlex.
- A review of the toxicological effects and allergenic potential of emerging alternative protein sources.Comprehensive reviews in food science and food safety · 2025Pooled it
- A Review of Allergen Characteristics from Major Plant Allergenic Foods.Foods (Basel, Switzerland) · 2026Review
- A Human Monoclonal Antibody Displays Promiscuous Binding to Multiple Type 1 nsLTP Allergens.Journal of investigational allergology & clinical immunology · 2026Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Nonspecific lipid transfer proteins (nsLTPs) have been categorized as panallergens and display widespread occurrence across plant-kingdom. Present study, investigated B-cell epitopes for LTPs from chickpea, mung-bean, cowpea, pigeon-pea, and soybean via in silico methods. In-silico predicted regions were evaluated for epitope-conservancy and property-based peptide similarity search by different allergen databases. Additionally, the in-silico predicted regions were compared with the experimentally validated epitopes of peach-LTP. Sequence-homology studies showed that chickpea and mung-bean LTPs shared significant homology, i.e., >70% and >60%, respectively, with other LTP allergens from lentil, garden-pea, peanut, etc. Phylogenetic-analysis also showed chickpea and mung-bean LTPs to be closely related to allergenic LTPs from lentil and peanut, respectively. Epitope-conservation analysis showed that two of the predicted B-cell epitopic regions in chickpea and mung-bean LTPs were also conserved in other allergenic LTPs from peach, peanut, garden-pea, lentil, and green-bean, and might serve as conserved B-cell epitopes of the LTP protein family. Property-distance index values for chickpea and mung-bean LTPs also showed that most of the epitopes shared similarity with the reported allergens like-lentil, peanut, apple, plum, tomato, etc. Present findings, may be explored for identification of probable allergenicity of novel LTPs, on the basis of the reported conserved B-cell epitopes, responsible for potential cross-reactivity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.