Food Science Program, College of Agriculture and Food Sciences, Florida A&M University, 1740 S. Martin Luther King Jr. Blvd. Room 305-A Perry Paige South, Tallahassee, FL 32307, USA.
Center for Viticulture and Small Fruits Research, College of Agriculture and Food Sciences, Florida A&M University, 6505 Mahan Drive, Tallahassee, FL 32317, USA.
Genes (Basel). 2022 Aug 17;13(8):1464. doi: 10.3390/genes13081464.
Fruit allergens are proteins from fruits or pollen that cause allergy in humans, an increasing food safety concern worldwide. With the globalization of food trade and changing lifestyles and dietary habits, characterization and identification of these allergens are urgently needed to inform public awareness, diagnosis and treatment of allergies, drug design, as well as food standards and regulations. This study conducted a phylogenetic reconstruction and protein clustering among 60 fruit and pollen allergens from 19 species, and analyzed the clusters, in silico, for cross-reactivity (IgE), 3D protein structure prediction, transmembrane and signal peptides, and conserved domains and motifs. Herein, we wanted to predict the likelihood of their interaction with antibodies, as well as cross-reactivity between the many allergens derived from the same protein families, as the potential for cross-reactivity complicates the management of fruit allergies. Phylogenetic analysis classified the allergens into four clusters. The first cluster ( = 9) comprising pollen allergens showed a high risk of cross-reactivity between eight allergens, with Bet v1 conserved domain, but lacked a transmembrane helix and signal peptide. The second ( = 10) cluster similarly suggested a high risk of cross-reactivity among allergens, with Prolifin conserved domain. However, the group lacked a transmembrane helix and signal peptide. The third ( = 13) and fourth ( = 29) clusters comprised allergens with significant sequence diversity, predicted low risk of cross-reactivity, and showed both a transmembrane helix and signal peptide. These results are critical for treatment and drug design that mostly use transmembrane proteins as targets. The prediction of high risk of cross-reactivity indicates that it may be possible to design a generic drug that will be effective against the wide range of allergens. Therefore, in the past, we may have avoided the array of fruit species if one was allergic to any one member of the cluster.
水果过敏原是来自水果或花粉的蛋白质，会引起人类过敏，这是一个日益受到全球关注的食品安全问题。随着食品贸易的全球化以及生活方式和饮食习惯的改变，迫切需要对这些过敏原进行特征描述和鉴定，以便为公众意识、过敏诊断和治疗、药物设计以及食品标准和法规提供信息。本研究对来自 19 个物种的 60 种水果和花粉过敏原进行了系统发育重建和蛋白质聚类分析，并对这些聚类进行了计算机分析，以评估其交叉反应性（IgE）、3D 蛋白质结构预测、跨膜和信号肽以及保守结构域和基序。在此，我们希望预测它们与抗体相互作用的可能性，以及来自同一蛋白质家族的许多过敏原之间的交叉反应性，因为这种交叉反应性增加了水果过敏的管理难度。系统发育分析将过敏原分为四个聚类。第一聚类（ = 9）包含花粉过敏原，这 8 种过敏原之间存在高交叉反应性风险，具有 Bet v1 保守结构域，但缺乏跨膜螺旋和信号肽。第二聚类（ = 10）同样提示过敏原之间存在高交叉反应性风险，具有 Prolifin 保守结构域。然而，该组缺乏跨膜螺旋和信号肽。第三聚类（ = 13）和第四聚类（ = 29）包含具有显著序列多样性的过敏原，预测交叉反应性风险较低，并且都具有跨膜螺旋和信号肽。这些结果对于治疗和药物设计至关重要，因为这些治疗和药物设计大多使用跨膜蛋白作为靶点。高交叉反应性风险的预测表明，有可能设计出一种通用药物，对广泛的过敏原都有效。因此，在过去，如果对聚类中的任何一个成员过敏，我们可能会避免食用一系列水果。
