REQUIMTE-LAQV, Faculdade de Farmácia, Universidade do Porto, Rua de Jorge Viterbo Ferreira, 228, 4050-313, Porto, Portugal.
Curr Allergy Asthma Rep. 2024 Nov;24(11):609-617. doi: 10.1007/s11882-024-01173-7. Epub 2024 Sep 20.
A holistic perspective on how physicochemical properties modulate the allergenicity of proteins has recently been performed for food allergens, launching the challenge of a similar analysis for aeroallergens. After a first review on aeroallergen classification into protein families (Part 1), this second part (Part 2) will exploit the impact of physicochemical properties (abundance/biological function, protein structure/presence of post-translational modifications, ligand/cofactor/lipid-binding) on inhalant protein allergenicity.
The abundance linked to biological function is correlated with increased allergenic risk for most protein families, while the loss of structural integrity with consequent destruction of conformational epitopes is well linked with decreased allergenicity. Ligand-binding effect totally depends on the ligand type being highly variable among aeroallergens. Knowledge about the physicochemical properties of aeroallergens is still scarce, which highlights the need for research using integrated approaches (in silico and experimental) to generate and analyze new data on known/new aeroallergens.
最近对食物过敏原的物理化学性质如何调节蛋白质的变应原性进行了全面的研究,这对空气过敏原的类似分析提出了挑战。在对空气过敏原进行蛋白家族分类的第一部分综述(第一部分)之后,这第二部分(第二部分)将探讨物理化学性质(丰度/生物学功能、蛋白结构/是否存在翻译后修饰、配体/辅助因子/脂质结合)对吸入性蛋白变应原性的影响。
大多数蛋白家族中,与生物功能相关的丰度与变应原性风险的增加相关,而结构完整性的丧失以及随之而来的构象表位的破坏与变应原性的降低密切相关。配体结合效应完全取决于配体类型,在空气变应原中具有高度可变性。关于空气变应原的物理化学性质的知识仍然匮乏,这凸显了需要使用综合方法(包括计算机模拟和实验)来生成和分析已知/新空气变应原的新数据。