Marini-Rapoport Orlee, Bhowmik Moumita, Keswani Tarun, Patil Sarita U
Center for Immunology and Inflammatory Diseases, Division of Rheumatology, Allergy, and Immunology, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Food Allergy Center, Massachusetts General Hospital, Boston, Massachusetts, USA.
Immunol Rev. 2025 Jul;332(1):e70042. doi: 10.1111/imr.70042.
B-cell epitope specificity on food allergens is highly relevant to understanding both the pathogenesis of IgE and IgG-mediated clinical tolerance after immunotherapy. The molecular binding interactions between the paratopes of antibodies and the epitopes of food allergens drive IgE-crosslinking, the subsequent activation of allergen effector cells, and the symptoms of systemic and life-threatening anaphylaxis. Various characteristics of allergen-specific IgE, such as high affinity and clonal diversity, can contribute to the persistence of food allergy and the severity of anaphylaxis upon allergen exposure. On the other hand, the induction of epitope-specific IgG antibodies in allergic individuals can inhibit IgE binding to food allergens. A subset of these can be neutralizing antibodies that effectively disrupt multiple allergen-IgE interactions to suppress effector responses. This review details the crucial role of epitope specificity and antibody clonality in both the pathogenesis of food allergy and in the development of clinical tolerance.
食物过敏原上的B细胞表位特异性对于理解免疫疗法后IgE介导和IgG介导的临床耐受性的发病机制都具有高度相关性。抗体互补位与食物过敏原表位之间的分子结合相互作用驱动IgE交联、随后过敏原效应细胞的激活以及全身性和危及生命的过敏反应症状。过敏原特异性IgE的各种特性,如高亲和力和克隆多样性,可导致食物过敏的持续存在以及接触过敏原时过敏反应的严重程度。另一方面,过敏个体中表位特异性IgG抗体的诱导可抑制IgE与食物过敏原的结合。其中一部分可以是中和抗体,它们能有效破坏多种过敏原-IgE相互作用以抑制效应反应。本综述详细阐述了表位特异性和抗体克隆性在食物过敏发病机制和临床耐受性发展中的关键作用。