Antigenic Structural Similarity as a Predictor for Antibody Cross-Reactivity

Christopher A. Beaudoin, T. Blundell
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引用次数: 0

Abstract

Antibodies are an essential component of the adaptive immune system that function to neutralize foreign invaders, such as bacterial and parasitic pathogens. However, B-cell epitopes remain difficult to predict due to their general indistinguishability from other protein regions. Epitope prediction tools in the past have largely relied on amino acid sequence similarity; however, implementing three-dimensional protein structure analyses into the epitope prediction algorithms has been shown to increase detection accuracy. Furthermore, structural comparisons between antigenic proteins for their potential to bind cross-reactive antibodies have not been explored extensively in the literature. Recent studies have pointed to the utility of looking at shared epitope structures in predicting antibody crossreactivity, which may shed light on cross-immunity between infectious pathogens and autoimmune diseases induced after infection. Thus, herein, the potential impact of including structural similarity comparisons in detecting shared epitopes is discussed. With the large amount of structural information being determined by three-dimensional computational protein modelling methods, the ability to perform these analyses is becoming more feasible.
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抗原结构相似性作为抗体交叉反应性的预测因子
抗体是适应性免疫系统的重要组成部分,其功能是中和外来入侵者,如细菌和寄生病原体。然而,由于b细胞表位与其他蛋白质区域一般难以区分,因此仍然难以预测。过去的表位预测工具主要依赖于氨基酸序列相似性;然而,在表位预测算法中实施三维蛋白质结构分析已被证明可以提高检测精度。此外,抗原蛋白结合交叉反应抗体的潜力的结构比较尚未在文献中广泛探讨。最近的研究指出,观察共享表位结构在预测抗体交叉反应性方面的效用,这可能有助于揭示感染性病原体与感染后诱导的自身免疫性疾病之间的交叉免疫。因此,本文讨论了包括结构相似性比较在内的检测共享表位的潜在影响。随着三维计算蛋白质建模方法确定了大量的结构信息,执行这些分析的能力变得更加可行。
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