Kanduc D
Department of Biochemistry & Molecular Biology Ernesto Quagliariello, University of Bari, Italy.
Curr Pharm Des. 2008;14(3):289-95. doi: 10.2174/138161208783413257.
Although a high number of allergenic peptide epitopes has been experimentally identified and defined, the molecular basis and the precise mechanisms underlying peptide allergenicity are unknown. This issue was analyzed exploring the relationship between peptide allergenicity and sequence similarity to the human proteome. The structured analysis of the data reported in literature put into evidence that the most part of IgE-binding epitopes are (or harbor) pentapeptide unit(s) with no/low similarity to the human proteome, this way suggesting that no or low sequence similarity to the host proteome might represent a minimum common denominator identifying allergenic peptides. The present literature analysis might be of relevance in devising and designing short amino acid modules to be used for blocking pathogenic IgE.
尽管已经通过实验鉴定并定义了大量的变应原性肽表位,但肽变应原性的分子基础和确切机制尚不清楚。通过探索肽变应原性与与人蛋白质组的序列相似性之间的关系来分析这个问题。对文献中报道的数据进行结构化分析表明,大多数IgE结合表位是(或含有)与人蛋白质组无/低相似性的五肽单元,这表明与宿主蛋白质组无或低序列相似性可能是识别变应原性肽的一个最小共同特征。目前的文献分析可能与设计用于阻断致病性IgE的短氨基酸模块相关。