异源抗体对接方法预测流感病毒血凝素B细胞构象表位

The feasibility analysis of using heterogenous antibody docking for predicting the B cell epitope of influenza virus hemagglutinin

为了对异源抗体对接方法预测流感病毒血凝素B细胞构象表位的可行性进行分析,本研究基于蛋白质相互作用界面的形状互补理论,使用异源抗体(来自于抗原抗体复合物1G9M、1RVF、1TPX、1NCA、1A2Y)的晶体结构同流感病毒血凝素(A/Aichi/2/68(H3N2))的晶体结构进行刚性分子对接,通过计算B细胞表位的预测表面和实际表面C-α原子之间的RSMD以及表位氨基酸的准确率,分析用异源抗体探测出血凝素B细胞表位的可能性。结果表明,不同的异源抗体均可结合到A/Aichi/2/68(H3N2)的已知B细胞表位,最佳的对接构象与原晶体结构重叠后表位残基C-α原子的均方根偏差均小于0.6埃,表位氨基酸预测的准确性大于60%,说明异源抗体对接方法可以尝试用于B细胞构象表位的预测。

The influenza virus hemagglutinin （A/Aichi/2/68 （H3N2）） and the the non-influenza virus hemagglutinin antibody （from the antigen-antibody complexes） were docked based on the shape complementarities at protein-protein interfaces, and the possibility of using heterogenous antibody to detect the binding surface of the hemagglutinin antibody are analysed. The results showed that the C-α atoms RMSD calculation of interface residue was below 0.6 ℃ after superimposition, and 〉60 % residues at the antibody-binding site could be predicted. This method could be useful for prediction of B cell discontinuous epitopes.