Phage-displayed peptides having antigenic similarities with porcine epidemic diarrhea virus (PEDV) neutralizing epitopes.

Phage-displayed peptides having antigenic similarities with porcine epidemic diarrhea virus (PEDV) neutralizing epitopes.
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DOI:
10.1016/j.virol.2006.04.027
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发表时间:
2006-10-10
期刊:
影响因子:
3.7
通讯作者:
Shin HJ
Shin HJ
中科院分区:
医学3区
文献类型:
--
作者:
Cruz DJ;Kim CJ;Shin HJ

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将七噬噬菌体随机肽库用于2C10,这是一种单克隆抗体,表现出对PEDV的中和活性。重组M13噬菌体显示了G3P次要涂层蛋白上显示肽SHRLP(Y/Q)(Y/Q)或GPRPVTH的重组噬菌体,在多个平盘后显示出与2C10(分别为70%和30%)的结合亲和力强(分别为70%和30%)。序列分析表明,这些肽与S蛋白的羧基末端发现的1368GPRLQPY1374相似。在中和抑制测定中,观察到与对应于PEDV S蛋白的C-末端内域的24-Mer合成肽竞争2C10的抗原结合位点,这证明了2C10的抗原结合点单克隆抗体。这一新发现表明,新发现的肽图案模仿中和表位脚踏室。
Seven-mer phage random peptide libraries were panned against 2C10, a monoclonal antibody that showed neutralizing activities against PEDV. Recombinant M13 phages displaying the peptides SHRLP(Y/Q)(P/V) or GPRPVTH on the g3p minor coat protein showed strong binding affinity with 2C10 (70% and 30% of recovered phages, respectively) after multiple panning. Sequence analysis suggested that these peptides are similar with 1368GPRLQPY1374 found at the carboxy-terminal of the S protein. In neutralization inhibition assays, the two peptide motifs and a 24-mer synthetic peptide corresponding to the C-terminal endodomain of PEDV S protein were observed to compete for the antigen binding site of 2C10, as demonstrated by the loss or reduction of neutralizing activity of the monoclonal antibody. This new finding suggests that the newly discovered peptide motifs mimic a neutralizing epitope PEDV.
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