The GPRLQPY motif located at the carboxy-terminal of the spike protein induces antibodies that neutralize Porcine epidemic diarrhea virus.
The GPRLQPY motif located at the carboxy-terminal of the spike protein induces antibodies that neutralize Porcine epidemic diarrhea virus.
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DOI：
10.1016/j.virusres.2007.10.015
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发表时间：
2008-03
期刊：
影响因子：
5
通讯作者：
Shin HJ
中科院分区：
文献类型：
--
作者：
Cruz DJ;Kim CJ;Shin HJ
猪流行性腹泻病毒刺突蛋白是参与病毒附着和侵入的主要表面糖蛋白，是中和抗体的作用靶点。在这里，一个新的抗原结构域上发现的刺突蛋白的羧基末端的肽基序GPRLQPY，其特征在于免疫原性进行了评估。一种合成肽，其线性序列与24 a.a.刺突蛋白的羧基末端部分（S-CT 24）在BALB/c小鼠中引发强烈的抗体应答，其具有针对S-CT 24和PEDV的特异性反应性。这些抗体显示对GPRLQPY基序具有特异性亲和力，如通过与缺乏该基序的肽的非反应性所证明的。此外，抗S-CT 24抗体在病灶减少中和试验中表现出针对KPEDV-9的中和活性，表明GPRLQPY基序诱导针对PEDV的中和抗体。
The spike protein of Porcine epidemic diarrhea virus is the main surface glycoprotein involved in virus attachment and entry and therefore is the target of neutralizing antibodies. Here, the immunogenicity of a novel antigenic domain found on the carboxy-terminal of the spike protein characterized by the peptide motif GPRLQPY, was evaluated. A synthetic peptide whose linear sequence is identical to the 24 a.a. carboxy-terminal portion of the spike protein (S-CT24) elicited a strong antibody response in BALB/c mice that had specific reactivity against the S-CT24 and PEDV. These antibodies were shown to have a specific affinity to the GPRLQPY motif, as demonstrated by non-reactivity with a peptide that lacks this motif. In addition, antiS-CT24 antibodies exhibited neutralizing activities against KPEDV-9 in focus reduction neutralization tests suggesting that the GPRLQPY motif induces neutralizing antibodies against PEDV.
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