He Shuizhen, Miao Ji, Zheng Zizheng, Wu Ting, Xie Minghui, Tang Ming, Zhang Jun, Ng Mun-Hon, Xia Ningshao
National Institute of Diagnostics and Vaccine Development of Infectious Disease, and Research Center for Medical Molecular Virology of Fujian Province, Xiamen University, Xiamen, 361005, PR China.
J Gen Virol. 2008 Jan;89(Pt 1):245-249. doi: 10.1099/vir.0.83308-0.
A truncated structural protein of hepatitis E virus (HEV), p239, occurs as 23 nm particles consisting of partial homodimers. As the latter resemble the HEV capsomere structurally and antigenically, it was postulated that the recombinant protein may serve as a probe for the HEV receptor. This hypothesis was supported by findings that purified p239 bound and penetrated different cell lines that are susceptible to HEV, and inhibited HEV infection of these cells. The binding was blocked by four of six monoclonal antibodies (mAbs) reactive against the dimeric domain of p239, and by two of three mAbs reactive against its monomeric domain, suggesting that binding may involve a portion of each domain. Mutation affecting the monomeric domain had no effect on binding or capacity to block HEV infection, whereas that affecting the dimeric domain diminished binding of the mutant peptide markedly and abrogated its capacity to block HEV infection. These results suggest that HEV infection might involve distinct receptor-binding sites.
戊型肝炎病毒（HEV）的一种截短结构蛋白p239，以由部分同源二聚体组成的23纳米颗粒形式存在。由于后者在结构和抗原性上类似于HEV衣壳粒，因此推测该重组蛋白可能用作HEV受体的探针。这一假设得到了以下发现的支持：纯化的p239能够结合并穿透对HEV易感的不同细胞系，并抑制这些细胞的HEV感染。六种针对p239二聚体结构域的单克隆抗体（mAb）中有四种，以及三种针对其单体结构域的mAb中有两种可阻断这种结合，这表明结合可能涉及每个结构域的一部分。影响单体结构域的突变对结合或阻断HEV感染的能力没有影响，而影响二聚体结构域的突变则显著降低了突变肽的结合能力，并消除了其阻断HEV感染的能力。这些结果表明，HEV感染可能涉及不同的受体结合位点。
