戊型肝炎病毒感染机制初步研究
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摘要
戊型肝炎病毒(HEV)不稳定易降解,难以从载毒标本中分离,而迄今为止仍没有有效的细胞培养模型,这很大程度上限制了HEV感染致病机制的研究。近年来,随着对HEV研究的深入,较好模拟了HEV病毒衣壳表面结构的重组蛋白为研究HEV与宿主细胞相互作用提供了一条新的途径。
HEV衣壳由单一蛋白(pORF2)组成,大量研究表明pORF2的重组表达片段p239(aa368—606)很好地模拟了HEV的免疫优势中和表位。p239对HEV与原代肝细胞、HepG2细胞的吸附阻断,p239对多株细胞系具有与HEV相似的嗜性,以及多株HEV特异单抗对p239与HepG2细胞结合的特异阻断,强有力地提示p239同时也很好地模拟了HEV与细胞膜的结合所具备的表面结构特征。因此,p239与HepG2细胞的吸附模型是探讨HEV与细胞膜相瓦作用的可靠工具。
不同结合区域的HEV单抗及其Fab片段对p239吸附细胞的阻断结果提示,p239表面至少存在两个细胞受体结合区域:其一为HEV的主要免疫优势中和表位(ORF2 aa459-606),另一个区域为aa423-438。这两个区域均对p239与细胞的特异性吸附有贡献,均能单独介导p239与嗜性细胞的吸附,但aa459-606区域吸附细胞的能力要明显强于后者,是介导p239吸附的主要部位。aa423-438区域与细胞表面作用力弱,在HEV结合过程中很可能只是增加病毒与主要受体结合的机会。
缺失了aa423-438的p239突变体Δ239保留了免疫优势中和表位,与p239一样均能阻断天然HEV对HepG2细胞的感染吸附。而丧失免疫优势表位的233N则不能有效阻断。此结果表明HEV与嗜性细胞的结合很可能同p239与HepG2细胞之间的结合一样,也是通过这两个区域,并且主要免疫优势区域(ORF2aa459-606)在HEV与细胞结合过程中发挥主要作用。
通过酵母双杂交,从人肝细胞cDNA文库中筛出四个可能与HEV衣壳蛋白相结合的蛋白:肝细胞药物代谢酶(p450)、转化相关蛋白(TRP13)、p38相结合蛋白(p38IP)、DDAH2。并通过免疫共沉淀初步验证了p38IP与E2的结合,提示HEV ORF2激活MAPK p38通路的可能。
通过亲和层析筛选HepG2、猴肝组织中与p239相结合的蛋白,并利用二维电泳(2-DE)结合生物质谱技术分离鉴定这些结合蛋白,得到6个可能与p239相互作用的蛋白:HSP90、GRP78/Bip、alpha tubulin、P43、ATPase beta subunit、某未命名蛋白。并通过免疫共沉淀、细胞共定位等多种实验手段进一步验证了GRP78/Bip、HSP90与p239的结合。结果表明,GRP78/Bip与p239、HSP90与p239在HepG2细胞内共定位。并且p239与E.coli表达经纯化的GRP78/Bip可直接结合,提示它们在细胞内的相互作用不是经由第三者为中介的结合。同时,ATP的加入会导致p239与GRP78/Bip结合的可逆解离,提示p239与GRP78/Bip的结合是ATP依赖的特异性结合,GRP78/Bip的ATPase活性在这种结合中有重要的作用。
本文建立了能较好模拟HEV与细胞的吸附过程的p239-HepG2吸附模型,进一步发现HEV上至少具有两个细胞受体结合区域。其中一个结合力较强的区域与HEV主要中和表位区域重叠,而另一个区域结合力较弱。为阐明HEV吸附机制奠定了良好基础,并提供了重要的研究工具。而对细胞内的p239结合蛋白的分离鉴定则为阐明HEV的复制、致病机制提供了重要线索。
Hepatitis E Virus [HEV] has emerged to be a dominant cause of acute hepatitis, replacing hepatitis A virus in some areas and comparable in others. Research into pathogenesis and epidemiology of infection caused by this virus has been severely hampered, because the virus could not be efficiently propagated in cell culture.
Previous studies suggest that p239, a recombinant protein specified by ORF2 of the HEV genome, models the HEV neutralization sites identified by the HEV neutralizing antibodies, 8C11 and 8H3, as well as other structural features of the protrusion projecting from the basal shell of the virus capsid identified by other monoclonal antibodies. Taking advantage of this structural resemblance, the objective of my thesis is to use this peptide as a probe to study interaction of HEV with its host cells. To this end, I have established a transient infection model for HEV, using the HepG2 and a variety of other cell line and analyzed the interactions between these cells and p239.
The results suggest that binding of p239 to HepG2 cells may occur via at least 2 separate sites locating to aa423-438 and aa459-606, respectively, of the HEV structural protein. These sites were distinguished by using a panel of monoclonal antibodies and also by mutagenesis.
Further analysis identified at least 7 host cell proteins which bind with p239, and suggest that these p239 binding host cell proteins include HSP90、GRP78/Bip、alpha tubulin、P43、ATPase beta subunit and an unknown cellular protein. Moreover, it was shown that binding of p239 to one of these cellular proteins, GRP78/Bip, is ATP dependent.
The most critical step of infection is for virus to gain entry into its host cells. The present study took advantage of the structural resemblance of a recombinant protein, p239, to neutralization sites and other structural features of the HEV capsid, and use it as a probe to analyze the mechanism by which the virus gain entry to its host cells. The findings that p239 could effectively block HEV infection of a variety of cell lines susceptible to infection by this virus suggests that this novel approach is valid for studying virus-cell interaction. The findings described in this thesis suggest that this is a complex process, brought about by concerted actions involving direct and indirect binding of the virus structural protein with multiple of host cell proteins locating to spatially distinct sites on the virus capsid, and the process may require energy expenditure. Further studies will be required to identify the major cellular proteins involved in direct and indirect binding with the virus and how the interactions act in concert to bring about HEV entry to host cells.
HEV衣壳由单一蛋白(pORF2)组成,大量研究表明pORF2的重组表达片段p239(aa368—606)很好地模拟了HEV的免疫优势中和表位。p239对HEV与原代肝细胞、HepG2细胞的吸附阻断,p239对多株细胞系具有与HEV相似的嗜性,以及多株HEV特异单抗对p239与HepG2细胞结合的特异阻断,强有力地提示p239同时也很好地模拟了HEV与细胞膜的结合所具备的表面结构特征。因此,p239与HepG2细胞的吸附模型是探讨HEV与细胞膜相瓦作用的可靠工具。
不同结合区域的HEV单抗及其Fab片段对p239吸附细胞的阻断结果提示,p239表面至少存在两个细胞受体结合区域:其一为HEV的主要免疫优势中和表位(ORF2 aa459-606),另一个区域为aa423-438。这两个区域均对p239与细胞的特异性吸附有贡献,均能单独介导p239与嗜性细胞的吸附,但aa459-606区域吸附细胞的能力要明显强于后者,是介导p239吸附的主要部位。aa423-438区域与细胞表面作用力弱,在HEV结合过程中很可能只是增加病毒与主要受体结合的机会。
缺失了aa423-438的p239突变体Δ239保留了免疫优势中和表位,与p239一样均能阻断天然HEV对HepG2细胞的感染吸附。而丧失免疫优势表位的233N则不能有效阻断。此结果表明HEV与嗜性细胞的结合很可能同p239与HepG2细胞之间的结合一样,也是通过这两个区域,并且主要免疫优势区域(ORF2aa459-606)在HEV与细胞结合过程中发挥主要作用。
通过酵母双杂交,从人肝细胞cDNA文库中筛出四个可能与HEV衣壳蛋白相结合的蛋白:肝细胞药物代谢酶(p450)、转化相关蛋白(TRP13)、p38相结合蛋白(p38IP)、DDAH2。并通过免疫共沉淀初步验证了p38IP与E2的结合,提示HEV ORF2激活MAPK p38通路的可能。
通过亲和层析筛选HepG2、猴肝组织中与p239相结合的蛋白,并利用二维电泳(2-DE)结合生物质谱技术分离鉴定这些结合蛋白,得到6个可能与p239相互作用的蛋白:HSP90、GRP78/Bip、alpha tubulin、P43、ATPase beta subunit、某未命名蛋白。并通过免疫共沉淀、细胞共定位等多种实验手段进一步验证了GRP78/Bip、HSP90与p239的结合。结果表明,GRP78/Bip与p239、HSP90与p239在HepG2细胞内共定位。并且p239与E.coli表达经纯化的GRP78/Bip可直接结合,提示它们在细胞内的相互作用不是经由第三者为中介的结合。同时,ATP的加入会导致p239与GRP78/Bip结合的可逆解离,提示p239与GRP78/Bip的结合是ATP依赖的特异性结合,GRP78/Bip的ATPase活性在这种结合中有重要的作用。
本文建立了能较好模拟HEV与细胞的吸附过程的p239-HepG2吸附模型,进一步发现HEV上至少具有两个细胞受体结合区域。其中一个结合力较强的区域与HEV主要中和表位区域重叠,而另一个区域结合力较弱。为阐明HEV吸附机制奠定了良好基础,并提供了重要的研究工具。而对细胞内的p239结合蛋白的分离鉴定则为阐明HEV的复制、致病机制提供了重要线索。
Hepatitis E Virus [HEV] has emerged to be a dominant cause of acute hepatitis, replacing hepatitis A virus in some areas and comparable in others. Research into pathogenesis and epidemiology of infection caused by this virus has been severely hampered, because the virus could not be efficiently propagated in cell culture.
Previous studies suggest that p239, a recombinant protein specified by ORF2 of the HEV genome, models the HEV neutralization sites identified by the HEV neutralizing antibodies, 8C11 and 8H3, as well as other structural features of the protrusion projecting from the basal shell of the virus capsid identified by other monoclonal antibodies. Taking advantage of this structural resemblance, the objective of my thesis is to use this peptide as a probe to study interaction of HEV with its host cells. To this end, I have established a transient infection model for HEV, using the HepG2 and a variety of other cell line and analyzed the interactions between these cells and p239.
The results suggest that binding of p239 to HepG2 cells may occur via at least 2 separate sites locating to aa423-438 and aa459-606, respectively, of the HEV structural protein. These sites were distinguished by using a panel of monoclonal antibodies and also by mutagenesis.
Further analysis identified at least 7 host cell proteins which bind with p239, and suggest that these p239 binding host cell proteins include HSP90、GRP78/Bip、alpha tubulin、P43、ATPase beta subunit and an unknown cellular protein. Moreover, it was shown that binding of p239 to one of these cellular proteins, GRP78/Bip, is ATP dependent.
The most critical step of infection is for virus to gain entry into its host cells. The present study took advantage of the structural resemblance of a recombinant protein, p239, to neutralization sites and other structural features of the HEV capsid, and use it as a probe to analyze the mechanism by which the virus gain entry to its host cells. The findings that p239 could effectively block HEV infection of a variety of cell lines susceptible to infection by this virus suggests that this novel approach is valid for studying virus-cell interaction. The findings described in this thesis suggest that this is a complex process, brought about by concerted actions involving direct and indirect binding of the virus structural protein with multiple of host cell proteins locating to spatially distinct sites on the virus capsid, and the process may require energy expenditure. Further studies will be required to identify the major cellular proteins involved in direct and indirect binding with the virus and how the interactions act in concert to bring about HEV entry to host cells.
引文
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