Interaction between desialylated hepatitis B virus and asialoglycoprotein receptor on hepatocytes may be indispensable for viral binding and entry
Interaction between desialylated hepatitis B virus and asialoglycoprotein receptor on hepatocytes may be indispensable for viral binding and entry
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DOI：
10.1111/j.1365-2893.2005.00648.x
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发表时间：
2006-01
影响因子：
2.5
通讯作者：
Takashi Owada;K. Matsubayashi;H. Sakata;H. Ihara;Shinichiro Sato;Kenji Ikebuchi;T. Kato;Hiroshi Azuma;Hisami Ikeda
中科院分区：
文献类型：
--
作者：
Takashi Owada;K. Matsubayashi;H. Sakata;H. Ihara;Shinichiro Sato;Kenji Ikebuchi;T. Kato;Hiroshi Azuma;Hisami Ikeda
概括。乙型肝炎病毒 (HBV) 感染的细胞受体尚未确定。本研究的目的是探讨去唾液酸化的 HBV 和仅在肝实质细胞上表达的脱唾液酸糖蛋白受体 (ASGP-R) 参与感染的可能性。通过在存在或不存在神经氨酸酶 (NA) 的情况下培养肝母细胞瘤细胞系、HepG2 和来自 HBV 载体的 HBV 颗粒来进行病毒结合和进入的测定。 NA 存在时，病毒结合和进入明显增强，并且这种结合的增强可以被脱唾液酸胎球蛋白和乙二胺四乙酸 (EDTA) 阻断。此外，作为感染性标记的共价闭合环状 (CCC)-DNA 在 NA 存在的情况下被检测到，但在 NA 不存在的情况下则无法检测到。 NA最佳浓度使感染力提高1000倍以上。我们的结论是，这种方法使得在体外评估 HBV 的感染性成为可能，并且一旦病毒颗粒被去唾液酸化，ASGP-R 可能是一种特定的 HBV 受体。
Summary. The cellular receptor for hepatitis B virus (HBV) infection has not yet been identified. The purpose of this study was to address the possibility of participation by desialylated HBV and the asialoglycoprotein receptor (ASGP‐R) exclusively expressed on liver parenchymal cells, in infection. Assays for viral binding and entry were performed by culturing a hepatoblastoma cell line, HepG2, and HBV particles derived from the HBV carrier in the presence or absence of neuraminidase (NA). Viral binding and entry were clearly enhanced in the presence of NA, and the enhancement of the binding could be blocked by asialo‐fetuin and ethylenediamine‐tetraacetic acid (EDTA). In addition, covalently closed circular (CCC)‐DNA, as a marker of infectivity, was detected in the presence of NA, but not in its absence. The optimal concentration of NA raised infectivity more than 1000 times. We concluded that this method makes it feasible to evaluate the infectivity of HBV in vitro and that ASGP‐R may be a specific HBV receptor once viral particles are desialylated.