Kuroki K, Cheung R, Marion P L, Ganem D
Department of Microbiology and Immunology, University of California Medical Center, San Francisco 94143.
J Virol. 1994 Apr;68(4):2091-6. doi: 10.1128/JVI.68.4.2091-2096.1994.
We have identified a 180-kDa cellular glycoprotein (gp180) that binds with high affinity to duck hepatitis B virus (DHBV) particles. The protein was detected by coprecipitating labeled duck hepatocyte proteins with virions or recombinant DHBV envelope proteins, using nonneutralizing monoclonal antibodies to the virion envelope. Binding of gp180 requires only the pre-S region of the viral large envelope protein, since recombinant fusion proteins bearing only this region efficiently coprecipitate gp180. The DHBV-gp180 interaction is blocked by two independent neutralizing monoclonal antibodies. The protein is found on both internal and surface membranes of the cell, and the species distribution of gp180 binding activity mirrors the known host range of DHBV infection. Functional gp180 is expressed in a wide variety of tissues in susceptible ducks.
我们鉴定出一种180 kDa的细胞糖蛋白(gp180),它能与鸭乙型肝炎病毒(DHBV)颗粒高亲和力结合。使用针对病毒粒子包膜的非中和性单克隆抗体,通过将标记的鸭肝细胞蛋白与病毒粒子或重组DHBV包膜蛋白共沉淀来检测该蛋白。gp180的结合仅需要病毒大包膜蛋白的前S区域,因为仅带有该区域的重组融合蛋白能有效地共沉淀gp180。DHBV与gp180的相互作用被两种独立的中和性单克隆抗体阻断。该蛋白存在于细胞的内膜和表面膜上,并且gp180结合活性的物种分布反映了已知的DHBV感染宿主范围。功能性gp180在易感鸭的多种组织中表达。