Immunological Studies of a 21 kDa Cellular Component Efficiently Incorporated into Rabies Virion Grown in a BHK‐21 Cell Culture
Immunological Studies of a 21 kDa Cellular Component Efficiently Incorporated into Rabies Virion Grown in a BHK‐21 Cell Culture
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对 BHK-21 细胞培养物中生长的狂犬病病毒粒子有效掺入 21 kDa 细胞成分的免疫学研究
作者：
J. Sagara;T. Tochikura;Toshiko Yamamoto;S. Tsukita;S. Tsukita;A. Kawai
为了研究掺入狂犬病病毒体的细胞组分，基于其与其他病毒体组分的反应性筛选单克隆抗体（MAb）。我们制备的两种MAb识别来自BHK-21细胞的病毒体相关21 kDa多肽（称为VAP 21）。由于MAb沉淀狂犬病病毒体，胰蛋白酶消化从病毒体中消除了VAP 21抗原，但碱处理（pH 11）没有，因此VAP 21似乎锚定在病毒包膜中并暴露在病毒体表面。尽管定量免疫印迹分析表明病毒粒子中VAP 21的浓度明显增加，但与细胞中的VAP 21含量与病毒糖蛋白（G）含量的比率相比，VAP 21含量与病毒糖蛋白（G）含量的比率降低了数倍。这些数据表明，VAP 21的分选发生在细胞上的病毒出芽过程中，但它可能是低效的，可能是由于VAP 21与病毒包膜蛋白更紧密的结合。这一假设似乎与免疫荧光研究的结果一致，即VAP 21与细胞中的病毒包膜抗原共定位分布。根据这些结果，表明VAP 21与细胞中的病毒包膜蛋白紧密结合，并且这种结合可能导致VAP 21被动但相对有效地掺入到病毒体中。
To investigate cellular components incorporated into the rabies virion, monoclonal antibodies (MAbs) were screened based on their reactivity with additional virion components. Two of the MAbs we prepared recognized a virion‐associated 21 kDa polypeptide (referred to as VAP21) from a BHK‐21 cell. Since the MAbs precipitated the rabies virion and trypsin digestion eliminated the VAP21 antigen from the virion but alkaline treatment (pH 11) did not, VAP21 seems to be anchored into the viral envelope and exposed on the virion surface. Although quantitative immunoblot analyses indicated an apparently increased concentration of VAP21 in the virion, the ratio of the content of VAP21 to that of viral glycoprotein (G) was several times decreased as compared to the ratio of those in the cell. These data suggest that sorting of VAP21 occurs during the viral budding process on the cell but that it might be inefficient, probably due to a more intimate association of VAP21 with the viral envelope proteins. This assumption seems to be consistent with the results of immunofluorescence studies; that is, VAP21 displayed colocalized distribution with viral envelope antigens in the cell. From these results, it is suggested that VAP21 closely associates with the viral envelope proteins in the cell, and this association might cause passive but relatively efficient incorporation of VAP21 into the virion.
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DOI：
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