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Location of Ferritin-Labeled Concanavalin A Binding to Influenza Virus and Tumor Cell Surfaces

机译:铁蛋白标记的康丹林的位置与流感病毒和肿瘤细胞表面的结合

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Concanavalin A (Con-A) was linked to ferritin with glutaraldehyde and chromatographed on Sepharose 6B to separate unconjugated Con-A and ferritin from covalently cross-linked molecules. Ehrlich ascites tumor cells were infected with WSA influenza virus, stained at intervals with the ferritin-labeled Con-A and examined by electron microscopy. The surfaces of most mature viruses were specifically stained, providing direct evidence that influenza viruses maturing in this cell type have exposed Con-A receptor sites. The ferritin cores of the staining reagent were found at an average distance of 21.3 nm from the virus membrane and 10.8 nm from the uninfected cell membrane. This finding was interpreted to mean that the population of Con-A receptor sites on influenza virus particles is located at an average distance from the virus membrane twice that of the population of Con-A receptor sites found on uninfected cells. The structural elements of viral membranes can provide a reliable means for evaluating electron microscopy staining reagents, thereby enhancing their usefulness as probes for the study of membrane relationships.
机译:Concanavalin A(Con-A)与铁蛋白与戊二醛连接,并在琼脂糖6b上进行色谱分离,将来自共价交联分子的未缀合的Con-A和铁蛋白分离。 EHRLICH腹水肿瘤细胞用WSA流感病毒感染,以与铁蛋白标记的CON-A的间隔染色并通过电子显微镜检查。特别染色了大多数成熟病毒的表面,提供了直接证据,即在这种细胞类型中成熟的流感病毒已经暴露了Con-A受体位点。染色试剂的铁蛋白芯被发现,从病毒膜的平均距离为21.3nm,从未感染的细胞膜为10.8nm。该发现被解释为意味着流感病毒颗粒上的Con-A受体位点的群体位于与病毒膜的平均距离,两倍于未感染细胞的Con-A受体位点的群体。病毒膜的结构元素可以提供用于评估电子显微镜染色试剂的可靠方法,从而提高其作为研究膜关系研究的探针的有用性。

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