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J. Biol. Chem., Vol. 275, Issue 23, 17549-17555, June 9, 2000

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Identification and Characterization of Cell Lines with a Defect in a Post-adsorption Stage of Sendai Virus-mediated Membrane Fusion^*

From the ^a Department of Neurovirology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, 565-0871, Japan, ^b University College London, MRC, Laboratory for Molecular Cell Biology, London, WC1 E6BT, United Kingdom, the ^c Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Sciences, Shizuoka, 422-8526, Japan, the ^d Molecular Medical Science Institute, Otsuka Pharmaceutical Co. Ltd., Tokushima, 771-0192, Japan, the ^e Department of Bacteriology, Hiroshima University School of Medicine, Hiroshima, 734-8551, Japan, the ^f Department of Bioscience and Technology, Faculty of Agriculture, Iwate University, Morioka, 020-8550, Japan, the ^g Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, Setagaya, Tokyo, 158-8501, Japan, and the ^h Department of Biochemistry, Hamamatsu University School of Medicine, Hamamatsu, Shizuoka, 431-3192, Japan

In the early stage of infection, Sendai virus delivers its genome into the cytoplasm by fusing the viral envelope with the cell membrane. Although the adsorption of virus particles to cell surface receptors has been characterized in detail, the ensuing complex process that leads to the fusion between the lipid bilayers remains mostly obscure. In the present study, we identified and characterized cell lines with a defect in the Sendai virus-mediated membrane fusion, using fusion-mediated delivery of fragment A of diphtheria toxin as an index. These cells, persistently infected with the temperature-sensitive variant Sendai virus, had primary viral receptors indistinguishable in number and affinity from those of parental susceptible cells. However, they proved to be thoroughly defective in the Sendai virus-mediated membrane fusion. We also found that viral HN protein expressed in the defective cells was responsible for the interference with membrane fusion. These results suggested the presence of a previously uncharacterized, HN-dependent intermediate stage in the Sendai virus-mediated membrane fusion.

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