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- W2022691837 abstract "The effect of tunicamycin (TM) on the synthesis, glycosylation, and maturation of Sendai virus glycoproteins was investigated. Incorporation of [3H]glucosamine into HN and F glycoproteins was completely inhibited by TM at a concentration of 0.5 μg/ml. Treatment of infected cells with TM under these conditions caused a 106-fold reduction in the production of infectious progeny virus. Synthesis of nonglycosylated viral proteins, P, NP, and M was clearly detected in TM-treated cells while synthesis of glycoproteins HN and F was not. However, two new polypeptides with molecular weights of 63,000 (T,) and 55,000 (T2) were synthesized in the presence of TM. Tryptic peptide analysis revealed that the T1 and T2 polypeptides are the nonglycosylated forms of the HN and F proteins, respectively. When microsome vesicles isolated from TM-treated cells were treated with trypsin, T1 and T2 were found to be protected from proteolysis, which suggests that after their synthesis the HN and F proteins are properly inserted into the endoplasmic reticulum bilayer even in the absence of glycosylation. In addition, the nonglycosylated forms of glycoproteins were found in pulse-chase experiments to normally migrate from rough to smooth cytoplasmic membranes. However, they could not be detected on the surface of infected cells by direct immunofluorescent staining, suggesting that the HN and F proteins can not be integrated into plasma membranes in the absence of glycosylation. Further, electron microscopic observation showed that there were no budding particles on the surfaces of TM-treated cells." @default.
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- W2022691837 date "1982-06-01" @default.
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- W2022691837 title "Effect of tunicamycin on the replication of sendai virus" @default.
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- W2022691837 doi "https://doi.org/10.1016/0042-6822(82)90106-4" @default.
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