Isolation and analysis of mode of action of novel inhibitors of intracellular translocation of glycoproteins

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Novel inhibitors are desired to analyze the mechanism of intracellular translocation of glycoproteins. For this purpose, a new screening method has been devised. This method is convenient but efficient to isolate specific inhibitors. The strategy of this method is based on the assumption that such inhibitors should inhibit cell fusion after infection with enveloped viruses without affecting glycoprotein synthesis. Inhibitors have been searched among cultures of microbes isolated from soil samples, and isolated. Characterization of these inhibitors waits for further investigation, but these inhibitors are different from those known to inhibit intracellular translocation of glycoproteins. In the presence of these inhibitors, vesicular stomatitis virus G protein accumulates intracellularly and has a molecular weight smaller than that of control mature G protein. This decrease in molecular weight is caused by incompleteness of processing of the saccharide side chain indicating that its intracellular translocation is stopped before reaching the trans compartment of the Golgi apparatus. Their mode of action is now under investigation.