Little S P, Huang A S
J Virol. 1978 Aug;27(2):330-9. doi: 10.1128/JVI.27.2.330-339.1978.
In a culture of Chinese hamster ovary cells infected with vesicular stomatitis virus, there is specific shedding of viral antigens into the medium. This shedding appears to be unrelated to progeny formation or to cell lysis. Although all five of the virus-specific proteins are detected in the extracellular soluble fraction, the major antigen is the Gs protein. This protein has a molecular weight of 54,000. Indirect analysis of the content of sialic acid as well as peptide analysis of the Gs and G proteins of vesicular stomatitis virus suggest that the Gs protein is derived from the G protein by proteolysis. Both proteins are hydrophobic when analyzed by charge-shift electrophoresis. The presence of phenylmethylsulfonyl fluoride in the culture medium or the removal of serum from the culture medium partially reduces the shedding of Gs protein. Increased shedding of the Gs protein is seen when there is an unstable M or matrix protein synthesized by a temperature-sensitive mutant, tsG31. These results indicate that the G protein is cleaved at the cell surface, thus releasing Gs protein into the medium. Furthermore, the stability of G protein at the cell surface appears to be dependent on its association with the M protein.
在感染水疱性口炎病毒的中国仓鼠卵巢细胞培养物中，病毒抗原会特异性地释放到培养基中。这种释放似乎与子代形成或细胞裂解无关。尽管在细胞外可溶性部分中检测到了所有五种病毒特异性蛋白，但主要抗原是Gs蛋白。该蛋白的分子量为54,000。对唾液酸含量的间接分析以及对水疱性口炎病毒的Gs和G蛋白的肽分析表明，Gs蛋白是由G蛋白通过蛋白水解作用衍生而来的。通过电荷转移电泳分析时，这两种蛋白都是疏水性的。培养基中存在苯甲基磺酰氟或从培养基中去除血清会部分减少Gs蛋白的释放。当温度敏感突变体tsG31合成不稳定的M或基质蛋白时，会观察到Gs蛋白的释放增加。这些结果表明，G蛋白在细胞表面被切割，从而将Gs蛋白释放到培养基中。此外，G蛋白在细胞表面的稳定性似乎取决于它与M蛋白的结合。
