van Steeg H, Kasperaitis M, Voorma H O, Benne R
Eur J Biochem. 1984 Feb 1;138(3):473-8. doi: 10.1111/j.1432-1033.1984.tb07940.x.
From ribosomal washes of neuroblastoma cells infected with Semliki Forest virus (SFV) a protein of Mr 33000 was purified, which comigrated with the viral capsid protein on sodium dodecyl sulfate/polyacrylamide gels and was recognized by antibodies against the capsid protein of SFV. This protein selectively inhibits the translation of host and early viral 42S mRNA in vitro, but has no effect on late viral 26S and encephalomyocarditis virus mRNA translation. Eukaryotic initiation factor 4B and cap-binding protein restore the translation of host and 42S mRNA to control levels. The capsid protein specifically prevents the binding of host mRNA into 80S initiation complexes, but has no effect on that of late viral mRNA. We propose that the capsid protein is the component responsible for the shut-off of host protein synthesis in SFV-infected cells and for the decreased translational activity of the crude ribosomal washes from these cells.
从用辛德毕斯病毒(SFV)感染的神经母细胞瘤细胞的核糖体洗脱物中,纯化出一种分子量为33000的蛋白质,它在十二烷基硫酸钠/聚丙烯酰胺凝胶上与病毒衣壳蛋白迁移率相同,并且能被抗SFV衣壳蛋白的抗体识别。这种蛋白质在体外能选择性抑制宿主和早期病毒42S mRNA的翻译,但对晚期病毒26S和脑心肌炎病毒mRNA的翻译没有影响。真核起始因子4B和帽结合蛋白能将宿主和42S mRNA的翻译恢复到对照水平。衣壳蛋白能特异性阻止宿主mRNA与80S起始复合物的结合,但对晚期病毒mRNA的结合没有影响。我们提出,衣壳蛋白是负责在SFV感染细胞中关闭宿主蛋白质合成以及导致这些细胞粗核糖体洗脱物翻译活性降低的成分。