Pérez L, Irurzun A, Carrasco L
Centro de Biología Molecular, Universidad Autónoma de Madrid, Spain.
J Gen Virol. 1994 Sep;75 ( Pt 9):2197-203. doi: 10.1099/0022-1317-75-9-2197.
Brefeldin A (BFA) is a macrolide antibiotic that blocks membrane traffic through the vesicular system and affects the glycosylation of viral glycoproteins. Treatment of HeLa cells infected with Semliki Forest virus (SFV) with BFA enhances the synthesis of late viral proteins. Proteolytic cleavage of p107 is partially blocked and viral glycoproteins accumulate in BFA-treated cells. This enhanced synthesis of late SFV proteins is due, at least in part, to an increase in the formation of the subgenomic SFV 26S mRNA. Since BFA blocks the replication of poliovirus genomes without affecting the cleavage of the translation initiation factor p220, protein synthesis was analysed in doubly infected cells. HeLa cells infected with SFV and poliovirus at the same multiplicity predominantly synthesize poliovirus proteins. But if these cells are treated with BFA they synthesize significant amounts of SFV capsid protein C for several hours, despite the fact that p220 has been degraded.
布雷菲德菌素A（BFA）是一种大环内酯类抗生素，它可阻断通过囊泡系统的膜转运，并影响病毒糖蛋白的糖基化。用BFA处理感染辛德毕斯病毒（SFV）的HeLa细胞可增强晚期病毒蛋白的合成。p107的蛋白水解切割被部分阻断，并且病毒糖蛋白在经BFA处理的细胞中积累。晚期SFV蛋白的这种合成增强至少部分归因于亚基因组SFV 26S mRNA形成的增加。由于BFA可阻断脊髓灰质炎病毒基因组的复制而不影响翻译起始因子p220的切割，因此对双重感染的细胞中的蛋白质合成进行了分析。以相同复数感染SFV和脊髓灰质炎病毒的HeLa细胞主要合成脊髓灰质炎病毒蛋白。但是，如果用BFA处理这些细胞，尽管p220已被降解，它们仍会在数小时内合成大量的SFV衣壳蛋白C。
