Nakhasi H L, Singh N K, Pogue G P, Cao X Q, Rouault T A
Division of Hematologic Products, CBER, Food and Drug Administration, National Institute of Child Health and Human Development, National Institute of Health, Bethesda, Maryland.
Arch Virol Suppl. 1994;9:255-67. doi: 10.1007/978-3-7091-9326-6_26.
We have analyzed the function of cis-acting elements of rubella virus RNA and the components which interact with these elements in viral RNA replication. We demonstrated that the 5'- and 3'-terminal sequences from RV RNA promote translation and negative-strand RNA synthesis of chimeric chloroamphenicol acetyltransferase (CAT) RNAs. These sequences have a potential to form stem-loop (SL) structures and bind cellular proteins specifically in RNA gel-shift and UV cross-linking assays. The 5' end binding proteins were identified to be Ro/SSA-associated antigens by virtue of being recognized in an RNA complex by an autoimmune patient serum with Ro antigen type specificity. Purification and sequence analysis of the 3' end binding protein revealed that it is a homologue of human calreticulin. The role of host protein in RV replication is discussed.
我们分析了风疹病毒RNA顺式作用元件的功能以及在病毒RNA复制过程中与这些元件相互作用的成分。我们证明,风疹病毒RNA的5'和3'末端序列可促进嵌合氯霉素乙酰转移酶(CAT)RNA的翻译和负链RNA合成。这些序列有可能形成茎环(SL)结构,并在RNA凝胶迁移和紫外线交联试验中特异性结合细胞蛋白。通过具有Ro抗原类型特异性的自身免疫患者血清在RNA复合物中识别出5'末端结合蛋白为Ro/SSA相关抗原。3'末端结合蛋白的纯化和序列分析表明,它是人类钙网蛋白的同源物。文中讨论了宿主蛋白在风疹病毒复制中的作用。