BIOSYNTHESIS OF PARAMYXOVIRUSES

用S.金黄色葡萄球菌蛋白酶裂解 将多肽P分成两个结构域，酸性蛋白酶敏感部分和酸性蛋白酶敏感部分。 碱性蛋白酶抗性核心，但对多肽NP几乎没有影响 和L. NDV多肽P的切割导致RNA的成比例损失， 合成活性表明P参与病毒RNA的合成。 三种方法被用来证明血凝和神经氨酸酶， 副粘病毒HN糖蛋白的活性涉及两个不同的位点。 通过用ts HN分析仙台病毒突变体来分离这些活性。 HN蛋白的单克隆抗体和HN蛋白类似物的用途 N-乙酰神经氨酸 在琼脂糖尿素凝胶上分离仙台病毒的mRNA， 负责合成鉴定的P、NP和M蛋白。 突变体ts 271的ts HN蛋白显示出快速降解， 合成.

Treatment of Sendai virus and NDV nucleocapsids with S. aureus protease cleaves polypeptide P into two domains, an acidic, protease-sensitive portion, and a basic, protease-resistant core, but has little to no effect on polypeptides NP and L. Cleavage of NDV polypeptide P resulted in a proportional loss of RNA synthetic activity suggesting that P is involved in the synthesis of viral RNA. Three approaches were used to show that the hemagglutinating and neuraminidase activities of the HN glycoprotein of paramyxoviruses involve two distinct sites. These activities were separated by analyzing a Sendai virus mutant with a ts HN protein and the use of monoclonal antibodies to HN and an analog of N-acetyl-neuraminic acid. The mRNAs of Sendai virus were separated on agarose urea gels and the RNAs responsible for synthesis of P, NP, and M proteins identified. The ts HN protein of mutant ts 271 was shown to be rapidly degraded after synthesis.