Mottet G, Portner A, Roux L
J Virol. 1986 Jul;59(1):132-41. doi: 10.1128/JVI.59.1.132-141.1986.
The immunoreactivity of the Sendai virus HN and F0 glycoproteins was shown to mature before reaching the final form exhibited by the native mature proteins. The maturation process differed for the two proteins. The native F0 immunoreactivity was shown to be defined cotranslationally, and the addition of high-mannose sugar residues may represent the final step in defining the maturation of immunoreactivity. On the other hand, native HN immunoreactivity was slowly fashioned during the hour after the completion of protein synthesis. Although addition of high-mannose sugar could constitute a necessary step in this slow maturation process, it was shown not to be sufficient. Processing of high-mannose sugars and HN self-association in homodimers and homotetramers were investigated as possible steps involved in the slow maturation of HN immunoreactivity. They were found not to play a significant role. On the other hand, conformational changes presumably took place during the maturation of HN immunoreactivity. Drastic immunoreactivity differences were also demonstrated between the native and denatured forms of the glycoproteins. Possible implications of these results in defining the pathways of glycoprotein synthesis are discussed.
仙台病毒HN和F0糖蛋白的免疫反应性在达到天然成熟蛋白所呈现的最终形式之前就已成熟。这两种蛋白的成熟过程有所不同。天然F0免疫反应性被证明是在共翻译时确定的，高甘露糖残基的添加可能代表了确定免疫反应性成熟的最后一步。另一方面，天然HN免疫反应性在蛋白质合成完成后的一小时内缓慢形成。尽管高甘露糖的添加可能是这个缓慢成熟过程中的一个必要步骤，但事实证明这还不够。研究了高甘露糖的加工以及HN在同二聚体和同四聚体中的自缔合，将其作为可能参与HN免疫反应性缓慢成熟的步骤。结果发现它们并没有起到显著作用。另一方面，在HN免疫反应性成熟过程中可能发生了构象变化。糖蛋白的天然形式和变性形式之间也表现出显著的免疫反应性差异。讨论了这些结果在确定糖蛋白合成途径方面的可能意义。
