Collins P L, Olmsted R A, Johnson P R
Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892.
J Gen Virol. 1990 Jul;71 ( Pt 7):1571-6. doi: 10.1099/0022-1317-71-7-1571.
The nucleotide and amino acid sequences of the mRNA and predicted polypeptide of the integral membrane small hydrophobic (SH) protein of human respiratory syncytial virus strain 18537 (a prototype strain of antigenic subgroup B) were determined from cloned cDNA. At the nucleotide and amino acid levels there was 78% and 76% identity, respectively, with the previously described SH mRNA and protein of strain A2 (a prototype strain of subgroup A). Most of the amino acid substitutions occurred in the predicted ectodomain (50% identity). The pattern of posttranslational processing of the strain 18537 SH protein was very similar to that of strain A2, yielding a nonglycosylated form and two glycosylated forms. Analysis of released virions of strain A2 by immunoprecipitation with SH-specific antibodies suggested that the major non-glycosylated species and one of the glycosylated species are virion structural components.
从克隆的互补脱氧核糖核酸（cDNA）中确定了人呼吸道合胞病毒18537株（抗原B亚组的原型株）完整膜小疏水（SH）蛋白的信使核糖核酸（mRNA）的核苷酸和氨基酸序列以及预测的多肽。在核苷酸和氨基酸水平上，与先前描述的A2株（A亚组的原型株）的SH mRNA和蛋白分别有78%和76%的同一性。大多数氨基酸替换发生在预测的胞外结构域（同一性为50%）。18537株SH蛋白的翻译后加工模式与A2株非常相似，产生一种非糖基化形式和两种糖基化形式。用SH特异性抗体通过免疫沉淀分析A2株释放的病毒粒子表明，主要的非糖基化种类和一种糖基化种类是病毒粒子的结构成分。
