Two glycoproteins are produced from the rotavirus neutralization gene.
Two glycoproteins are produced from the rotavirus neutralization gene.
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轮状病毒中和基因产生两种糖蛋白。
DOI：
10.1016/0042-6822(86)90046-2
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发表时间：
1986
期刊：
影响因子：
3.7
通讯作者：
Estes,MK
中科院分区：
文献类型：
--
作者：
Chan,WK;Penaranda,ME;Crawford,SE;Estes,MK
轮状病毒的主要中和抗原是外衣壳糖蛋白VP 7，表观分子量为38，000（38 K）。猿轮状病毒SA 11基因组片段9编码VP 7，包含两个同相起始密码子，每个密码子后面是编码疏水氨基酸区域的序列。我们已经确定，这个基因是功能双顺反子的分析合成的VP 7在SA 11感染的细胞和无细胞翻译系统编程与混合选择，段9特定的mRNA和狗胰腺微粒体。杂交选择基因9 mRNA在小麦胚中的翻译产生了分子量为37 K和35.3K的两种不同的多肽。在微粒体存在下的体外翻译产生了一条38 K的弥散带，该带经内切糖苷酶H消化后转化为37 K和35.3K的前体带。对缺乏VP 7中糖基化位点的SA 11变体的研究证实了这些引物-产物关系，并通过表明由第一个AUG翻译产生的糖蛋白含有切割的信号序列而由第二个AUG翻译产生的糖蛋白含有未切割的信号序列来扩展它们。免疫沉淀与单特异性抗VP 7血清和改进的凝胶电泳条件使我们能够表明，这两个VP 7在感染细胞中表达在相似的时间，都被发现在几个不同的轮状病毒株的纯化病毒颗粒。这两种VP 7糖蛋白在功能上是否不同仍有待确定。
The major neutralization antigen of rotaviruses is an outer capsid glycoprotein, VP7, with an apparent molecular weight of 38,000 (38K). The simian rotavirus SA11 genome segment 9, which codes for VP7, contains two in-phase initiation codons, each of which is followed by a sequence that codes for a region of hydrophobic amino acids. We have determined that this gene is functionally bicistronic by analyzing the synthesis of VP7 in SA11-infected cells and in cell-free translation systems programmed with hybrid-selected, segment 9 specific mRNA and dog pancreatic microsomes. The translation of hybrid-selected gene 9 mRNA in wheat germ extracts yielded two distinct polypeptides of molecular weights 37K and 35.3K.In vitrotranslation in the presence of microsomes yielded one diffuse band of 38K that was converted into the 37K and 35.3K precursor bands by digestion with endoglycosidase H. Studies with a variant of SA11 that lacks the glycosylation site in VP7 confirmed these precursor-product relationships and extended them by indicating that the glycoprotein produced by translation from the first AUG contained a cleaved signal sequence whereas the glycoprotein produced by translation from the second AUG contained an uncleaved signal sequence. Immunoprecipitation with monospecific anti-VP7 serum and improved gel electrophoresis conditions allowed us to show that both VP7s were expressed at similar times in infected cells and both were found in purified virus particles of several different rotavirus strains. Whether these two VP7 glycoproteins are functionally distinct remains to be determined.