FURTHER CHARACTERIZATION OF THE SOLUBLE FORM OF THE G-GLYCOPROTEIN OF RESPIRATORY SYNCYTIAL VIRUS
FURTHER CHARACTERIZATION OF THE SOLUBLE FORM OF THE G-GLYCOPROTEIN OF RESPIRATORY SYNCYTIAL VIRUS
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DOI：
10.1128/jvi.62.7.2228-2233.1988
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发表时间：
1988-07-01
影响因子：
5.4
通讯作者：
PATTERSON, JL
中科院分区：
文献类型：
--
作者：
HENDRICKS, DA;MCINTOSH, K;PATTERSON, JL
呼吸道合胞病毒G糖蛋白的一种可溶性形式，即附着蛋白，从感染的HEp-2细胞中脱落。Long和18537株的Gs蛋白分别具有82和71千道尔顿的表观分子大小，比病毒体相关形式（Gv）小6至9千道尔顿。对Long株的Gs蛋白进行了进一步的鉴定。在感染后24小时，这些培养物中所有放射性标记的G分子中约有六分之一作为Gs蛋白存在。Gs蛋白在感染后6小时的培养液中明显可见，但Gv蛋白直到感染后12小时才能被识别，这一观察结果与呼吸道合胞病毒的12小时日食期一致。因此，Gs蛋白至少部分地从完整的感染细胞中脱落，并且在子代病毒出现之前。较小的Gs蛋白（74千道尔顿）的外观与衣霉素孵育的感染呼叫的液体中显示，除了N-连接的寡糖是不需要的G2蛋白的发生和脱落。纯化的Gs蛋白的氨基末端的测序揭示了两个不同的末端，其世代与氨基酸65和66之间以及残基74和75之间的全长G蛋白的切割一致。该结果表明，Gs蛋白以两种不同的形式存在，其缺乏全长G蛋白的所提出的胞质内和跨膜结构域。
A soluble form of the G glycoprotein, the attachment protein, of respiratory syncytial virus is shed from infected HEp-2 cells. The Gs proteins of the Long and 18537 strains have apparent molecular sizes of 82 and 71 kilodaltons, respectively, 6 to 9 kilodaltons smaller than the virion-associated forms (Gv). The Gs protein of the Long strain was further characterized. Approximately one in six of all of the radiolabelled G molecules in these cultures at 24 h postinfection was present as the Gs protein. The Gs protein was clearly evident in culture fluids at 6 h postinfection, but the Gv protein could not be discerned until 12 h after infection, an observation that is consistent with the 12-h eclipse period for respiratory syncytial virus. Therefore, the Gs protein is shed, in part at least, from intact, infected cells and before the appearance of progeny virus. The appearance of a smaller Gs protein (74 kilodaltons) in fluids of infected calls which were incubated with tunicamycin shows that addition of N-linked oligosaccharides is not required for the genesis and shedding of the G2 protein. Sequencing of the amino terminus of purified Gs protein revealed two different termini, whose generations are consistent with cleavages of the full-length G protein between amino acids 65 and 66 and between residues 74 and 75. This result suggests that the Gs protein is present in two different forms which lack the proposed intracytoplasmic and transmembrane domains of the full-length G protein.