Restriction of cell surface expression of Sendai virus hemagglutinin-neuraminidase glycoprotein correlates with its higher instability in persistently and standard plus defective interfering virus infected BHK-21 cells.
Restriction of cell surface expression of Sendai virus hemagglutinin-neuraminidase glycoprotein correlates with its higher instability in persistently and standard plus defective interfering virus infected BHK-21 cells.
复制标题
仙台病毒血凝素神经氨酸酶糖蛋白的细胞表面表达的限制与其在持续和标准加缺陷干扰病毒感染的 BHK-21 细胞中的较高不稳定性相关。
DOI：
10.1016/0042-6822(84)90152-1
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发表时间：
1984
期刊：
影响因子：
3.7
通讯作者：
Portner,A
中科院分区：
文献类型：
--
作者：
Roux,L;Beffy,P;Portner,A
为了了解仙台病毒产生持续感染的机制，研究了受标准病毒、标准和缺陷干扰颗粒（混合病毒感染）感染的BHK-21细胞表面血凝素-神经氨酸酶（HN）和融合（Fo）糖蛋白的表达情况。通过结合抗HN和抗Fo单克隆抗体，检测感染细胞表面HN和Fo的表达。结果表明，在混合病毒感染和持续感染期间，HN的表达相对于Fo受到限制。通过脉冲追踪实验进一步研究了HN水平的降低，结果显示HN在持续感染的细胞中周转率增加，在混合病毒感染的细胞中周转率增加，程度较小。在对脉冲追逐实验中产生的病毒颗粒[35S]蛋氨酸标记的蛋白质组成进行分析时，发现新合成的HN周转率增加与其掺入病毒颗粒减少有关。有趣的是，较差的HN结合也与基质M蛋白进入病毒颗粒的效率较低有关。
To gain an understanding of the mechanism(s) by which Sendai virus generates a persistent infection, the expression of the hemagglutinin-neuraminidase (HN) and fusion (Fo) glycoproteins at the surfaces of BHK-21 cells infected with standard virus, a mixture of standard and defective interfering (DI) particles (mixed virus infection), and during persistent infection was investigated. The expression of HN and Fo was measured on the surfaces of infected cells by the binding of anti-HN and anti-Fo monoclonal antibodies. The results show that HN expression was restricted relative to Fo during mixed virus and persistent infections. The decreased levels of HN were investigated further by pulse-chase experiments which revealed that HN has an increased turnover rate in persistently infected cells and, to a lesser extent, in mixed virus infected cells. In analyzing the [35S]methionine-labeled protein composition of virus particles produced during the pulse-chase experiments, the increased turnover of newly synthesized HN was found to correlate with its decreased incorporation into virus particles. Interestingly, the poor HN incorporation also correlates with less efficient incorporation of the matrix M protein into virus particles.