与E2糖蛋白中单个氨基酸变化相关的辛德毕斯病毒神经毒力改变的机制
Mechanism of altered Sindbis virus neurovirulence associated with a single-amino-acid change in the E2 Glycoprotein.
作者信息
Tucker P C, Griffin D E
机构信息
Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
出版信息
J Virol. 1991 Mar;65(3):1551-7. doi: 10.1128/JVI.65.3.1551-1557.1991.
Abstract
The mechanism by which amino acid changes in the E1 and E2 surface glycoproteins of Sindbis virus affect neurovirulence is unknown. We have studied two recombinant viruses which differ in virulence. One (TE) contains Gly and the other (TES) contains Arg at position 172 in E2. TE causes more rapid death than TES in newborn mice. Both viruses replicate similarly in nonneuronal cells, but TE replicates more rapidly in the brains of newborn mice and in neuroblastoma cells. TE also induces earlier viral RNA synthesis in neuroblastoma cells. 35S-labeled TE binds more efficiently to brain and neuroblastoma cells, but not to nonneuronal cells, than TES. We propose that a region of the E2 glycoprotein affected by the amino acid occupying position 172 is important for binding to an alphavirus receptor on neurons and influences neurovirulence by this mechanism.
摘要
辛德毕斯病毒E1和E2表面糖蛋白中的氨基酸变化影响神经毒力的机制尚不清楚。我们研究了两种毒力不同的重组病毒。一种（TE）在E2的第172位含有甘氨酸，另一种（TES）在该位置含有精氨酸。在新生小鼠中，TE比TES导致死亡更快。两种病毒在非神经细胞中的复制情况相似，但TE在新生小鼠大脑和神经母细胞瘤细胞中的复制更快。TE在神经母细胞瘤细胞中也诱导更早的病毒RNA合成。与TES相比，35S标记的TE与大脑和神经母细胞瘤细胞的结合更有效，但与非神经细胞的结合则不然。我们提出，E2糖蛋白中受占据第172位的氨基酸影响的区域对于与神经元上的甲病毒受体结合很重要，并通过这种机制影响神经毒力。
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