Respiratory syncytial virus polypeptides: their location in the virion.
Respiratory syncytial virus polypeptides: their location in the virion.
复制标题
呼吸道合胞病毒多肽：它们在病毒粒子中的位置。
DOI：
10.1016/0042-6822(79)90408-2
复制
发表时间：
1979
期刊：
影响因子：
3.7
通讯作者：
S. Levine
中科院分区：
文献类型：
--
作者：
M. Peeples;S. Levine
纯化的呼吸道合胞体（RS）病毒除了先前报道的六至七种多肽之外还含有（S. Levine，1977，J. Virol.，21，427-431），大多肽（VPO），MW > 160，000。用胰蛋白酶处理纯化的病毒可除去主要的糖蛋白VP 1和VP 2。用2%Triton X-100的HBSS溶液（相当于0.15MNaCl）处理纯化的病毒，可溶解糖蛋白VP 1和2以及非糖基化蛋白VP 5，分子量为28，000，这表明VP 5是一种M蛋白。用溶于0.4MNaCl的2%Triton X-100处理，除VPO和VP 3外，所有病毒体蛋白都溶解，它们在0.8MNaCl中也不溶解。结果表明，VP 3，MW 44，000，是主要的核衣壳蛋白，并且VPO不是病毒制剂的表面污染物，而是与核衣壳密切相关。只有VP 3存在于通过CsCl等密度离心从RS病毒感染的细胞分离的核衣壳中。
Purified respiratory syncytial (RS) virus contains, in addition to the six to seven polypeptides previously reported (S. Levine, 1977,J. Virol.,21, 427–431), a large polypeptide (VPO), MW > 160,000. Treatment of purified virus with trypsin removes the major glycoproteins, VP1 and 2. Treatment of purified virus with 2% Triton X-100 in HBSS (equivalent to 0.15MNaCl) solubilizes the glycoproteins VP1 and 2 and a nonglycosylated protein, VP5, MW 28,000, which suggests that VP5 is an M protein. Treatment with 2% Triton X-100 in 0.4MNaCl solubilizes all the virion proteins except VPO and VP3, which are also not solubilized in 0.8MNaCl. The results suggest that VP3, MW 44,000, is the major nucleocapsid protein, and that VPO is not a superficial contaminant of the virus preparation, but instead is closely associated with the nucleocapsid. Only VP3 is present in nucleocapsids isolated from RS virus-infected cells by isopycnic centrifugation in CsCl.