Schinkel Stephanie C Burke, Rubin Steven, Wright Kathryn E
Department of Biochemistry, Microbiology and Immunology, University of Ottawa, 451 Smyth Road, Ottawa, K1H 8M5, Canada.
Food and Drug Administration (FDA), Center for Biologics Evaluation and Research (CBER), OVRR, DVP, 10903 New Hampshire Avenue, Bldg 52/72, Silver Spring, MD, 20993, United States.
Virus Res. 2017 Jan 2;227:104-109. doi: 10.1016/j.virusres.2016.10.003. Epub 2016 Oct 6.
Temperature sensitivity is a phenotype often associated with attenuation of viruses. Previously, we purified several mumps variants from an incompletely attenuated Urabe strain live attenuated vaccine. Here we characterize one isolate that is sensitive to growth at high temperature. This virus was attenuated in a small animal model of mumps virulence, and we identified unique coding substitutions in the hemagglutinin-neuraminidase (HN), the viral polymerase (L) gene, and a non-coding substitution close to the anti-genome promoter sequences. At the non-permissive temperature, transcription of viral mRNAs and production of the replication intermediate were reduced compared to events at the permissive temperature and to a non-ts virulent Urabe virus. As well, synthesis of viral proteins was also reduced at the higher temperature. While the actual sequence substitutions in the ts virus were unique, the pattern of substitutions in HN, L and genome end sequences is similar to another attenuated Urabe virus previously described by us.
温度敏感性是一种常与病毒减毒相关的表型。此前,我们从一种未完全减毒的腮腺炎病毒株(Urabe株)活疫苗中纯化出了几种腮腺炎病毒变体。在此,我们对一种在高温下生长敏感的分离株进行了特性分析。该病毒在腮腺炎病毒毒力的小动物模型中表现出减毒特性,并且我们在血凝素 - 神经氨酸酶(HN)、病毒聚合酶(L)基因以及靠近反基因组启动子序列处发现了独特的编码替换。在非允许温度下,与在允许温度下以及与非温度敏感的强毒株Urabe病毒相比,病毒mRNA的转录和复制中间体的产生均减少。同样,在较高温度下病毒蛋白的合成也减少。虽然温度敏感病毒中的实际序列替换是独特的,但在HN、L和基因组末端序列中的替换模式与我们之前描述的另一种减毒Urabe病毒相似。