蜱传脑炎病毒包膜蛋白E中的单个氨基酸取代导致在小鼠模型中减毒。
A single amino acid substitution in envelope protein E of tick-borne encephalitis virus leads to attenuation in the mouse model.
作者信息
Holzmann H, Heinz F X, Mandl C W, Guirakhoo F, Kunz C
机构信息
Institute of Virology, University of Vienna, Austria.
出版信息
J Virol. 1990 Oct;64(10):5156-9. doi: 10.1128/JVI.64.10.5156-5159.1990.
Abstract
We have determined the virulence characteristics of seven monoclonal antibody escape mutants of tick-borne encephalitis virus in the mouse model. One of the mutants with an amino acid substitution from tyrosine to histidine at residue 384 revealed strongly reduced pathogenicity after peripheral inoculation of adult mice but retained its capacity to replicate in the mice and to induce a high-titered antibody response. Infection with the attenuated mutant resulted in resistance to challenge with virulent virus. Assessment of nonconservative amino acid substitutions in other attenuated flaviviruses suggests that a structural element including residue 384 may represent an important determinant of flavivirus virulence in general.
摘要
我们已经在小鼠模型中确定了蜱传脑炎病毒的七个单克隆抗体逃逸突变体的毒力特征。其中一个突变体在第384位氨基酸处由酪氨酸替换为组氨酸，在成年小鼠外周接种后显示出致病性大幅降低，但仍保留在小鼠体内复制并诱导高滴度抗体反应的能力。用减毒突变体感染可导致对强毒病毒攻击产生抗性。对其他减毒黄病毒中非保守氨基酸替换的评估表明，包括第384位残基在内的一个结构元件可能总体上代表黄病毒毒力的一个重要决定因素。
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