期刊
JOURNAL OF VIROLOGY
卷 83, 期 10, 页码 4823-4834出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01710-08
关键词
-
类别
资金
- Boehringer Ingelheim Vetmedica GmbH
- Deutsche Forschungsgemeinschaft [DFGME1367/4]
Pestiviruses represent important pathogens of farm animals that have evolved unique strategies and functions to stay within their host populations. E-rns, a structural glycoprotein of pestiviruses, exhibits RNase activity and represents a virulence factor of the viruses. E-rns forms disulfide linked homodimers that are found in virions and virus-infected cells. Mutation or deletion of cysteine 171, the residue engaged in intermolecular disulfide bond formation, results in loss of dimerization as tested in coprecipitation and native protein gel electrophoresis analyses. Nevertheless, stable virus mutants with changes affecting cysteine codon 171 could be recovered in tissue culture. These mutants grew almost as well as the parental viruses and exhibited an RNase-positive phenotype. E-rns dimerization-negative mutants of classical swine fever virus were found to be attenuated in pigs even though the virus clearly replicated and induced a significant neutralizing antibody response in the animals.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据