Biophysical characterization and vector-specific antagonist activity of domain III of the tick-borne flavivirus envelope protein
Biophysical characterization and vector-specific antagonist activity of domain III of the tick-borne flavivirus envelope protein
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DOI：
10.1128/jvi.75.8.4002-4007.2001
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发表时间：
2001-04-01
影响因子：
5.4
通讯作者：
Watowich, SJ
中科院分区：
文献类型：
--
作者：
Bhardwaj, S;Holbrook, M;Watowich, SJ
尽管包膜蛋白的结构域III与黄病毒的宿主细胞结合及组织嗜性这些功能有关，但负责这些功能的分子决定因素在很大程度上仍是未知的。我们研究了兰加特病毒结构域III的溶液特性和拮抗活性。我们的研究结果表明，结构域III采用一种稳定折叠的结构，它能够介导蜱传黄病毒而非蚊传黄病毒与其靶细胞的结合。我们确定了三组在系统发育上保守的残基，它们可能是结构域III的载体特异性拮抗活性的原因。
The molecular determinants responsible for flavivirus host cell binding and tissue tropism are largely unknown, although domain III of the envelope protein has been implicated in these functions. We examined the solution properties and antagonist activity of Langat virus domain III. Our results suggest that domain III adopts a stably folded structure that can mediate binding of tick-borne flaviviruses but not mosquito-borne flaviviruses to their target cells. Three clusters of phylogenetically conserved residues are identified that may be responsible for the vector-specific antagonist activity of domain III.