Bhardwaj S, Holbrook M, Shope R E, Barrett A D, Watowich S J
Department of Human Biological Chemistry & Genetics and Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, Texas 77555, USA.
J Virol. 2001 Apr;75(8):4002-7. doi: 10.1128/JVI.75.8.4002-4007.2001.
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.
尽管包膜蛋白的结构域III被认为与这些功能有关，但负责黄病毒宿主细胞结合和组织嗜性的分子决定因素在很大程度上尚不清楚。我们研究了兰加特病毒结构域III的溶液特性和拮抗活性。我们的结果表明，结构域III采用稳定折叠的结构，可介导蜱传黄病毒而非蚊传黄病毒与其靶细胞的结合。鉴定出三个系统发育保守残基簇，它们可能负责结构域III的载体特异性拮抗活性。
