Holzmann H, Stiasny K, York H, Dorner F, Kunz C, Heinz F X
Institute of Virology, University of Vienna, Austria.
Arch Virol. 1995;140(2):213-21. doi: 10.1007/BF01309857.
A set of ten monoconal antibodies (mabs) specific for the tick-borne encephalitis (TBE) virus envelope protein E were prepared and characterized with respect to their functional activities, the location of their binding sites on protein E and the involvement of their epitopes in acid pH-induced conformational changes and interactions with the precursor to the membrane protein (prM) in immature virions. The majority of these mabs mapped to the previously defined antigenic domain A. All of the mabs recognize parts of the E protein which undergo low pH-induced structural rearrangements believed to be necessary for the fusion activity of the virus, and six of the mabs define epitopes which are affected by the prM-E interaction in immature virions. They are therefore of potential value as specific reagents for studying the structure and function of protein E, as well as the function of the prM-E association. Five of the mabs exhibited neutralizing activity, and can therefore be used for the selection of escape mutants.
制备了一组针对蜱传脑炎（TBE）病毒包膜蛋白E的十种单克隆抗体（mab），并对其功能活性、在蛋白E上结合位点的位置以及其表位在酸性pH诱导的构象变化和与未成熟病毒粒子中膜蛋白前体（prM）相互作用中的参与情况进行了表征。这些mab中的大多数定位于先前定义的抗原结构域A。所有mab均识别E蛋白中经历低pH诱导的结构重排的部分，据信这对病毒的融合活性是必需的，并且其中六种mab定义了受未成熟病毒粒子中prM-E相互作用影响的表位。因此，它们作为研究蛋白E的结构和功能以及prM-E关联功能的特异性试剂具有潜在价值。其中五种mab表现出中和活性，因此可用于选择逃逸突变体。
