包膜蛋白融合环中的突变可减弱西尼罗河病毒NY99株对小鼠的神经侵袭性。
A mutation in the envelope protein fusion loop attenuates mouse neuroinvasiveness of the NY99 strain of West Nile virus.
作者信息
Zhang Shuliu, Li Li, Woodson Sara E, Huang Claire Y-H, Kinney Richard M, Barrett Alan D T, Beasley David W C
机构信息
Department of Microbiology and Immunology, University of Texas Medical Branch, 301 University Blvd., Galveston, TX 77555-0609, USA.
出版信息
Virology. 2006 Sep 15;353(1):35-40. doi: 10.1016/j.virol.2006.05.025. Epub 2006 Jun 27.
Substitutions were engineered individually and in combinations at the fusion loop, receptor-binding domain and a stem-helix structure of the envelope protein of a West Nile virus strain, NY99, and their effects on mouse virulence and presentation of epitopes recognized by monoclonal antibodies (MAbs) were assessed. A single substitution within the fusion loop (L107F) attenuated mouse neuroinvasiveness of NY99. No substitutions attenuated NY99 neurovirulence. The L107F mutation also abolished binding of a non-neutralizing MAb, 3D9, whose epitope had not been previously identified. MAb 3D9 was subsequently shown to be broadly cross-reactive with other flaviviruses, consistent with binding near the highly conserved fusion loop.
对西尼罗河病毒株NY99包膜蛋白的融合环、受体结合域和茎螺旋结构进行了单独和组合的替换工程，并评估了它们对小鼠毒力以及单克隆抗体（MAb）识别的表位呈现的影响。融合环内的单个替换（L107F）减弱了NY99对小鼠的神经侵袭性。没有替换能减弱NY99的神经毒力。L107F突变也消除了非中和性单克隆抗体3D9的结合，其表位此前尚未确定。随后发现单克隆抗体3D9与其他黄病毒具有广泛的交叉反应性，这与在高度保守的融合环附近的结合一致。
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