Honeychurch Kady M, Yang Guang, Jordan Robert, Hruby Dennis E
Department of Microbiology, Oregon State University, 220 Nash Hall, Corvallis, OR 97331, USA.
J Virol. 2007 Jul;81(13):7310-5. doi: 10.1128/JVI.00034-07. Epub 2007 May 2.
The Tyr-X-X-Leu (YxxL) motif of the vaccinia virus F13L protein was examined for late (L) domain activity. The ability of an F13L deletion virus to form plaques was restored by PCR products containing single alanine substitutions within the motif and a YAAL construct but not by constructs lacking both the Y and L residues. Recombinant viruses possessing alanine substitutions in place of the tyrosine or the leucine residue in the YxxL motif demonstrated small, asymmetrical plaques. RNA interference-dependent depletion of Alix and TSG101 (host proteins involved in L domain-dependent protein trafficking) diminished extracellular enveloped virion production to various degrees, suggesting that the YxxL motif is a genuine L domain.
对痘苗病毒F13L蛋白的Tyr-X-X-Leu（YxxL）基序进行了晚期（L）结构域活性检测。通过在该基序内含有单个丙氨酸取代的PCR产物和一个YAAL构建体，可恢复F13L缺失病毒形成蚀斑的能力，但缺乏Y和L残基的构建体则不能恢复。在YxxL基序中，用丙氨酸取代酪氨酸或亮氨酸残基的重组病毒表现出小的、不对称的蚀斑。RNA干扰依赖性地消耗Alix和TSG101（参与L结构域依赖性蛋白质运输的宿主蛋白）会不同程度地减少细胞外被膜病毒粒子的产生，这表明YxxL基序是一个真正的L结构域。
