Ciancanelli Michael J, Basler Christopher F
Department of Microbiology, Box 1124, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029, USA.
J Virol. 2006 Dec;80(24):12070-8. doi: 10.1128/JVI.01743-06. Epub 2006 Sep 27.
Matrix (M) proteins reportedly direct the budding of paramyxoviruses from infected cells. In order to begin to characterize the assembly process for the highly lethal, emerging paramyxovirus Nipah virus (NiV), we have examined the budding of NiV M. We demonstrated that expression of the NiV M protein is sufficient to produce budding virus-like particles (VLPs) that are physically and morphologically similar to NiV. We identified in NiV M a sequence, YMYL, with similarity to the YPDL late domain found in the equine infectious anemia virus Gag protein. When the YMYL within NiV M was mutated, VLP release was abolished and M was relocalized to the nucleus, but the mutant M proteins retained oligomerization activity. When YMYL was fused to a late-domain mutant of the Ebola virus VP40 matrix protein, VP40 budding was restored. These results suggest that the YMYL sequence may act as a trafficking signal and a late domain for NiV M.
据报道，基质（M）蛋白指导副粘病毒从受感染细胞中出芽。为了开始表征高致死性新兴副粘病毒尼帕病毒（NiV）的组装过程，我们研究了NiV M的出芽情况。我们证明，NiV M蛋白的表达足以产生在物理和形态上与NiV相似的出芽病毒样颗粒（VLP）。我们在NiV M中鉴定出一个序列YMYL，它与马传染性贫血病毒Gag蛋白中的YPDL晚期结构域相似。当NiV M中的YMYL发生突变时，VLP释放被消除，M重新定位到细胞核，但突变的M蛋白保留了寡聚化活性。当YMYL与埃博拉病毒VP40基质蛋白的晚期结构域突变体融合时，VP40出芽得以恢复。这些结果表明，YMYL序列可能作为NiV M的转运信号和晚期结构域。
