Department of Neurology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-4283, USA.
Virology. 2010 Sep 1;404(2):139-47. doi: 10.1016/j.virol.2010.04.012. Epub 2010 May 31.
La Crosse virus is a leading cause of pediatric encephalitis in the Midwestern United States and an emerging pathogen in the American South. The LACV glycoprotein Gc plays a critical role in entry as the virus attachment protein. A 22 amino acid hydrophobic region within Gc (1066-1087) was recently identified as the LACV fusion peptide. To further define the role of Gc (1066-1087) in virus entry, fusion, and neuropathogenesis, a panel of recombinant LACV (rLACV) fusion peptide mutant viruses was generated. Replication of mutant rLACVs was significantly reduced. In addition, the fusion peptide mutants demonstrated decreased fusion phenotypes relative to LACV-WT. Interestingly, these viruses maintained their ability to cause neuronal loss in culture, suggesting that the fusion peptide of LACV Gc is a determinant of properties associated with neuroinvasion (growth to high titer in muscle cells and a robust fusion phenotype), but not necessarily of neurovirulence.
拉科罗拉多病毒是美国中西部儿童脑炎的主要病因，也是美国南部新兴的病原体。拉科罗拉多病毒糖蛋白 Gc 作为病毒附着蛋白，在进入过程中起着关键作用。最近发现 Gc（1066-1087）内的 22 个氨基酸疏水区是拉科罗拉多病毒融合肽。为了进一步确定 Gc（1066-1087）在病毒进入、融合和神经发病机制中的作用，生成了一组重组拉科罗拉多病毒（rLACV）融合肽突变病毒。突变体 rLACV 的复制明显减少。此外，与 LACV-WT 相比，融合肽突变体显示出降低的融合表型。有趣的是，这些病毒在培养物中仍保持引起神经元丧失的能力，这表明拉科罗拉多病毒 Gc 的融合肽是与神经入侵相关的特性（在肌肉细胞中高滴度生长和强烈的融合表型）的决定因素，但不一定是神经毒力的决定因素。
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