Feldmann H, Volchkov V E, Volchkova V A, Klenk H D
Institut für Virologie, Philipps-Universität Marburg, Germany.
Arch Virol Suppl. 1999;15:159-69. doi: 10.1007/978-3-7091-6425-9_11.
Filoviruses cause systemic infections that can lead to severe hemorrhagic fever in human and non-human primates. The primary target of the virus appears to be the mononuclear phagocytic system. As the virus spreads through the organism, the spectrum of target cells increases to include endothelial cells, fibroblasts, hepatocytes, and many other cells. There is evidence that the filovirus glycoprotein plays an important role in cell tropism, spread of infection, and pathogenicity. Biosynthesis of the glycoprotein forming the spikes on the virion surface involves cleavage by the host cell protease furin into two disulfide linked subunits GP1 and GP2. GP1 is also shed in soluble form from infected cells. Different strains of Ebola virus show variations in the cleavability of the glycoprotein, that may account for differences in pathogenicity, as has been observed with influenza viruses and paramyxoviruses. Expression of the spike glycoprotein of Ebola virus, but not of Marburg virus, requires transcriptional editing. Unedited GP mRNA yields the nonstructural glycoprotein sGP, which is secreted extensively from infected cells. Whether the soluble glycoproteins GP1 and sGP interfere with the humoral immune response and other defense mechanisms remains to be determined.
丝状病毒可引发全身性感染，在人类和非人类灵长类动物中可导致严重的出血热。该病毒的主要靶标似乎是单核吞噬细胞系统。随着病毒在机体中传播，靶细胞的范围扩大，包括内皮细胞、成纤维细胞、肝细胞及许多其他细胞。有证据表明，丝状病毒糖蛋白在细胞嗜性、感染传播及致病性方面发挥重要作用。病毒粒子表面形成刺突的糖蛋白的生物合成涉及宿主细胞蛋白酶弗林蛋白酶将其切割成两个通过二硫键连接的亚基GP1和GP2。GP1也以可溶性形式从受感染细胞中脱落。不同株的埃博拉病毒在糖蛋白的可切割性方面存在差异，这可能解释了致病性的差异，正如在流感病毒和副粘病毒中所观察到的那样。埃博拉病毒刺突糖蛋白的表达需要转录编辑，而马尔堡病毒则不需要。未经编辑的GP mRNA产生非结构糖蛋白sGP，其从受感染细胞中大量分泌。可溶性糖蛋白GP1和sGP是否会干扰体液免疫反应及其他防御机制仍有待确定。
