Department of Global Epidemiology, Hokkaido University Research Center for Zoonosis Control, Sapporo, Japan.
Biochem Biophys Res Commun. 2010 Dec 3;403(1):144-8. doi: 10.1016/j.bbrc.2010.10.136. Epub 2010 Nov 5.
Cellular C-type lectins have been reported to facilitate filovirus infection by binding to glycans on filovirus glycoprotein (GP). However, it is not clearly known whether interaction between C-type lectins and GP mediates all the steps of virus entry (i.e., attachment, internalization, and membrane fusion). In this study, we generated vesicular stomatitis viruses pseudotyped with mutant GPs that have impaired structures of the putative receptor binding regions and thus reduced ability to infect the monkey kidney cells that are routinely used for virus propagation. We found that infectivities of viruses with the mutant GPs dropped in C-type lectin-expressing cells, parallel with those in the monkey kidney cells, whereas binding activities of these GPs to the C-type lectins were not correlated with the reduced infectivities. These results suggest that C-type lectin-mediated entry of filoviruses requires other cellular molecule(s) that may be involved in virion internalization or membrane fusion.
细胞 C 型凝集素已被报道通过与丝状病毒糖蛋白 (GP) 上的聚糖结合来促进丝状病毒感染。然而，目前尚不清楚 C 型凝集素与 GP 之间的相互作用是否介导病毒进入的所有步骤（即附着、内化和膜融合）。在这项研究中，我们生成了带有突变 GP 的水疱性口炎病毒假型，这些突变 GP 的受体结合区结构受损，因此感染常规用于病毒繁殖的猴肾细胞的能力降低。我们发现，突变 GP 的病毒在表达 C 型凝集素的细胞中的感染性与在猴肾细胞中的感染性平行下降，而这些 GP 与 C 型凝集素的结合活性与降低的感染性不相关。这些结果表明，丝状病毒的 C 型凝集素介导的进入需要其他细胞分子，这些分子可能参与病毒的内化或膜融合。
