| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 3424405 | Virology | 2012 | 7 Pages |
Rice stripe virus (RSV) belongs to the genus Tenuivirus and its genome consists of four single-stranded RNAs encoding seven proteins. Here, we have analyzed the processing and membrane association of Pc2 encoded by vcRNA2 in insect cells. The enhanced green fluorescent protein (eGFP) was fused to the Pc2 and used for the detection of Pc2 fusion proteins. The results showed that Pc2 was cleaved to produce two proteins named Pc2-N and Pc2-C. When expressed alone, either Pc2-N or Pc2-C could transport to the Endoplasmic reticulum (ER) membranes independently. Further mutagenesis studies revealed that Pc2 contained three ER-targeting domains. The results led us to propose a model for the topology of the Pc2 in which an internal signal peptide immediately followed a cleavage site, and two transmembrane regions are contained.
► The processing and intracellular localization of RSV Pc2 have been studied in this article. ► The Pc2 precursor was partially processed to produce two proteins Pc2-N and Pc2-C. ► Either Pc2-N or Pc2-C could transport to the ER on its own. ► Further mutagenesis studies revealed that Pc2 contained three ER-targeting domains. ► A model for the topology of the Pc2 was proposed based on the results in this paper.
