کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2048324 | 1074076 | 2012 | 8 صفحه PDF | دانلود رایگان |

Several studies suggest that the open reading frame 3 (ORF3) gene of porcine epidemic diarrhea virus (PEDV) is related to viral infectivity and pathogenicity, but its function remains unknown. Here, we propose a structure model of the ORF3 protein consisting of four TM domains and forming a tetrameric assembly. ORF3 protein can be detected in PEDV-infected cells and it functions as an ion channel in both Xenopus laevis oocytes and yeast. Mutation analysis showed that Tyr170 in TM4 is important for potassium channel activity. Furthermore, viral production is reduced in infected Vero cells when ORF3 gene is silenced by siRNA. Interestingly, the ORF3 gene from an attenuated PEDV encodes a truncated protein with 49 nucleotide deletions, which lacks the ion channel activity.
► Computational modeling of PEDV OFR3 protein.
► Wild-type PEDV ORF3 protein functions as an ion channel and regulates virus production.
► The truncated protein encoded by an attenuated-type PEDV ORF3 shows less channel activity.
Journal: FEBS Letters - Volume 586, Issue 4, 17 February 2012, Pages 384–391