Viroporin activity and membrane topology of classic swine fever virus p7 protein
Viroporins are a group of viral proteins that participate in viral replication cycles, including modification of membrane permeability and promotion of viral release. Although biological data have been accumulated on viroporion-like proteins of other viruses belonging to family Flaviviridae, the vir...
| Main Authors: | , , , , , , , , , , |
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| Format: | Journal Article |
| Language: | English |
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2013
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| Online Access: | https://hdl.handle.net/10356/98696 http://hdl.handle.net/10220/16950 |
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| author | Guo, Hui-Chen Sun, Shi-Qi Sun, De-Hui Wei, Yan-Quan Xu, Jin Huang, Mei Liu, Xiang-Tao Liu, Zai-Xin Luo, Jian-Xiong Yin, Hong Liu, Ding Xiang |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Guo, Hui-Chen Sun, Shi-Qi Sun, De-Hui Wei, Yan-Quan Xu, Jin Huang, Mei Liu, Xiang-Tao Liu, Zai-Xin Luo, Jian-Xiong Yin, Hong Liu, Ding Xiang |
| author_sort | Guo, Hui-Chen |
| collection | NTU |
| description | Viroporins are a group of viral proteins that participate in viral replication cycles, including modification of membrane permeability and promotion of viral release. Although biological data have been accumulated on viroporion-like proteins of other viruses belonging to family Flaviviridae, the viroporin activity and membrane topology of p7 protein from classical swine fever virus (CSFV), a member of the genus Pestivirus of the family Flaviviridae, are largely unknown. In this study, sequence analysis of the primary structure of p7 polypeptide demonstrates that p7 contains two putative transmembrane regions connected by a short hydrophilic segment. Expression of p7 protein in Escherichia coli leads to the permeabilization of bacterial cells to small molecules. The p7 protein also enhances the permeability of mammalian cells, increasing the intracellular Ca2+ concentration and the permeability of cells to the translation inhibitor Hygromycin B. This protein is an integral membrane protein and can form homo-oligomers. It mainly localizes to the ER at the early stage of the expression and can be transferred to the plasma membrane at the late stage of the expression. Detergent permeabilization assays confirmed that the p7 protein is a 2-pass transmembrane protein and its N and C termini are exposed to the ER lumen. Deletion analysis showed that amino acid residues 41–63 may be essential for the viroporin activity of the protein. Our studies demonstrate that CSFV p7 possesses properties commonly associated with viroporins, which could be a potential target for the development of a therapeutic intervention for classic swine fever virus infection. |
| first_indexed | 2024-10-01T07:30:34Z |
| format | Journal Article |
| id | ntu-10356/98696 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:30:34Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/986962020-03-07T12:18:14Z Viroporin activity and membrane topology of classic swine fever virus p7 protein Guo, Hui-Chen Sun, Shi-Qi Sun, De-Hui Wei, Yan-Quan Xu, Jin Huang, Mei Liu, Xiang-Tao Liu, Zai-Xin Luo, Jian-Xiong Yin, Hong Liu, Ding Xiang School of Biological Sciences DRNTU::Science::Biological sciences Viroporins are a group of viral proteins that participate in viral replication cycles, including modification of membrane permeability and promotion of viral release. Although biological data have been accumulated on viroporion-like proteins of other viruses belonging to family Flaviviridae, the viroporin activity and membrane topology of p7 protein from classical swine fever virus (CSFV), a member of the genus Pestivirus of the family Flaviviridae, are largely unknown. In this study, sequence analysis of the primary structure of p7 polypeptide demonstrates that p7 contains two putative transmembrane regions connected by a short hydrophilic segment. Expression of p7 protein in Escherichia coli leads to the permeabilization of bacterial cells to small molecules. The p7 protein also enhances the permeability of mammalian cells, increasing the intracellular Ca2+ concentration and the permeability of cells to the translation inhibitor Hygromycin B. This protein is an integral membrane protein and can form homo-oligomers. It mainly localizes to the ER at the early stage of the expression and can be transferred to the plasma membrane at the late stage of the expression. Detergent permeabilization assays confirmed that the p7 protein is a 2-pass transmembrane protein and its N and C termini are exposed to the ER lumen. Deletion analysis showed that amino acid residues 41–63 may be essential for the viroporin activity of the protein. Our studies demonstrate that CSFV p7 possesses properties commonly associated with viroporins, which could be a potential target for the development of a therapeutic intervention for classic swine fever virus infection. 2013-10-28T03:08:15Z 2019-12-06T19:58:34Z 2013-10-28T03:08:15Z 2019-12-06T19:58:34Z 2013 2013 Journal Article Guo, H.-C., Sun, S.-Q., Sun, D.-H., Wei, Y.-Q., Xu, J., Huang, M., et al. (2013). Viroporin activity and membrane topology of classic swine fever virus p7 protein. The International Journal of Biochemistry & Cell Biology, 45(7), 1186-1194. 1357-2725 https://hdl.handle.net/10356/98696 http://hdl.handle.net/10220/16950 10.1016/j.biocel.2013.03.021 en The international journal of biochemistry & cell biology |
| spellingShingle | DRNTU::Science::Biological sciences Guo, Hui-Chen Sun, Shi-Qi Sun, De-Hui Wei, Yan-Quan Xu, Jin Huang, Mei Liu, Xiang-Tao Liu, Zai-Xin Luo, Jian-Xiong Yin, Hong Liu, Ding Xiang Viroporin activity and membrane topology of classic swine fever virus p7 protein |
| title | Viroporin activity and membrane topology of classic swine fever virus p7 protein |
| title_full | Viroporin activity and membrane topology of classic swine fever virus p7 protein |
| title_fullStr | Viroporin activity and membrane topology of classic swine fever virus p7 protein |
| title_full_unstemmed | Viroporin activity and membrane topology of classic swine fever virus p7 protein |
| title_short | Viroporin activity and membrane topology of classic swine fever virus p7 protein |
| title_sort | viroporin activity and membrane topology of classic swine fever virus p7 protein |
| topic | DRNTU::Science::Biological sciences |
| url | https://hdl.handle.net/10356/98696 http://hdl.handle.net/10220/16950 |
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