Please use this identifier to cite or link to this item:
https://hdl.handle.net/10356/103364
Title: | Viroporin activity of the foot-and-mouth disease virus non-structural 2B protein | Authors: | Ao, Da Guo, Hui-Chen Sun, Shi-Qi Sun, De-Hui Fung, To Sing Wei, Yan-Quan Han, Shi-Chong Yao, Xue-Ping Cao, Sui-Zhong Liu, Ding Xiang Liu, Xiang-Tao |
Keywords: | DRNTU::Science::Biological sciences | Issue Date: | 2015 | Source: | Ao, D., Guo, H.-C., Sun, S.-Q., Sun, D.-H., Fung, T. S., Wei, Y.-Q., et al. (2015). Viroporin activity of the foot-and-mouth disease virus non-structural 2B protein. PLOS One, 10(5), e0125828-. | Series/Report no.: | PLOS One | Abstract: | Viroporins are a family of low-molecular-weight hydrophobic transmembrane proteins that are encoded by various animal viruses. Viroporins form transmembrane pores in host cells via oligomerization, thereby destroying cellular homeostasis and inducing cytopathy for virus replication and virion release. Among the Picornaviridae family of viruses, the 2B protein encoded by enteroviruses is well understood, whereas the viroporin activity of the 2B protein encoded by the foot-and-mouth disease virus (FMDV) has not yet been described. An analysis of the FMDV 2B protein domains by computer-aided programs conducted in this study revealed that this protein may contain two transmembrane regions. Further biochemical, biophysical and functional studies revealed that the protein possesses a number of features typical of a viroporin when it is overexpressed in bacterial and mammalian cells as well as in FMDV-infected cells. The protein was found to be mainly localized in the endoplasmic reticulum (ER), with both the N- and C-terminal domains stretched into the cytosol. It exhibited cytotoxicity in Escherichia coli, which attenuated 2B protein expression. The release of virions from cells infected with FMDV was inhibited by amantadine, a viroporin inhibitor. The 2B protein monomers interacted with each other to form both intracellular and extracellular oligomers. The Ca2+ concentration in the cells increased, and the integrity of the cytoplasmic membrane was disrupted in cells that expressed the 2B protein. Moreover, the 2B protein induced intense autophagy in host cells. All of the results of this study demonstrate that the FMDV 2B protein has properties that are also found in other viroporins and may be involved in the infection mechanism of FMDV. | URI: | https://hdl.handle.net/10356/103364 http://hdl.handle.net/10220/25827 |
ISSN: | 1932-6203 | DOI: | 10.1371/journal.pone.0125828 | Schools: | School of Biological Sciences | Rights: | © 2015 Ao et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. | Fulltext Permission: | open | Fulltext Availability: | With Fulltext |
Appears in Collections: | SBS Journal Articles |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Viroporin activity of the foot-and-mouth disease virus non-structural 2B protein.pdf | 1.2 MB | Adobe PDF | View/Open |
SCOPUSTM
Citations
10
40
Updated on Mar 25, 2024
Web of ScienceTM
Citations
10
39
Updated on Oct 29, 2023
Page view(s) 50
433
Updated on Mar 28, 2024
Download(s) 20
200
Updated on Mar 28, 2024
Google ScholarTM
Check
Altmetric
Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.