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
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

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