Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/103364
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dc.contributor.authorAo, Daen
dc.contributor.authorGuo, Hui-Chenen
dc.contributor.authorSun, Shi-Qien
dc.contributor.authorSun, De-Huien
dc.contributor.authorFung, To Singen
dc.contributor.authorWei, Yan-Quanen
dc.contributor.authorHan, Shi-Chongen
dc.contributor.authorYao, Xue-Pingen
dc.contributor.authorCao, Sui-Zhongen
dc.contributor.authorLiu, Ding Xiangen
dc.contributor.authorLiu, Xiang-Taoen
dc.contributor.editorLiang, Chenen
dc.date.accessioned2015-06-08T04:54:25Zen
dc.date.accessioned2019-12-06T21:10:59Z-
dc.date.available2015-06-08T04:54:25Zen
dc.date.available2019-12-06T21:10:59Z-
dc.date.copyright2015en
dc.date.issued2015en
dc.identifier.citationAo, 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-.en
dc.identifier.issn1932-6203en
dc.identifier.urihttps://hdl.handle.net/10356/103364-
dc.description.abstractViroporins 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.en
dc.language.isoenen
dc.relation.ispartofseriesPLOS Oneen
dc.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.en
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleViroporin activity of the foot-and-mouth disease virus non-structural 2B proteinen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1371/journal.pone.0125828en
dc.description.versionPublished versionen
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