Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/106041
Title: Protein-protein interactions of viroporins in coronaviruses and paramyxoviruses : new targets for antivirals?
Authors: Torres, Jaume
Surya, Wahyu
Li, Yan
Liu, Ding Xiang
Keywords: DRNTU::Science::Biological sciences::Microbiology::Bacteria
Issue Date: 2015
Source: Torres, J., Surya, W., Li, Y., & Liu, D. X. (2015). Protein-protein interactions of viroporins in coronaviruses and paramyxoviruses : new targets for antivirals? Viruses, 7(6), 2858-2883.
Series/Report no.: Viruses
Abstract: Viroporins are members of a rapidly growing family of channel-forming small polypeptides found in viruses. The present review will be focused on recent structural and protein-protein interaction information involving two viroporins found in enveloped viruses that target the respiratory tract; (i) the envelope protein in coronaviruses and (ii) the small hydrophobic protein in paramyxoviruses. Deletion of these two viroporins leads to viral attenuation in vivo, whereas data from cell culture shows involvement in the regulation of stress and inflammation. The channel activity and structure of some representative members of these viroporins have been recently characterized in some detail. In addition, searches for protein-protein interactions using yeast-two hybrid techniques have shed light on possible functional roles for their exposed cytoplasmic domains. A deeper analysis of these interactions should not only provide a more complete overview of the multiple functions of these viroporins, but also suggest novel strategies that target protein-protein interactions as much needed antivirals. These should complement current efforts to block viroporin channel activity.
URI: https://hdl.handle.net/10356/106041
http://hdl.handle.net/10220/26274
ISSN: 1999-4915
DOI: 10.3390/v7062750
Rights: © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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