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MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels
dc.contributor.author | Surya, Wahyu | |
dc.contributor.author | Li, Yan | |
dc.contributor.author | Verdiá Báguena, Carmen | |
dc.contributor.author | Aguilella, Vicente | |
dc.contributor.author | Torres, Jaume | |
dc.date.accessioned | 2016-03-22T12:36:37Z | |
dc.date.available | 2016-03-22T12:36:37Z | |
dc.date.issued | 2015-04 | |
dc.identifier.citation | SURYA, Wahyu, et al. MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels. Virus research, 2015, vol. 201, p. 61-66. | ca_CA |
dc.identifier.uri | http://hdl.handle.net/10234/154885 | |
dc.description.abstract | The Middle East respiratory syndrome coronavirus (MERS-CoV) is a newly identified pathogen able of human transmission that causes a mortality of almost 40%. As in the case of SARS-CoV, MERS virus lacking E protein represents a potential vaccine. In both cases, abolishment of channel activity may be a contributor to the attenuation observed in E-deleted viruses. Herein, we report that purified MERS-CoV E protein, like SARS-CoV E protein, is almost fully α-helical, has a single α-helical transmembrane domain, and forms pentameric ion channels in lipid bilayers. Based on these similarities, and the proposed involvement of channel activity as virulence factor in SARS-CoV E protein, MERS-CoV E protein may constitute a potential drug target. | ca_CA |
dc.format.extent | 5 p. | ca_CA |
dc.format.mimetype | application/pdf | ca_CA |
dc.language.iso | eng | ca_CA |
dc.publisher | Elsevier | ca_CA |
dc.relation.isPartOf | Virus Research Volume 201, April 2015 | ca_CA |
dc.rights | Copyright © 2015 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. | ca_CA |
dc.rights.uri | http://rightsstatements.org/vocab/InC/1.0/ | * |
dc.subject | Middle East respiratory syndrome coronavirus (MERS) | ca_CA |
dc.subject | Envelope protein | ca_CA |
dc.subject | Ion channel | ca_CA |
dc.subject | Purification | ca_CA |
dc.subject | Oligomeric state | ca_CA |
dc.title | MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels | ca_CA |
dc.type | info:eu-repo/semantics/article | ca_CA |
dc.identifier.doi | http://dx.doi.org/10.1016/j.virusres.2015.02.023 | |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | ca_CA |
dc.relation.publisherVersion | http://www.sciencedirect.com/science/article/pii/S0168170215001136 | ca_CA |
dc.type.version | info:eu-repo/semantics/publishedVersion |
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