MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels
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Otros documentos de la autoría: Surya, Wahyu; Li, Yan; Verdiá Báguena, Carmen; Aguilella, Vicente; Torres, Jaume
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MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channelsFecha de publicación
2015-04Editor
ElsevierCita bibliográfica
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.Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://www.sciencedirect.com/science/article/pii/S0168170215001136Versión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
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 ... [+]
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. [-]
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Virus Research Volume 201, April 2015Derechos de acceso
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