The Complex Proteolipidic Behavior of the SARS-CoV-2 Envelope Protein Channel: Weak Selectivity and Heterogeneous Oligomerization
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Otros documentos de la autoría: Surya, Wahyu; Tavares Neto, Ernesto; Sanchis, Andrea; Queralt-Martín, María; Alcaraz, Antonio; Torres, Jaume; Aguilella, Vicente
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Título
The Complex Proteolipidic Behavior of the SARS-CoV-2 Envelope Protein Channel: Weak Selectivity and Heterogeneous OligomerizationAutoría
Fecha de publicación
2023-08-05Editor
Multidisciplinary Digital Publishing Institute (MDPI)ISSN
1661-6596Cita bibliográfica
SURYA, Wahyu, et al. The Complex Proteolipidic Behavior of the SARS-CoV-2 Envelope Protein Channel: Weak Selectivity and Heterogeneous Oligomerization. International Journal of Molecular Sciences, 2023, vol. 24, no 15, p. 12454.Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
https://www.mdpi.com/1422-0067/24/15/12454Versión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
The envelope (E) protein is a small polypeptide that can form ion channels in coronaviruses. In SARS coronavirus 2 (SARS-CoV-2), the agent that caused the recent COVID-19 pandemic, and its predecessor SARS-CoV-1, E ... [+]
The envelope (E) protein is a small polypeptide that can form ion channels in coronaviruses. In SARS coronavirus 2 (SARS-CoV-2), the agent that caused the recent COVID-19 pandemic, and its predecessor SARS-CoV-1, E protein is found in the endoplasmic reticulum–Golgi intermediate compartment (ERGIC), where virion budding takes place. Several reports claim that E protein promotes the formation of “cation-selective channels”. However, whether this term represents specificity to certain ions (e.g., potassium or calcium) or the partial or total exclusion of anions is debatable. Herein, we discuss this claim based on the available data for SARS-CoV-1 and -2 E and on new experiments performed using the untagged full-length E protein from SARS-CoV-2 in planar lipid membranes of different types, including those that closely mimic the ERGIC membrane composition. We provide evidence that the selectivity of the E-induced channels is very mild and depends strongly on lipid environment. Thus, despite past and recent claims, we found no indication that the E protein forms cation-selective channels that prevent anion transport, and even less that E protein forms bona fide specific calcium channels. In fact, the E channel maintains its multi-ionic non-specific neutral character even in concentrated solutions of Ca2+ ions. Also, in contrast to previous studies, we found no evidence that SARS-CoV-2 E channel activation requires a particular voltage, high calcium concentrations or low pH, in agreement with available data from SARS-CoV-1 E. In addition, sedimentation velocity experiments suggest that the E channel population is mostly pentameric, but very dynamic and probably heterogeneous, consistent with the broad distribution of conductance values typically found in electrophysiological experiments. The latter has been explained by the presence of proteolipidic channel structures. [-]
Publicado en
International Journal of Molecular Sciences, Volume 24, Issue 15 (August 2023) Article number 12454Entidad financiadora
Spanish Government | Ministry of Education - Singapore | Universitat Jaume I
Código del proyecto o subvención
2019-108434GB-I00, MCIN/AEI/10.13039/501100011033 | RG92/21 | UJI-B2022-42
Derechos de acceso
© 2023 by the authors.
info:eu-repo/semantics/openAccess
info:eu-repo/semantics/openAccess
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