Single-molecule conformational dynamics of viroporin ion channels regulated by lipid-protein interactions
Impacto
Scholar |
Otros documentos de la autoría: Largo, Eneko; Queralt-Martín, María; Carravilla Palomanes, Pablo; Nieva, José L.; Alcaraz, Antonio
Metadatos
Mostrar el registro completo del ítemcomunitat-uji-handle:10234/9
comunitat-uji-handle2:10234/2507
comunitat-uji-handle3:10234/6973
comunitat-uji-handle4:
INVESTIGACIONMetadatos
Título
Single-molecule conformational dynamics of viroporin ion channels regulated by lipid-protein interactionsAutoría
Fecha de publicación
2020-02Editor
ElsevierISSN
1567-5394Cita bibliográfica
E. Largo, M. Queralt-Martín, P. Carravilla, J. L. Nieva, A. Alcaraz. Single-molecule conformational dynamics of viroporin ion channels regulated by lipid-protein interactions. Biochemistry, 137 (2021), pp. 107641, 10.1016/j.bioelechem.2020.107641Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
https://www.sciencedirect.com/science/article/pii/S1567539420304266#bi005Versión
info:eu-repo/semantics/submittedVersionPalabras clave / Materias
Resumen
Classic swine fever is a highly contagious and often fatal viral disease that is caused by the classical swine fever virus (CSFV). Protein p7 of CFSV is a prototype of viroporin, a family of small, highly hydrophobic ... [+]
Classic swine fever is a highly contagious and often fatal viral disease that is caused by the classical swine fever virus (CSFV). Protein p7 of CFSV is a prototype of viroporin, a family of small, highly hydrophobic proteins postulated to modulate virus-host interactions during the processes of virus entry, replication and assembly. It has been shown that CSFV p7 displays substantial ion channel activity when incorporated into membrane systems, but a deep rationalization of the size and dynamics of the induced pores is yet to emerge. Here, we use high-resolution conductance measurements and current fluctuation analysis to demonstrate that CSFV p7 channels are ruled by equilibrium conformational dynamics involving protein-lipid interactions. Atomic force microscopy (AFM) confirms the existence of a variety of pore sizes and their tight regulation by solution pH. We conclude that p7 viroporin forms subnanometric channels involved in virus propagation, but also much larger pores (1–10 nm in diameter) with potentially significant roles in virus pathogenicity. Our findings provide new insights into the sources of noise in protein electrochemistry and demonstrate the existence of slow complex dynamics characteristic of crowded systems like biomembrane surfaces. [-]
Publicado en
Bioelectrochemistry, 2021, vol. 137Derechos de acceso
Copyright © Elsevier B.V.
http://rightsstatements.org/vocab/InC/1.0/
info:eu-repo/semantics/openAccess
http://rightsstatements.org/vocab/InC/1.0/
info:eu-repo/semantics/openAccess
Aparece en las colecciones
- FCA_Articles [503]