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Viroporins, Examples of the Two-Stage Membrane Protein Folding Model

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Viroporins, Examples of the Two-Stage Membrane Protein Folding Model

dc.contributor.author	Martínez Gil, Luis
dc.contributor.author	Mingarro Muñoz, Ismael
dc.date.accessioned	2015-12-16T13:04:33Z
dc.date.available	2015-12-16T13:04:33Z
dc.date.issued	2015
dc.identifier.citation	Martínez Gil, Luis Mingarro Muñoz, Ismael 2015 Viroporins, Examples of the Two-Stage Membrane Protein Folding Model Viruses 7 7 3462 3482
dc.identifier.uri	http://hdl.handle.net/10550/49539
dc.description.abstract	Viroporins are small, α-helical, hydrophobic virus encoded proteins, engineered to form homo-oligomeric hydrophilic pores in the host membrane. Viroporins participate in multiple steps of the viral life cycle, from entry to budding. As any other membrane protein, viroporins have to find the way to bury their hydrophobic regions into the lipid bilayer. Once within the membrane, the hydrophobic helices of viroporins interact with each other to form higher ordered structures required to correctly perform their porating activities. This two-step process resembles the two-stage model proposed for membrane protein folding by Engelman and Poppot. In this review we use the membrane protein folding model as a leading thread to analyze the mechanism and forces behind the membrane insertion and folding of viroporins. We start by describing the transmembrane segment architecture of viroporins, including the number and sequence characteristics of their membrane-spanning domains. Next, we connect the differences found among viroporin families to their viral genome organization, and finalize focusing on the pathways used by viroporins in their way to the membrane and on the transmembrane helix-helix interactions required to achieve proper folding and assembly.
dc.language.iso	eng
dc.relation.ispartof	Viruses, 2015, vol. 7, num. 7, p. 3462-3482
dc.subject	Proteïnes
dc.subject	Virus
dc.subject	Genòmica
dc.subject	Genètica
dc.title	Viroporins, Examples of the Two-Stage Membrane Protein Folding Model
dc.type	journal article	es_ES
dc.date.updated	2015-12-16T13:04:34Z
dc.identifier.doi	10.3390/v7072781
dc.identifier.idgrec	107805
dc.rights.accessRights	open access	es_ES