Membrane integration of poliovirus 2B viroporin
Entity
UAM. Departamento de Biología MolecularPublisher
American Society for MicrobiologyDate
2011-11-01Citation
10.1128/JVI.05421-11
Journal of Virology 85.21 (2011): 11315-11324
ISSN
1098-5514 (online)DOI
10.1128/JVI.05421-11Editor's Version
http://dx.doi.org/10.1128/JVI.05421-11Subjects
Virus; Amino acid sequence; Molecular sequence data; Biología y Biomedicina / BiologíaRights
© 2014, American Society for MicrobiologyAbstract
Virus infections can result in a variety of cellular injuries, and these often involve the permeabilization of host membranes by viral proteins of the viroporin family. Prototypical viroporin 2B is responsible for the alterations in host cell membrane permeability that take place in enterovirus-infected cells. 2B protein can be localized at the endoplasmic reticulum (ER) and the Golgi complex, inducing membrane remodeling and the blockade of glycoprotein trafficking. These findings suggest that 2B has the potential to integrate into the ER membrane, but specific information regarding its biogenesis and mechanism of membrane insertion is lacking. Here, we report experimental results of in vitro translation-glycosylation compatible with the transloconmediated insertion of the 2B product into the ER membrane as a double-spanning integral membrane protein with an N-/C-terminal cytoplasmic orientation. A similar topology was found when 2B was synthesized in cultured cells. In addition, the in vitro translation of several truncated versions of the 2B protein suggests that the two hydrophobic regions cooperate to insert into the ER-derived microsomal membranes
Files in this item
Google Scholar:Martínez-Gil, Luis
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Bañó-Polo, Manuel
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Redondo, Natalia
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Sánchez-Martínez, Silvia
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Nieva -, José Luis
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Carrasco, Luis
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Mingarro, Ismael
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