Membrane permeabilization by poliovirus proteins 2B and 2BC - PubMed (original) (raw)

. 1996 Sep 20;271(38):23134-7.

doi: 10.1074/jbc.271.38.23134.

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Membrane permeabilization by poliovirus proteins 2B and 2BC

R Aldabe et al. J Biol Chem. 1996.

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Abstract

Poliovirus infection leads to drastic alterations in membrane permeability late during infection. Transient expression of each nonstructural protein of poliovirus by means of recombinant vaccinia virus encoding the T7 RNA polymerase indicates that proteins 2B and 2BC strongly enhance membrane permeability to hygromycin B in HeLa cells. Almost no effect on expression of proteins 2C, 3A, 3AB, and 3C was found. Deletions and point mutations in 2B and 2BC have identified sequences in 2B involved in membrane permeabilization. Regions located at both ends of 2B are necessary to bring about these permeability alterations. A deletion of 11 amino acids of 2BC at the junction between 2B and 2C, as well as long deletions in 2C encompassing the GTPase motifs of this protein, do not impair the capacity of 2BC to modify the permeability of the membrane. The release of compounds such as choline or uridine from preloaded cells is also augmented by 2B and 2BC expression.

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