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Originally published In Press as doi:10.1074/jbc.M202018200 on March 13, 2002
J. Biol. Chem., Vol. 277, Issue 20, 17789-17796, May 17, 2002
Modification of Late Membrane Permeability in Avian
Reovirus-infected Cells
VIROPORIN ACTIVITY OF THE S1-ENCODED NONSTRUCTURAL p10
PROTEIN*
Gustavo
Bodelón,
Lucía
Labrada ,
José
Martínez-Costas, and
Javier
Benavente§
From the Departamento de Bioquímica y Biología
Molecular, Facultad de Farmacia, Universidad de Santiago de
Compostela, 15782 Santiago de Compostela, Spain
Infection of chicken embryo fibroblasts by avian
reovirus induces an increase in the permeability of the host plasma
membrane at late, but not early, infection times. The absence of
permeability changes at early infection times, as well as the
dependence of late membrane modification on both viral protein
synthesis and an active exocytic route, suggest that a virus-encoded
membrane protein is required for avian reovirus to permeabilize cells. Further studies revealed that expression of nonstructural p10 protein
in bacterial cells arrested cell growth and enhanced membrane permeability. Membrane leakiness was also observed following transient expression of p10 in BSC-40 monkey cells. Both its permeabilizing effect and the fact that p10 shares several structural and physical characteristics with other membrane-active viral proteins indicate that
p10 is an avian reovirus viroporin. Furthermore, the fusogenic extracellular NH2-terminal domain of p10 appears to
be dispensable for permeabilizing activity, because its deletion
entirely abolished the fusogenic activity of p10, without affecting its
ability to associate with cell membranes and to enhance membrane
permeability. Similar properties have reported previously for
immunodeficiency virus type I transmembrane glycoprotein gp41. Thus,
like gp41, p10 appears to be a multifunctional protein that
plays key roles in virus-host interaction.
*
This work was supported by Spanish Ministry of Science and
Technology Grant PB97-0523.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Dept. of Medicine, Columbia University College of
Physicians and Surgeons, New York, NY 10032.
§
To whom correspondence should be addressed. Tel./Fax:
34-981-599157; E-mail: bnjbena@usc.es.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.
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