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J. Biol. Chem., Vol. 277, Issue 49, 46923-46931, December 6, 2002

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Alphavirus 6K Proteins Form Ion Channels^*

Julian V. Melton, Gary D. Ewart^§, Ronald C. Weir^¶, Philip G. Board, Eva Lee, and Peter W. Gage^**

From the  Division of Molecular Bioscience, John Curtin School of Medical Research, The Australian National University, GPO Box 334, Canberra ACT 2601, Australia, ^§ Biotron Limited, LPO Box A315, Australian National University, Canberra ACT 2601, Australia, the ^¶ School of Biochemistry and Molecular Biology, The Australian National University, GPO Box 334, Canberra ACT 2601, Australia, and the  Division of Immunology and Genetics, John Curtin School of Medical Research, The Australian National University, GPO Box 334, Canberra ACT 2601, Australia

Ross River virus and Barmah Forest virus are Australian arboviruses of the Alphavirus genus. Features of alphavirus infection include an increased permeability of cells to monovalent cations followed by virion budding. Virally encoded ion channels are thought to have a role in these processes. In this paper, the 6K proteins of Ross River virus and Barmah Forest virus are shown to form cation-selective ion channels in planar lipid bilayers. Using a novel purification method, bacterially expressed 6K proteins were inserted into bilayers with a defined orientation (i.e. N-terminal cis, C-terminal trans). Channel activity was reversibly inhibited by antibodies to the N and C termini of 6K protein added to the cis and trans baths, respectively. Channel conductances varied from 40-800 picosiemens, suggesting that the protein is able to form channels with a range of possible oligomerization states.

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