Abstract
The large chlorella virus PBCV-1, which contains double-stranded DNA (dsDNA), encodes a 94-codon open reading frame (ORF) that contains a motif resembling the signature sequence of the pore domain of potassium channel proteins. Phylogenetic analyses of the encoded protein, Kcv, indicate a previously unidentified type of potassium channel. The messenger RNA encoded by the ORF leads to functional expression of a potassium-selective conductance in Xenopus laevis oocytes. The channel blockers amantadine and barium, but not cesium, inhibit this conductance, in addition to virus plaque formation. Thus, PBCV-1 encodes the first known viral protein that functions as a potassium-selective channel and is essential in the virus life cycle.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amantadine / pharmacology
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Barium / pharmacology
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Cesium / pharmacology
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Chlorella / virology
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Isoelectric Point
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Molecular Sequence Data
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Molecular Weight
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Oocytes
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Patch-Clamp Techniques
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Phycodnaviridae / chemistry
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Phycodnaviridae / drug effects
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Phycodnaviridae / genetics*
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Phycodnaviridae / physiology*
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Potassium / metabolism
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Potassium Channels / chemistry*
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Potassium Channels / genetics
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Potassium Channels / physiology*
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Recombinant Proteins / metabolism
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Sodium / metabolism
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Viral Plaque Assay
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Viral Proteins*
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Virus Replication / drug effects
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Xenopus laevis
Substances
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Kcv potassium channel, Chlorella virus
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Potassium Channels
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RNA, Messenger
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Recombinant Proteins
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Viral Proteins
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Cesium
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Barium
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Sodium
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Amantadine
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Potassium