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Peer-reviewedCC BY 4.0Proceedings of the National Academy of Sciences of the United States of America

A functional two-pore-domain K+ channel from a large DNA virus

  • Oliver Rauh1
  • Sebastian Mach2
  • Oliver Clarke3,4
  • Jonas Toews1
  • James L. Van Etten5
  • Mike Althaus1
  • Anna Moroni6
  • Gerhard Thiel2,6
6 affiliations
  1. 1Institute for Functional Gene Analytics, Department of Natural Sciences, Bonn-Rhein-Sieg University of Applied Sciences, Rheinbach 53359, Germany
  2. 2Department of Biology, Membrane Biophysics, Technische Universität Darmstadt, Darmstadt 64287, Germany
  3. 3Department of Anesthesiology, Columbia University Irving Medical Center, New York, NY 10032
  4. 4Department of Biology, Irving Institute for Clinical and Translational Research, Columbia University, New York, NY 10032
  5. 5Department of Plant Pathology and Nebraska Center for Virology, University of Nebraska Lincoln, Lincoln, NE 68583-0900
  6. 6Department of Biosciences, University of Milan, Milan 20133, Italy
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Abstract

The evolutionary history of proteins helps to understand their structure/function correlates and suggests on how functional complexity evolved from primitive precursors. In the superfamily of K+ channels, functional features of complex eukaryotic inward rectifier (Kir) channels and voltage-dependent (Kv) channels could be understood in terms of an increase in structural complexity of their prokaryotic precursors. K2P channels, which are made from tandem repeats of two pore domains, are not found in prokaryotes and their evolutionary origin is still unknown. In searching for primitive K2P channel precursors, we screened the genomes of nucleocytoplasmic large DNA viruses (NCLDVs) for genes coding for K2P channels. This was motivated by two reasons: NCLDVs are already known for coding primitive Kir type channels, and they play important roles in the evolution of eukaryotes. Here, we report that the NCLDV Pyramimonas orientalis virus codes for K2P-like K+ channels. With only 178 amino acids and no cytosolic domains, this Kpov protein is much smaller than any eukaryotic K2P channel, but still functional as K+ selective channel in lipid bilayers. Phylogenetic analysis suggests that Kpov is not the product of molecular piracy from the host but may result from fusion of primitive viral K+ channel pore domains.

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Cite

BibTeXRIS
BibTeX
@article{rauh2026functional,
  title = {{A functional two-pore-domain K+ channel from a large DNA virus}},
  author = {Oliver Rauh and Sebastian Mach and Oliver Clarke and Jonas Toews and James L. Van Etten and Mike Althaus and Anna Moroni and Gerhard Thiel},
  journal = {Proceedings of the National Academy of Sciences of the United States of America},
  year = {2026},
  month = oct,
  doi = {10.1073/pnas.2626158123},
  url = {https://doi.org/10.1073/pnas.2626158123},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - A functional two-pore-domain K+ channel from a large DNA virus
AU  - Oliver Rauh
AU  - Sebastian Mach
AU  - Oliver Clarke
AU  - Jonas Toews
AU  - James L. Van Etten
AU  - Mike Althaus
AU  - Anna Moroni
AU  - Gerhard Thiel
PY  - 2026
DA  - 2026/10/23
JO  - Proceedings of the National Academy of Sciences of the United States of America
DO  - 10.1073/pnas.2626158123
UR  - https://doi.org/10.1073/pnas.2626158123
AB  - The evolutionary history of proteins helps to understand their structure/function correlates and suggests on how functional complexity evolved from primitive precursors. In the superfamily of K+ channels, functional features of complex eukaryotic inward rectifier (Kir) channels and voltage-dependent (Kv) channels could be understood in terms of an increase in structural complexity of their prokaryotic precursors. K2P channels, which are made from tandem repeats of two pore domains, are not found in prokaryotes and their evolutionary origin is still unknown. In searching for primitive K2P channel precursors, we screened the genomes of nucleocytoplasmic large DNA viruses (NCLDVs) for genes coding for K2P channels. This was motivated by two reasons: NCLDVs are already known for coding primitive Kir type channels, and they play important roles in the evolution of eukaryotes. Here, we report that the NCLDV Pyramimonas orientalis virus codes for K2P-like K+ channels. With only 178 amino acids and no cytosolic domains, this Kpov protein is much smaller than any eukaryotic K2P channel, but still functional as K+ selective channel in lipid bilayers. Phylogenetic analysis suggests that Kpov is not the product of molecular piracy from the host but may result from fusion of primitive viral K+ channel pore domains.
SN  - 0027-8424
SN  - 1091-6490
ER  -