Cargando…
A Functional K(+) Channel from Tetraselmis Virus 1, a Member of the Mimiviridae
Potassium ion (K(+)) channels have been observed in diverse viruses that infect eukaryotic marine and freshwater algae. However, experimental evidence for functional K(+) channels among these alga-infecting viruses has thus far been restricted to members of the family Phycodnaviridae, which are larg...
Autores principales: | , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7650704/ https://www.ncbi.nlm.nih.gov/pubmed/33003637 http://dx.doi.org/10.3390/v12101107 |
_version_ | 1783607538332205056 |
---|---|
author | Kukovetz, Kerri Hertel, Brigitte Schvarcz, Christopher R. Saponaro, Andrea Manthey, Mirja Burk, Ulrike Greiner, Timo Steward, Grieg F. Van Etten, James L. Moroni, Anna Thiel, Gerhard Rauh, Oliver |
author_facet | Kukovetz, Kerri Hertel, Brigitte Schvarcz, Christopher R. Saponaro, Andrea Manthey, Mirja Burk, Ulrike Greiner, Timo Steward, Grieg F. Van Etten, James L. Moroni, Anna Thiel, Gerhard Rauh, Oliver |
author_sort | Kukovetz, Kerri |
collection | PubMed |
description | Potassium ion (K(+)) channels have been observed in diverse viruses that infect eukaryotic marine and freshwater algae. However, experimental evidence for functional K(+) channels among these alga-infecting viruses has thus far been restricted to members of the family Phycodnaviridae, which are large, double-stranded DNA viruses within the phylum Nucleocytoviricota. Recent sequencing projects revealed that alga-infecting members of Mimiviridae, another family within this phylum, may also contain genes encoding K(+) channels. Here we examine the structural features and the functional properties of putative K(+) channels from four cultivated members of Mimiviridae. While all four proteins contain variations of the conserved selectivity filter sequence of K(+) channels, structural prediction algorithms suggest that only two of them have the required number and position of two transmembrane domains that are present in all K(+) channels. After in vitro translation and reconstitution of the four proteins in planar lipid bilayers, we confirmed that one of them, a 79 amino acid protein from the virus Tetraselmis virus 1 (TetV-1), forms a functional ion channel with a distinct selectivity for K(+) over Na(+) and a sensitivity to Ba(2+). Thus, virus-encoded K(+) channels are not limited to Phycodnaviridae but also occur in the members of Mimiviridae. The large sequence diversity among the viral K(+) channels implies multiple events of lateral gene transfer. |
format | Online Article Text |
id | pubmed-7650704 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76507042020-11-10 A Functional K(+) Channel from Tetraselmis Virus 1, a Member of the Mimiviridae Kukovetz, Kerri Hertel, Brigitte Schvarcz, Christopher R. Saponaro, Andrea Manthey, Mirja Burk, Ulrike Greiner, Timo Steward, Grieg F. Van Etten, James L. Moroni, Anna Thiel, Gerhard Rauh, Oliver Viruses Article Potassium ion (K(+)) channels have been observed in diverse viruses that infect eukaryotic marine and freshwater algae. However, experimental evidence for functional K(+) channels among these alga-infecting viruses has thus far been restricted to members of the family Phycodnaviridae, which are large, double-stranded DNA viruses within the phylum Nucleocytoviricota. Recent sequencing projects revealed that alga-infecting members of Mimiviridae, another family within this phylum, may also contain genes encoding K(+) channels. Here we examine the structural features and the functional properties of putative K(+) channels from four cultivated members of Mimiviridae. While all four proteins contain variations of the conserved selectivity filter sequence of K(+) channels, structural prediction algorithms suggest that only two of them have the required number and position of two transmembrane domains that are present in all K(+) channels. After in vitro translation and reconstitution of the four proteins in planar lipid bilayers, we confirmed that one of them, a 79 amino acid protein from the virus Tetraselmis virus 1 (TetV-1), forms a functional ion channel with a distinct selectivity for K(+) over Na(+) and a sensitivity to Ba(2+). Thus, virus-encoded K(+) channels are not limited to Phycodnaviridae but also occur in the members of Mimiviridae. The large sequence diversity among the viral K(+) channels implies multiple events of lateral gene transfer. MDPI 2020-09-29 /pmc/articles/PMC7650704/ /pubmed/33003637 http://dx.doi.org/10.3390/v12101107 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Kukovetz, Kerri Hertel, Brigitte Schvarcz, Christopher R. Saponaro, Andrea Manthey, Mirja Burk, Ulrike Greiner, Timo Steward, Grieg F. Van Etten, James L. Moroni, Anna Thiel, Gerhard Rauh, Oliver A Functional K(+) Channel from Tetraselmis Virus 1, a Member of the Mimiviridae |
title | A Functional K(+) Channel from Tetraselmis Virus 1, a Member of the Mimiviridae |
title_full | A Functional K(+) Channel from Tetraselmis Virus 1, a Member of the Mimiviridae |
title_fullStr | A Functional K(+) Channel from Tetraselmis Virus 1, a Member of the Mimiviridae |
title_full_unstemmed | A Functional K(+) Channel from Tetraselmis Virus 1, a Member of the Mimiviridae |
title_short | A Functional K(+) Channel from Tetraselmis Virus 1, a Member of the Mimiviridae |
title_sort | functional k(+) channel from tetraselmis virus 1, a member of the mimiviridae |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7650704/ https://www.ncbi.nlm.nih.gov/pubmed/33003637 http://dx.doi.org/10.3390/v12101107 |
work_keys_str_mv | AT kukovetzkerri afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT hertelbrigitte afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT schvarczchristopherr afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT saponaroandrea afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT mantheymirja afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT burkulrike afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT greinertimo afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT stewardgriegf afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT vanettenjamesl afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT moronianna afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT thielgerhard afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT rauholiver afunctionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT kukovetzkerri functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT hertelbrigitte functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT schvarczchristopherr functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT saponaroandrea functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT mantheymirja functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT burkulrike functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT greinertimo functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT stewardgriegf functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT vanettenjamesl functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT moronianna functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT thielgerhard functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae AT rauholiver functionalkchannelfromtetraselmisvirus1amemberofthemimiviridae |