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A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion
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| Veröffentlicht in: | Journal of general virology 94(2013), 11, Seite 2549-2556 |
|---|---|
| Personen und Körperschaften: | , |
| Titel: | A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion/ Giulia Romani, Adrianna Piotrowski, Stefan Hillmer, James Gurnon, James L. van Etten, Anna Moroni, Gerhard Thiel and Brigitte Hertel |
| Format: | E-Book-Kapitel |
| Sprache: | Englisch |
| veröffentlicht: |
01 November 2013
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| Gesamtaufnahme: |
: Journal of general virology, 94(2013), 11, Seite 2549-2556
, volume:94 |
| Quelle: | Verbunddaten SWB Lizenzfreie Online-Ressourcen |
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| 245 | 1 | 2 | |a A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion |c Giulia Romani, Adrianna Piotrowski, Stefan Hillmer, James Gurnon, James L. van Etten, Anna Moroni, Gerhard Thiel and Brigitte Hertel |
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| 520 | |a Most chloroviruses encode small K+ channels, which are functional in electrophysiological assays. The experimental finding that initial steps in viral infection exhibit the same sensitivity to channel inhibitors as the viral K+ channels has led to the hypothesis that the channels are structural proteins located in the internal membrane of the virus particles. This hypothesis was questioned recently because proteomic studies failed to detect the channel protein in virions of the prototype chlorovirus Paramecium bursaria chlorella virus 1 (PBCV-1). Here, we used a mAb raised against the functional K+ channel from chlorovirus MA-1D to search for the viral K+ channel in the virus particle. The results showed that the antibody was specific and bound to the tetrameric channel on the extracellular side. The antibody reacted in a virus-specific manner with protein extracts from chloroviruses that encoded channels similar to that from MA-1D. There was no cross-reactivity with chloroviruses that encoded more diverse channels or with a chlorovirus that lacked a K+ channel gene. Together with electron microscopic imaging, which revealed labelling of individual virus particles with the channel antibody, these results establish that the viral particles contain an active K+ channel, presumably located in the lipid membrane that surrounds the DNA in the mature virions. | ||
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| contents | Most chloroviruses encode small K+ channels, which are functional in electrophysiological assays. The experimental finding that initial steps in viral infection exhibit the same sensitivity to channel inhibitors as the viral K+ channels has led to the hypothesis that the channels are structural proteins located in the internal membrane of the virus particles. This hypothesis was questioned recently because proteomic studies failed to detect the channel protein in virions of the prototype chlorovirus Paramecium bursaria chlorella virus 1 (PBCV-1). Here, we used a mAb raised against the functional K+ channel from chlorovirus MA-1D to search for the viral K+ channel in the virus particle. The results showed that the antibody was specific and bound to the tetrameric channel on the extracellular side. The antibody reacted in a virus-specific manner with protein extracts from chloroviruses that encoded channels similar to that from MA-1D. There was no cross-reactivity with chloroviruses that encoded more diverse channels or with a chlorovirus that lacked a K+ channel gene. Together with electron microscopic imaging, which revealed labelling of individual virus particles with the channel antibody, these results establish that the viral particles contain an active K+ channel, presumably located in the lipid membrane that surrounds the DNA in the mature virions. |
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| spelling | Romani, Giulia VerfasserIn (DE-588)1136449507 (DE-627)89293459X (DE-576)490554601 aut, A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion Giulia Romani, Adrianna Piotrowski, Stefan Hillmer, James Gurnon, James L. van Etten, Anna Moroni, Gerhard Thiel and Brigitte Hertel, 01 November 2013, 8, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Gesehen am 06.07.2017, Most chloroviruses encode small K+ channels, which are functional in electrophysiological assays. The experimental finding that initial steps in viral infection exhibit the same sensitivity to channel inhibitors as the viral K+ channels has led to the hypothesis that the channels are structural proteins located in the internal membrane of the virus particles. This hypothesis was questioned recently because proteomic studies failed to detect the channel protein in virions of the prototype chlorovirus Paramecium bursaria chlorella virus 1 (PBCV-1). Here, we used a mAb raised against the functional K+ channel from chlorovirus MA-1D to search for the viral K+ channel in the virus particle. The results showed that the antibody was specific and bound to the tetrameric channel on the extracellular side. The antibody reacted in a virus-specific manner with protein extracts from chloroviruses that encoded channels similar to that from MA-1D. There was no cross-reactivity with chloroviruses that encoded more diverse channels or with a chlorovirus that lacked a K+ channel gene. Together with electron microscopic imaging, which revealed labelling of individual virus particles with the channel antibody, these results establish that the viral particles contain an active K+ channel, presumably located in the lipid membrane that surrounds the DNA in the mature virions., Hillmer, Stefan VerfasserIn (DE-588)1035578948 (DE-627)748756485 (DE-576)167740814 aut, Enthalten in Journal of general virology Reading : Soc., 1967 94(2013), 11, Seite 2549-2556 Online-Ressource (DE-627)316018058 (DE-600)2007065-2 (DE-576)090954734 1465-2099 nnns, volume:94 year:2013 number:11 pages:2549-2556 extent:8, http://dx.doi.org/10.1099/vir.0.055251-0 Verlag Resolving-System kostenfrei Volltext, http://jgv.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.055251-0 Verlag kostenfrei Volltext, http://dx.doi.org/10.1099/vir.0.055251-0 LFER, LFER 2017-07-10T00:00:00Z |
| spellingShingle | Romani, Giulia, Hillmer, Stefan, A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion, Most chloroviruses encode small K+ channels, which are functional in electrophysiological assays. The experimental finding that initial steps in viral infection exhibit the same sensitivity to channel inhibitors as the viral K+ channels has led to the hypothesis that the channels are structural proteins located in the internal membrane of the virus particles. This hypothesis was questioned recently because proteomic studies failed to detect the channel protein in virions of the prototype chlorovirus Paramecium bursaria chlorella virus 1 (PBCV-1). Here, we used a mAb raised against the functional K+ channel from chlorovirus MA-1D to search for the viral K+ channel in the virus particle. The results showed that the antibody was specific and bound to the tetrameric channel on the extracellular side. The antibody reacted in a virus-specific manner with protein extracts from chloroviruses that encoded channels similar to that from MA-1D. There was no cross-reactivity with chloroviruses that encoded more diverse channels or with a chlorovirus that lacked a K+ channel gene. Together with electron microscopic imaging, which revealed labelling of individual virus particles with the channel antibody, these results establish that the viral particles contain an active K+ channel, presumably located in the lipid membrane that surrounds the DNA in the mature virions. |
| swb_id_str | 490554636 |
| title | A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion |
| title_auth | A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion |
| title_full | A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion Giulia Romani, Adrianna Piotrowski, Stefan Hillmer, James Gurnon, James L. van Etten, Anna Moroni, Gerhard Thiel and Brigitte Hertel |
| title_fullStr | A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion Giulia Romani, Adrianna Piotrowski, Stefan Hillmer, James Gurnon, James L. van Etten, Anna Moroni, Gerhard Thiel and Brigitte Hertel |
| title_full_unstemmed | A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion Giulia Romani, Adrianna Piotrowski, Stefan Hillmer, James Gurnon, James L. van Etten, Anna Moroni, Gerhard Thiel and Brigitte Hertel |
| title_in_hierarchy | A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion / Giulia Romani, Adrianna Piotrowski, Stefan Hillmer, James Gurnon, James L. van Etten, Anna Moroni, Gerhard Thiel and Brigitte Hertel, |
| title_short | A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion |
| title_sort | virus encoded potassium ion channel is a structural protein in the chlorovirus paramecium bursaria chlorella virus 1 virion |
| url | http://dx.doi.org/10.1099/vir.0.055251-0, http://jgv.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.055251-0 |