In planta protein interactions of three alphacryptoviruses and three betacryptoviruses from white clover, red clover and dill by bimolecular fluorescence complementation analysis
- verfasst von
- Till Lesker, Edgar Maiss
- Abstract
Plant-infecting viruses of the genera Alpha- and Betacryptovirus within the family Partitiviridae cause no visible effects on their hosts and are only transmitted by cell division and through gametes. The bipartite dsRNA genome is encoding a RNA-dependent RNA polymerase (RdRp) and a coat protein (CP). Aside from sequence and structural analysis, the investigation of protein interactions is another step towards virus characterization. Therefore, ORFs of two type members White Clover Cryptic Virus 1 and 2 (WCCV-1 and WCCV-2), as well as the related viruses from Red Clover and Dill were introduced into a bimolecular fluorescence complementation assay. We showed CP-CP dimerization for all tested viruses with localization for alphacryptoviruses at the nuclear membrane and for betacryptoviruses close to cell walls within the cytoplasm. For CPs of WCCV-1 and WCCV-2, deletion mutants were created to determine internal interaction sites. Moreover, RdRp self-interaction was found for all viruses, whereas CP-RdRp interactions were only detectable for the alphacryptoviruses. An intra-genus test of CPs was successful in various virus combinations, whereas an inter-genus interaction of WCCV-1CP and WCCV-2CP was absent. This is the first report of in vivo protein interactions of members in the family Partitiviridae, indicating distinct features of the alpha- and betacryptoviruses.
- Organisationseinheit(en)
-
Abteilung Phytomedizin
- Typ
- Artikel
- Journal
- Viruses
- Band
- 5
- Seiten
- 2512-2530
- Anzahl der Seiten
- 19
- ISSN
- 1999-4915
- Publikationsdatum
- 09.10.2013
- Publikationsstatus
- Veröffentlicht
- Peer-reviewed
- Ja
- ASJC Scopus Sachgebiete
- Infektionskrankheiten, Virologie
- Ziele für nachhaltige Entwicklung
- SDG 3 – Gute Gesundheit und Wohlergehen
- Elektronische Version(en)
-
https://doi.org/10.3390/v5102512 (Zugang:
Offen)
https://doi.org/10.15488/56 (Zugang: Offen)