The Tomato yellow leaf curl virus V2 protein forms aggregates depending on the cytoskeleton integrity and binds viral genomic DNA

Adi Moshe, Eduard Belausov, Annette Niehl, Manfred Heinlein, Henryk Czosnek, Rena Gorovits*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

The spread of Tomato yellow leaf curl virus (TYLCV) was accompanied by the formation of coat protein (CP) aggregates of increasing size in the cytoplasm and nucleus of infected tomato (Solanum lycopersicum) cells. In order to better understand the TYLCV-host interaction, we investigated the properties and the subcellular accumulation pattern of the non-structural viral protein V2. CP and V2 are the only sense-oriented genes on the virus circular single-stranded DNA genome. Similar to CP, V2 localized to cytoplasmic aggregates of increasing size and as infection progressed was also found in nuclei, where it co-localized with CP. V2 was associated with viral genomic DNA molecules, suggesting that V2 functions as a DNA shuttling protein. The formation and the 26S proteasome-mediated degradation of V2 aggregates were dependent on the integrity of the actin and microtubule cytoskeleton. We propose that the cytoskeleton-dependent formation and growth of V2 aggregates play an important role during TYLCV infection, and that microtubules and actin filaments are important for the delivery of V2 to the 26S proteasome.

Original languageEnglish
Article number9967
JournalScientific Reports
Volume5
DOIs
StatePublished - 5 May 2015

Bibliographical note

Funding Information:
The V2:GFP construct was a gift from Prof. Y. Gafni, Volcani Center, Bet Dagan, Israel. This research was supported by a grant from the Israel Science foundation ISF to R.G. and H.C. (1037/13) and by a grant from the U.S. Agency for International Development, Middle East Research and Cooperation (MERC program) to H.C. (GEG-G-00-02-00003-00, Project M21-037). A.M. was rewarded with a Short-Term Scientific Mission grant from COST FA0806.

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