The Tomato yellow leaf curl virus V2 protein forms aggregates depending on the cytoskeleton integrity and binds viral genomic DNA.
Fiche publication
Date publication
mai 2015
Journal
Scientific reports
Auteurs
Membres identifiés du Cancéropôle Est :
Dr HEINLEIN Manfred
Tous les auteurs :
Moshe A, Belausov E, Niehl A, Heinlein M, Czosnek H, Gorovits R
Lien Pubmed
Résumé
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.
Mots clés
Begomovirus, pathogenicity, Capsid Proteins, genetics, Cytoskeleton, metabolism, DNA, Viral, genetics, Dimerization, Genes, Viral, genetics, Genome, Viral, genetics, Lycopersicon esculentum, metabolism, Multiprotein Complexes, Proteasome Endopeptidase Complex, metabolism, Protein Binding
Référence
Sci Rep. 2015 May 5;5:9967