Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI- and COPII-dependent manner

Single-stranded positive-sense RNA viruses induce the biogenesis of cytoplasmic membranous vesicles, where viral replication takes place. However, the mechanism underlying this characteristic vesicular proliferation remains poorly understood. Previously, a 6-kDa potyvirus membrane protein (6K) was s...

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Veröffentlicht in:Journal of virology Jg. 82; H. 24; S. 12252
Hauptverfasser: Wei, Taiyun, Wang, Aiming
Format: Journal Article
Sprache:Englisch
Veröffentlicht: United States 15.12.2008
Schlagworte:
ADP-Ribosylation Factor 1 - genetics
ADP-Ribosylation Factor 1 - metabolism
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis - virology
Biomarkers
Coat Protein Complex I - metabolism
COP-Coated Vesicles - metabolism
Cytoplasmic Vesicles - metabolism
Endoplasmic Reticulum - metabolism
Intracellular Membranes - metabolism
Nicotiana - genetics
Nicotiana - metabolism
Nicotiana - virology
Organelle Biogenesis
Plant Leaves - genetics
Plant Leaves - metabolism
Potyvirus - physiology
Protein Transport
R-SNARE Proteins - genetics
R-SNARE Proteins - metabolism
Solubility
Viral Fusion Proteins - genetics
Viral Fusion Proteins - metabolism
Virus Replication
ISSN:1098-5514, 1098-5514
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Zusammenfassung:Single-stranded positive-sense RNA viruses induce the biogenesis of cytoplasmic membranous vesicles, where viral replication takes place. However, the mechanism underlying this characteristic vesicular proliferation remains poorly understood. Previously, a 6-kDa potyvirus membrane protein (6K) was shown to interact with the endoplasmic reticulum (ER) and to induce the formation of the membranous vesicles. In this study, the involvement of the early secretory pathway in the formation of the 6K-induced vesicles was investigated in planta. By means of live-cell imaging, it was found that the 6K protein was predominantly colocalized with Sar1, Sec23, and Sec24, which are known markers of ER exit sites (ERES). The localization of 6K at ERES was prevented by the coexpression of a dominant-negative mutant of Sar1 that disables the COPII activity or by the coexpression of a mutant of Arf1 that disrupts the COPI complex. The secretion of a soluble secretory marker targeting the apoplast was arrested at the level of the ER in cells overexpressing 6K or infected by a potyvirus. This blockage of protein trafficking out of the ER by 6K and the distribution of 6K toward the ERES may account for the aggregation of the 6K-bound vesicles. Finally, virus infection was reduced when the accumulation of 6K at ERES was inhibited by impairing either the COPI or COPII complex. Taken together, these results imply that the cellular COPI and COPII coating machineries are involved in the biogenesis of the potyvirus 6K vesicles at the ERES for viral-genome replication.
Bibliographie:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:1098-5514
1098-5514
DOI:10.1128/JVI.01329-08