Andreja Kežar (Author), Luka Kavčič (Author), Martin Pólak (Author), Jiři Nováček (Author), Ion Gutierrez-Aguirre (Author), Magda Tušek-Žnidarič (Author), Anna Coll Rius (Author), Katja Stare (Author), Kristina Gruden (Author), Maja Ravnikar (Author), David Pahovnik (Author), Ema Žagar (Author), Franci Merzel (Author), Gregor Anderluh (Author), Marjetka Podobnik (Author)

Abstract

Potato virus Y (PVY) is among the most economically important plant pathogens. Using cryoelectron microscopy, we determined the near-atomic structure of PVY’s flexuous virions, revealing a previously unknown lumenal interplay between extended carboxyl-terminal regions of the coat protein units and viral RNA. RNA–coat protein interactions are crucial for the helical configuration and stability of the virion, as revealed by the unique near-atomic structure of RNA-free virus-like particles. The structures offer the first evidence for plasticity of the coat protein’s amino- and carboxyl-terminal regions. Together with mutational analysis and in planta experiments, we show their crucial role in PVY infectivity and explain the ability of the coat protein to perform multiple biological tasks. Moreover, the high modularity of PVY virus-like particles suggests their potential as a new molecular scaffold for nanobiotechnological applications.

Keywords

plant pathogens;potato virus Y;viral RNA;

Data

Language: English
Year of publishing:
Typology: 1.01 - Original Scientific Article
Organization: KI - National Institute of Chemistry
UDC: 577.2
COBISS: 5135183 Link will open in a new window
ISSN: 2375-2548
Views: 32
Downloads: 8
Average score: 0 (0 votes)
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Other data

Source comment: Nasl. z nasl. zaslona; Opis vira z dne 30. 7. 2019;
Pages: str. 1-13
Volume: ǂVol. ǂ5
Issue: ǂno. ǂ7
Chronology: 2019
DOI: 10.1126/sciadv.aaw3808
ID: 24579929