1. Structural basis for the multitasking nature of the potato virus Y coat protein
- Author
-
Kristina Gruden, Andreja Kežar, Luka Kavčič, Magda Tušek Žnidarič, Katja Stare, Ion Gutiérrez-Aguirre, Marjetka Podobnik, Franci Merzel, Martin Polak, Maja Ravnikar, Jiří Nováček, Gregor Anderluh, David Pahovnik, Ema Žagar, and Anna Coll
- Subjects
Models, Molecular ,Protein Conformation ,viruses ,Potyvirus ,Plasma protein binding ,Protein–protein interaction ,03 medical and health sciences ,Structure-Activity Relationship ,Protein structure ,Capsid ,Virus-like particle ,Structural Biology ,Amino Acid Sequence ,Binding site ,Peptide sequence ,Research Articles ,030304 developmental biology ,Plant Diseases ,0303 health sciences ,Multidisciplinary ,Binding Sites ,biology ,Chemistry ,030302 biochemistry & molecular biology ,fungi ,Virion ,RNA ,food and beverages ,SciAdv r-articles ,biology.organism_classification ,3. Good health ,Cell biology ,Potato virus Y ,RNA, Viral ,Capsid Proteins ,Research Article ,Protein Binding - Abstract
Structural and functional studies of the coat protein regions of potato virus Y reveal crucial roles in viral infectivity., 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.
- Published
- 2019