Structural basis for the multitasking nature of the potato virus Y coat protein

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This publication doesn't include Institute of Computer Science. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.

Authors	KEZAR A. KAVCIC L. POLÁK Martin NOVÁČEK Jiří GUTIERREZ-AGUIRRE I. ZNIDARIC M.T. CO A. STARE K. GRUDEN K. RAVNIKAR M. PAHOVNIK D. ZAGAR E. MERZEL F. ANDERLUH G. PODOBNIK M.
Year of publication	2019
Type	Article in Periodical
Magazine / Source	Science advances
MU Faculty or unit	Central European Institute of Technology
Citation
Web	https://advances.sciencemag.org/content/advances/5/7/eaaw3808.full.pdf
Doi	http://dx.doi.org/10.1126/sciadv.aaw3808
Keywords	REAL-TIME PCR; CRYO-EM; PLANT-VIRUSES; POTYVIRUS; TERMINUS; ELECTROSTATICS; REFINEMENT; RESOLUTION; RESIDUES; PVYNTN
Description	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.
Related projects:	Czech Infrastructure for Integrative Structural Biology