6hxz
Virus-like Particles based on Potato Virus Y
Structural highlights
Function[A0A0C4URS3_9POTV] Helper component proteinase: required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.[SAAS:SAAS00890155] Publication Abstract from PubMedPotato 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. Structural basis for the multitasking nature of the potato virus Y coat protein.,Kezar A, Kavcic L, Polak M, Novacek J, Gutierrez-Aguirre I, Znidaric MT, Coll A, Stare K, Gruden K, Ravnikar M, Pahovnik D, Zagar E, Merzel F, Anderluh G, Podobnik M Sci Adv. 2019 Jul 17;5(7):eaaw3808. doi: 10.1126/sciadv.aaw3808. eCollection 2019, Jul. PMID:31328164[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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