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8C6V

The RNA silencing suppressor P8 from High-Plains Wheat Mosaic Virus

Summary for 8C6V
Entry DOI10.2210/pdb8c6v/pdb
DescriptorP8 RNA silencing suppressor, GLYCEROL, BETA-MERCAPTOETHANOL, ... (6 entities in total)
Functional Keywordshigh plains wheat mosaic virus, rna silencing, plant virus, virus, viral protein
Biological sourceEmaravirus tritici
Total number of polymer chains4
Total formula weight84913.35
Authors
Hamo, S.,Dessau, M. (deposition date: 2023-01-12, release date: 2024-07-24, Last modification date: 2024-12-11)
Primary citationHamo, S.,Izhaki-Tavor, L.S.,Tatineni, S.,Dessau, M.
The RNA Silencing Suppressor P8 From High Plains Wheat Mosaic Virus is a Functional Tetramer.
J.Mol.Biol., 436:168870-168870, 2024
Cited by
PubMed Abstract: In plants, RNA interference (RNAi) serves as a critical defense mechanism against viral infections by regulating gene expression. However, viruses have developed RNA silencing suppressor (RSS) proteins to evade this defense mechanism. The High Plains wheat mosaic virus (HPWMoV) is responsible for the High Plains disease in wheat and produces P7 and P8 proteins, which act as RNA silencing suppressors. P8, in particular, lacks sequence similarity to known suppressors, prompting inquiries into its structure and function. Here, we present a comprehensive analysis of P8, elucidating its structure and function. Using X-ray crystallography, we resolved the full-length P8 structure at 1.9 Å resolution, revealing a tetrameric arrangement formed by two identical dimers. Through structure-based mutagenesis, biochemical assays, and functional studies in plants, we demonstrate that HPWMoV P8's RNA silencing suppression activity relies on its oligomeric state. Contrary to previous report, our findings indicate that while a P8 fused to maltose-binding protein (MBP-P8) was hypothesized to bind short double-stranded RNA, the native P8 tetramer does not interact with small interfering RNA (siRNA). This suggests an alternative mechanism for its function, yet to be determined. Our study sheds light on the structural and functional characteristics of HPWMoV P8, providing valuable insights into the complex interplay between viral suppressors and host defense mechanisms. SIGNIFICANCE STATEMENT: Effective action to address malnutrition in all its forms requires an understanding of the mechanisms affecting it. Wheat, crucial for human and animal consumption, faces threats from biotic and abiotic stresses. RNA silencing is a key defense against viral infections in plants. Plant viruses employ various mechanisms, including encoding viral RNA silencing suppression (VRS) proteins, to evade host immune responses. Despite the conservation of RNA-silencing pathways, viral RSS proteins exhibit diverse sequences, structures, and mechanisms. Our study focuses on P8, an RSS protein from HPWMoV. Understanding its structure and assembly is a crucial step toward comprehending how these viruses counteract host defenses, aiding in combatting malnutrition.
PubMed: 39571786
DOI: 10.1016/j.jmb.2024.168870
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

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