ArticlePLoS pathogens2020
The potyviral silencing suppressor HCPro recruits and employs host ARGONAUTE1 in pro-viral functions.
Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- Systematic Screening of Host Interactors forPlants (Basel, Switzerland) · 2026Article
- Tomato Chlorotic Virus Minor Coat Protein Interferes With the Host Proteasome Function by Competitive Disruption of SlPAD1-SlPA4 Interaction to Enhance Viral Infection.Molecular plant pathology · 2025Article
- Co-Infection ofIranian journal of biotechnology · 2025Article
- Viral coat proteins decrease the gene silencing activity of cognate and heterologous viral suppressors.Scientific reports · 2024Article
- Development of a TaqMan qPCR for the Simultaneous Detection of the TuMV and BBWV2 Viruses Responsible for the Viral Disease inMicroorganisms · 2024Article
- Story of an infection: Viral dynamics and host responses in theScience advances · 2024Article
- Potyviral Helper-Component Protease: Multifaced Functions and Interactions with Host Proteins.Plants (Basel, Switzerland) · 2024Review
- Rubisco small subunit (RbCS) is co-opted by potyvirids as the scaffold protein in assembling a complex for viral intercellular movement.PLoS pathogens · 2024Article
- Cell Fractionation and the Identification of Host Proteins Involved in Plant-Virus Interactions.Pathogens (Basel, Switzerland) · 2024Review
- Mutations in the WG and GW motifs of the three RNA silencing suppressors of grapevine fanleaf virus alter their systemic suppression ability and affect virus infectivity.Frontiers in microbiology · 2024Article
- Induction and suppression of gene silencing in plants by nonviral microbes.Molecular plant pathology · 2023Review
- Role of Plant Virus Movement Proteins in Suppression of Host RNAi Defense.International journal of molecular sciences · 2023Review
- A Zinc Finger Motif in the P1 N Terminus, Highly Conserved in a Subset of Potyviruses, Is Associated with the Host Range and Fitness of Telosma Mosaic Virus.Journal of virology · 2023Article
- Development of an assay system for the analysis of host RISC activity in the presence of a potyvirus RNA silencing suppressor, HC-Pro.Virology journal · 2023Article
- Proteome expansion in the Potyviridae evolutionary radiation.FEMS microbiology reviews · 2022Review
- Article
- Interplay of HCPro and CP in the Regulation of Potato Virus A RNA Expression and Encapsidation.Viruses · 2022Article
- Construction of full-length infectious clones of turnip mosaic virus isolates infecting Perilla frutescens and genetic analysis of recently emerged strains in Korea.Archives of virology · 2022Article
- Insight into aphid mediatedFrontiers in microbiology · 2022Review
- An Importin-β-like Protein fromViruses · 2021Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we demonstrate a novel pro-viral role for the Nicotiana benthamiana ARGONAUTE 1 (AGO1) in potyvirus infection. AGO1 strongly enhanced potato virus A (PVA) particle production and benefited the infection when supplied in excess. We subsequently identified the potyviral silencing suppressor, helper-component protease (HCPro), as the recruiter of host AGO1. After the identification of a conserved AGO1-binding GW/WG motif in potyviral HCPros, we used site-directed mutagenesis to introduce a tryptophan-to-alanine change into the HCPro (HCProAG) of PVA (PVAAG) and turnip mosaic virus (TuMVAG). AGO1 co-localization and co-immunoprecipitation with PVA HCPro was significantly reduced by the mutation suggesting the interaction was compromised. Although the mutation did not interfere with HCPro's complementation or silencing suppression capacity, it nevertheless impaired virus particle accumulation and the systemic spread of both PVA and TuMV. Furthermore, we found that the HCPro-AGO1 interaction was important for AGO1's association with the PVA coat protein. The coat protein was also more stable in wild type PVA infection than in PVAAG infection. Based on these findings we suggest that potyviral HCPro recruits host AGO1 through its WG motif and engages AGO1 in the production of stable virus particles, which are required for an efficient systemic infection.
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