ArticleVirus genes2019
Triticum aestivum heat shock protein 23.6 interacts with the coat protein of wheat yellow mosaic virus.
Article in Virus genes, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Small heat shock and J-domain proteins direct defense against areca palm velarivirus 1 by degrading coat protein via autophagy.Nature communications · 2026Article
- Competition for Chaperones: A Trade-Off Between Thermotolerance and Antiviral Immunity in Plants.Current issues in molecular biology · 2025Review
- Heat Stress and Plant-Biotic Interactions: Advances and Perspectives.Plants (Basel, Switzerland) · 2024Review
- A papain-like cysteine protease-released small signal peptide confers wheat resistance to wheat yellow mosaic virus.Nature communications · 2023Article
- Review
- Transcriptome profiling of pepper leaves by RNA-Seq during an incompatible and a compatible pepper-tobamovirus interaction.Scientific reports · 2021Article
- Bymovirus-induced yellow mosaic diseases in barley and wheat: viruses, genetic resistances and functional aspects.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2020Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The role of heat shock proteins (HSPs) in viral replication has been described in numerous publications. Wheat yellow mosaic virus (WYMV) belongs to the genus Bymovirus (family Potyviridae), which causes yellow mosaic and dwarf symptoms in wheat (Triticum aestivum). In this study, the T. aestivum heat shock protein 23.6 (TaHSP23.6), which belongs to the small heat shock protein family, was shown to interact with the WYMV coat protein (CP) in a yeast two-hybrid screen. The co-localization and interaction between TaHSP23.6 and WYMV CP were additionally verified in Nicotiana benthamiana by co-localization assays and bimolecular fluorescence complementation (BiFC). Not only the transcription of TaHSP23.6 but also that of other HSP family members (TaHSP70, TaHSP90, and TaHSP101) was up-regulated in WYMV-infected leaves, as shown by semi-quantitative PCR assays. Interestingly, the expression levels of the T. aestivum heat stress transcription factor A2 (TaHSFA2) members were varied in response to WYMV infection. Thus, our results provide insights into the interaction between TaHSP23.6 and WYMV infection.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.