Evidence map›Paper›PMID 41889145›Full record

ArticleMolecular plant pathology2026

Tobacco Rattle Virus Coat Protein Targets Ferredoxin 1 for Degradation.

Shaorui Tian, Changyun Liu, Jie Dong, Xin Zhu, Xingyi Luo, Weina Liu, Haoran Peng, Lin Cai, Xianchao Sun

Abstract read
In one paragraph

Article in Molecular plant pathology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Shaorui TianChongqing Key Laboratory of Plant Disease Biology, College of Plant Protection, Southwest University, Chongqing, China.
Changyun LiuChongqing Key Laboratory of Plant Disease Biology, College of Plant Protection, Southwest University, Chongqing, China.
Jie DongChongqing Key Laboratory of Plant Disease Biology, College of Plant Protection, Southwest University, Chongqing, China.
Xin ZhuChongqing Key Laboratory of Plant Disease Biology, College of Plant Protection, Southwest University, Chongqing, China.
Xingyi LuoChongqing Key Laboratory of Plant Disease Biology, College of Plant Protection, Southwest University, Chongqing, China.
Weina LiuChongqing Key Laboratory of Plant Disease Biology, College of Plant Protection, Southwest University, Chongqing, China.
Haoran PengChongqing Key Laboratory of Plant Disease Biology, College of Plant Protection, Southwest University, Chongqing, China.
Lin CaiGuizhou Key Laboratory for Tobacco Quality, College of Tobacco Science of Guizhou University, Guiyang, China.ORCID 0009-0008-4491-5380
Xianchao SunChongqing Key Laboratory of Plant Disease Biology, College of Plant Protection, Southwest University, Chongqing, China.ORCID 0000-0003-0062-4916

Funding

Chongqing Municipal Training Program of Innovation and Entrepreneurship for Undergraduates S202410635056Innovation Fund for Graduate Students of Chongqing CYB240123National Natural Science Foundation of China 31870147National Natural Science Foundation of China 32570175Science and Technology Projects of Chongqing Company of China Tobacco Corporation B20241NY1303Science and Technology Projects of Chongqing Company of China Tobacco Corporation B20241NY1310
6 · The paper itself

Abstract

Plant virus infections commonly inhibit leaf photosynthesis, leading to characteristic symptoms such as chlorosis. However, whether a conserved mechanism underpins this phenomenon remains unclear. Here, we demonstrate that the coat protein (CP) of tobacco rattle virus (TRV) interacts with Nicotiana benthamiana ferredoxin (NbFd1) in chloroplasts, recruiting the 26S proteasome to promote NbFd1 degradation. This degradation reduces the net photosynthetic rate facilitated by NbFd1, ultimately causing leaf chlorosis. Notably, this interaction is not unique to TRV CP, as other viral proteins also recognise Fd1, suggesting a conserved mechanism among plant viruses. Evolutionary analyses indicate that Fd1 originated from prokaryotic photosynthetic bacteria and was maintained in plants through endosymbiosis under strong selective pressure. Notably, Fd1 from Selaginella moellendorffii, an early-diverging vascular plant, is also recognised by TRV CP, suggesting an ancient origin of this interaction. In addition, Solanum lycopersicum Fd1 interacts with TRV CP, and its overexpression suppresses TRV-GFP infection, supporting a defensive role. Together, these findings show that TRV CP targets Fd1 to impair host photosynthesis and promote symptom development, whereas highlighting the evolutionary significance of this interaction.

Indexed as

Capsid ProteinsFerredoxinsNicotianaPlant ProteinsPlant VirusesChloroplastsPhotosynthesisProteasome Endopeptidase ComplexProteolysisCapsid ProteinsFerredoxinsPlant ProteinsProteasome Endopeptidase Complexcoat proteinsconservationferredoxin 1interactiontobacco rattle virus

Identifiers

PMID41889145
PMCPMC13097427

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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 Socratic graph.