Evidence map›Paper›PMID 42049738›Full record

ArticleNature communications2026

Small heat shock and J-domain proteins direct defense against areca palm velarivirus 1 by degrading coat protein via autophagy.

Ruibai Zhao, Jie Lu, Zengyu Xing, Jinling Zhai, Hongxing Wang, Xianmei Cao, Xi Huang

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Ruibai Zhao *National Key Laboratory for Tropical Crop Breeding, School of Breeding and Multiplication, Sanya Institute of Breeding and Multiplication, Hainan University, Sanya, China.
Jie Lu *National Key Laboratory for Tropical Crop Breeding, School of Breeding and Multiplication, Sanya Institute of Breeding and Multiplication, Hainan University, Sanya, China.ORCID http://orcid.org/0009-0004-9320-210X
Zengyu XingNational Key Laboratory for Tropical Crop Breeding, School of Breeding and Multiplication, Sanya Institute of Breeding and Multiplication, Hainan University, Sanya, China.
Jinling ZhaiNational Key Laboratory for Tropical Crop Breeding, School of Breeding and Multiplication, Sanya Institute of Breeding and Multiplication, Hainan University, Sanya, China.
Hongxing WangNational Key Laboratory for Tropical Crop Breeding, School of Breeding and Multiplication, Sanya Institute of Breeding and Multiplication, Hainan University, Sanya, China.
Xianmei CaoNational Key Laboratory for Tropical Crop Breeding, School of Breeding and Multiplication, Sanya Institute of Breeding and Multiplication, Hainan University, Sanya, China. 184419@hainanu.edu.cn.ORCID http://orcid.org/0009-0007-6729-0072
Xi HuangNational Key Laboratory for Tropical Crop Breeding, School of Breeding and Multiplication, Sanya Institute of Breeding and Multiplication, Hainan University, Sanya, China. xihuang@hainanu.edu.cn.ORCID http://orcid.org/0000-0002-3605-2692

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Both autophagy and heat shock proteins (HSPs) play dual roles in viral infections, yet their coordination in antiviral defense remains unclear. Here, we show that a cytosolic small heat shock protein (AcsHSP) and a type II J-domain protein (AcDNAJB13) from areca palm interact with the coat protein (CP) of areca palm velarivirus 1 (APV1) independently of HSP70 chaperones. Their closest Nicotiana benthamiana homologs also bind CP. Both APV1 infection and CP expression induces the transcription of sHSP and DNAJB13, which in turn inhibits CP accumulation. Silencing of these genes enhances APV1 infection and CP accumulation, while overexpression of AcsHSP reduces viral accumulation. Mechanistically, CP is degraded via autophagy. Both AcsHSP and AcDNAJB13 interact with the autophagosome marker ATG8f1. However, AcsHSP strengthens CP-ATG8f1 binding, whereas AcDNAJB13 weakens it. These findings reveal distinct yet complementary mechanisms by which sHSP and DNAJB13 coordinate with autophagy to restrict viral infection.

Indexed as

AutophagyCapsid ProteinsHeat-Shock Proteins, SmallPlant ProteinsAutophagy-Related Protein 8 FamilyHSP40 Heat-Shock ProteinsNicotianaPicornaviralesPlant DiseasesProtein BindingProteolysisAutophagy-Related Protein 8 FamilyCapsid ProteinsHeat-Shock Proteins, SmallHSP40 Heat-Shock ProteinsPlant Proteins

Identifiers

PMID42049738
PMCPMC13328657

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Registered trials

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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.