Evidence map›Paper›PMID 41144906›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026

Insect I-Type Lysozymes Function as Antiviral Proteases by Forming Biomolecular Condensates.

Yu Du, Yuqing Xiao, Manman Hu, Jinhua Yang, You Li, Taiyun Wei

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Insect I-Type Lysozymes Function as Antiviral Proteases by Forming Biomolecular Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    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

6 authors.

Yu DuState Key Laboratory of Agricultural and Forestry Biosecurity, Fujian Agriculture and Forestry University, Fuzhou, Fujian, 350002, China.
Yuqing XiaoState Key Laboratory of Agricultural and Forestry Biosecurity, Fujian Agriculture and Forestry University, Fuzhou, Fujian, 350002, China.
Manman HuState Key Laboratory of Agricultural and Forestry Biosecurity, Fujian Agriculture and Forestry University, Fuzhou, Fujian, 350002, China.
Jinhua YangState Key Laboratory of Agricultural and Forestry Biosecurity, Fujian Agriculture and Forestry University, Fuzhou, Fujian, 350002, China.
You LiState Key Laboratory of Agricultural and Forestry Biosecurity, Fujian Agriculture and Forestry University, Fuzhou, Fujian, 350002, China.
Taiyun WeiState Key Laboratory of Agricultural and Forestry Biosecurity, Fujian Agriculture and Forestry University, Fuzhou, Fujian, 350002, China.ORCID https://orcid.org/0000-0002-0732-9752

Funding

National Key Research and Development Program of China 2023YFD1400300National Natural Science Foundation of China U23A20197
6 · The paper itself

Abstract

Lysozymes are well-known for their ability to cleave bacterial peptidoglycan, but their potential to hydrolyze viral components as a form of antiviral defense remains poorly understood. This study demonstrates that insect i-type lysozymes (Lyz-I1), regulated by the Toll signaling pathway, function as proteases that directly cleave viral proteins. Structural and functional analyses reveal that the catalytic dyad Glu34/Asp50 in leafhopper Lyz-I1, while retaining its essential role in bacterial peptidoglycan hydrolysis, also mediates specific binding to Lys180 on the viroplasm protein Pns9 of rice gall dwarf virus (RGDV). This interaction catalyzes the cleavage of the adjacent peptide bond of Lys180, leading to Pns9 degradation, which disrupts viroplasm assembly and inhibits viral replication. Notably, this proteolytic antiviral mechanism of Lyz-I1 shows evolutionary conservation across major rice reoviruses and their respective leafhopper or planthopper vectors. Additionally, leafhopper Lyz-I1 undergoes liquid-liquid phase separation, forming biomolecular condensates that concentrate Pns9 and enhance proteolytic efficiency. Critically, exogenous application of Lyz-I1 not only effectively reduces viral titer and disease symptoms in RGDV-infected rice plants but also induces plant immune defense. Consequently, this work provides the evidence that lysozymes can function as specific antiviral proteases, establishing a foundation for innovative control strategies against viral diseases.

Indexed as

Antiviral AgentsHemipteraInsect ProteinsMuramidasePeptide HydrolasesAnimalsOryzaPlant DiseasesReoviridaeViral ProteinsAntiviral AgentsInsect ProteinsMuramidasePeptide HydrolasesViral Proteinsantiviral proteaseliquid–liquid phase separationlysozymerice virusesToll signaling pathway

Identifiers

PMID41144906
PMCPMC12766996

What OpenQuestion holds

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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.