Evidence mapPaperPMID 41578407Full record

ArticleVeterinary research2026

Cathelicidin CATH-2 suppresses the NF-κB/ROS/NLRP3 signaling pathway via regulating mTOR-dependent autophagy during Streptococcus suis infection.

Liuyi Xu, Yilin Lu, Shichao Xu, Yuqian Liu, Hongdou Liu, Tingting Zhang, Yandi Pan, Yi Lu, Zhouyuan Wang, Xuefeng Cao and 3 more

Abstract read
In one paragraph

Article in Veterinary research, 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. Review
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

13 authors.

Liuyi XuJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China.
Yilin LuJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China.
Shichao XuJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China.
Yuqian LiuJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China.
Hongdou LiuJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China.
Tingting ZhangJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China.
Yandi PanJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China.
Yi LuJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China.
Zhouyuan WangKunming Hemeihua Feed Limited Company, Kunming, China.
Xuefeng CaoJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China.
Zhiwei LiJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China.
Rendong FangJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China.
Lianci PengJoint International Research Laboratory of Animal Health and Animal Food Safety, College of Veterinary Medicine, No.2 Tiansheng Road, Beibei District, Chongqing, 400715, China. penglianci@swu.edu.cn.

Funding

Chongqing Modern Agricultural Industry Technology System CQMAITS202312Chongqing Science and Technology Commission CSTB2024TIAD-LDX0009Fundamental Research Funds for the Central Universities SWU-KT25016Graduate Research Innovation Project of Southwest University SWUS2315National Center of Technology Innovation for pigs NCTIP-XD/C17National Natural Science Foundation of China 32473027National Natural Science Foundation of China 32473043
6 · The paper itself

Abstract

Cathelicidin CATH-2 has been reported to exert potent anti-inflammatory activity in different species though neutralizing stimuli such as lipopolysaccharide (LPS) and lipoteichoic acid (LTA). CATH-2 has been shown to inhibit Streptococcus suis (S. suis)-induced activation of dendritic cells and macrophages by binding to LTA. However, the exact mechanism of this prophylactically anti-inflammatory activity remains unclear. Therefore, we investigated the anti-inflammatory activity and mechanism of CATH-2 in mice peritoneal macrophages pretreated with CATH-2 followed by S. suis infection. The results showed that CATH-2 pretreatment significantly reduced S. suis-induced transcription and secretion of interleukin (IL)-1β, IL-6, and IL-12. CATH-2 also downregulated NOD-, LRR-, and pyrin domain-containing protein 3 (NLRP3) expression and apoptosis-associated speck-like protein containing a CARD (ASC) oligomerization, and inhibited the maturation of IL-1β, suggesting that CATH-2 inhibits NLRP3 activation. In addition, CATH-2 significantly inhibited S. suis-induced phosphorylation of p65 and extracellular signal-regulated kinase (ERK). Further study showed that CATH-2 inhibited S. suis-induced reactive oxygen species (ROS) by upregulating the expression of ROS scavenging genes including catalase (CAT) and superoxide dismutase 1 (SOD1). Mechanistically, transcriptome analysis revealed that CATH-2 regulated the protein kinase B (ATK)/mammalian target of rapamycin (mTOR) pathway, which was evident by the downregulation of phosphorylated (p)-ATK and p-mTOR induced by CATH-2. Notably, CATH-2 induced autophagy and autophagic flux. Inhibition of mTOR using rapamycin enhanced the CATH-2-induced autophagic efficacy, demonstrating that CATH-2 induces mTOR-dependent autophagy. However, inhibition of autophagy using 3-methyladenine (3-MA) reversed the reduction in the expression of p-p65, p-ERK, and IL-1β induced by CATH-2. Our study reveals that CATH-2 inhibits the nuclear factor kappa-B (NF-κB)/NLRP3-mediated inflammatory response through the induction of mTOR-dependent autophagy during S. suis infection, which provides new insight into the anti-inflammatory pathways of antimicrobial peptides.

Indexed as

Antimicrobial Cationic PeptidesAutophagySignal TransductionStreptococcal InfectionsStreptococcus suisAnimalsCathelicidinsMacrophages, PeritonealMiceNF-kappa BNLR Family, Pyrin Domain-Containing 3 ProteinReactive Oxygen SpeciesTOR Serine-Threonine KinasesAntimicrobial Cationic PeptidesCathelicidinsmTOR protein, mouseNF-kappa BNLR Family, Pyrin Domain-Containing 3 ProteinNlrp3 protein, mouseReactive Oxygen SpeciesTOR Serine-Threonine Kinasesanti-inflammatory responseautophagyCathelicidin-2Streptococcus suis

Identifiers

PMID41578407
PMCPMC12911090

What Socratic holds

Textmetadata
LicenceCC BY
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.