Dataset Information

Serine protease HtrA promotes Campylobacter jejuni intestinal colonization through degrading antimicrobial peptide LL-37

ABSTRACT: We carried out a DNA pull-down assay using the PhtrA promoter as a bait to capture potential direct transcriptional regulators from cellular lysates of P116B strain

ORGANISM(S): Campylobacter Jejuni

SUBMITTER: Jinlin Huang

PROVIDER: PXD073907 | iProX | Sat Jan 31 00:00:00 GMT 2026

REPOSITORIES: iProX

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Serine protease HtrA promotes Campylobacter jejuni intestinal colonization through degrading antimicrobial peptide LL-37.

Li Xiaofei X Zhang Mengjie M Xu Zhenzhen Z Li Yunlu Y Bian Su S Tang Yuanyue Y Jiao Xinan X Gundogdu Ozan O Huang Jinlin J

Science advances 20260520 21

Campylobacter jejuni (C. jejuni) is a leading cause of human gastroenteritis worldwide and must overcome intestinal innate immunity, including antimicrobial peptide LL-37. However, how C. jejuni responds to LL-37 remains unclear. Here, we showed that C. jejuni infection stimulates intestinal epithelial cells to secrete LL-37, exhibiting effective antibacterial activity against 86.3% of C. jejuni clinical isolates by disrupting essential processes required for b ...[more]

PMID: 42160414

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Project description:Foodborne pathogenic bacterial infections pose significant challenges to global food safety and public health, while the issue of antimicrobial resistance (AMR) has worsened in recent years, creating an urgent need for safe, natural alternatives to combat foodborne pathogens and associated intestinal diseases. This study focuses on the Antimicrobial and Protease-resistant Peptide R7I, composed of natural amino acids, elucidating its mechanisms of action as a functional food ingredient in modulating intestinal health, thereby offering novel strategies for antibiotic alternatives. The results showed a 13.52% increase in average daily weight gain in the R7I group compared to the control group. Average daily feed intake was significantly lower (P < 0.05) in the control group than in both the normal and R7I groups. Additionally, serum and jejunal lipopolysaccharide (LPS) content, as well as serum D-lactic acid levels (P < 0.05), were reduced in the R7I group, indicating markedly alleviated intestinal permeability. Compared to the control group, the R7I group significantly reduced serum levels of lactate dehydrogenase and total bile acids, while increasing high-density lipoprotein levels (P < 0.05). R7I treatment significantly elevated (P < 0.05) serum levels of anti-inflammatory cytokines interleukin-4 (IL-4) and interleukin-4 (IL-10), while suppressing production of the pro-inflammatory cytokines tumor necrosis factor-alpha (TNF-α) and interleukin-17 (IL-17). Furthermore, multi-omics analyses revealed that R7I alleviated Enterotoxigenic Escherichia coli (ETEC)-induced intestinal damage through synergistic mechanisms involving modulation of gene expression regulatory pathways, restructuring of gut microbiota composition, and improvement of metabolite profiles. These findings substantiate the potential of R7I as a promising antibiotic-alternative functional food ingredient, offering new strategies for preventing foodborne diseases and managing intestinal health.

Dataset Information

Serine protease HtrA promotes Campylobacter jejuni intestinal colonization through degrading antimicrobial peptide LL-37

Publications

Serine protease HtrA promotes <i>Campylobacter jejuni</i> intestinal colonization through degrading antimicrobial peptide LL-37.

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Dataset Information

Serine protease HtrA promotes Campylobacter jejuni intestinal colonization through degrading antimicrobial peptide LL-37

Publications

Serine protease HtrA promotes &lt;i&gt;Campylobacter jejuni&lt;/i&gt; intestinal colonization through degrading antimicrobial peptide LL-37.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Serine protease HtrA promotes <i>Campylobacter jejuni</i> intestinal colonization through degrading antimicrobial peptide LL-37.