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Sponsored AI Networking Cookbook: Practical recipes for AI-assisted network automation and development AI Networking Cookbook: Practical recipes for AI-assisted network automation and development

Author

Xin-Hua Chen

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Aug 2026

A dual-function interleukin-1 receptor couples bacterial recognition to MyD88-dependent NF-κB activation during antibacterial immunity in shrimp.

The interleukin-1 receptor (IL-1R) is a key member of the Toll/interleukin-1 receptor superfamily that plays essential roles in inflammatory signaling and immune regulation in vertebrates. Unlike vertebrate IL-1Rs, which are primarily specialized for the recognition of endogenous IL-1 family cytokines, the biological functions of IL-1R in crustaceans remain poorly understood. In this study, we systematically investigated the immune function of IL-1R in the Pacific white shrimp (Penaeus vannamei) during Vibrio parahaemolyticus infection. Tissue distribution analysis revealed that IL-1R was predominantly expressed in hemocytes and was significantly induced following immune stimulation. Co-immunoprecipitation and AlphaFold-based structural modeling demonstrated that IL-1R interacted with the adaptor protein MyD88 through its intracellular Toll/interleukin-1 receptor (TIR) domain. Functional analyses showed that silencing IL-1R markedly impaired pathogen-induced NF-κB (Dorsal) nuclear translocation, indicating that IL-1R functions upstream of the MyD88-Dorsal signaling pathway. Notably, recombinant IL-1R exhibited broad-spectrum binding activity toward both Gram-positive and Gram-negative bacteria, revealing a pathogen-recognition function that has not been reported for vertebrate IL-1Rs. Furthermore, administration of soluble recombinant IL-1R significantly increased bacterial burden and mortality in infected shrimp, whereas RNA interference-mediated knockdown of IL-1R produced similar susceptibility phenotypes. Collectively, our findings revealed a previously unrecognized dual-function mechanism of crustacean IL-1R, acting both as a pathogen-recognition receptor and as a signaling receptor that activated the MyD88-Dorsal pathway to orchestrate antibacterial immunity. This study expands current understanding of IL-1R evolution and innate immune regulation in crustaceans and provides a potential molecular target for disease-resistant breeding and immune intervention strategies in shrimp aquaculture.

Si-You Huang, Wan-Li Lu, Yuxin Shi et al. · 0 citations
Aug 2026

Atypical toxin psyrT modulates bacterial virulence and host inflammatory responses in Pseudomonas plecoglossicida-infected large yellow croaker.

Bacterial toxin-antitoxin (TA) systems are widespread genetic modules that regulate bacterial stress adaptation and pathogenicity. The atypical Type II psyrTA system encodes the toxin PsyrT with conserved RecQ-containing DEXDc and HELICc helicase domains, a rare architecture among characterized TA toxins. The toxic and pathogenic regulatory functions of helicase-containing TA toxins remain experimentally unvalidated. Here, we functionally characterized the psyrTA system in Pseudomonas plecoglossicida PQLYC4, the pathogen causing visceral white spot disease in large yellow croaker. Heterologous expression in Escherichia coli verified that PsyrT exerts potent growth-inhibitory toxicity, which is efficiently alleviated by cognate PsyrA via direct physical interaction. Deletion of psyrT markedly impaired biofilm formation, downregulated virulence gene transcription, reduced splenic colonization, and alleviated splenic histopathological damage in infected fish. Additionally, ΔpsyrT infection significantly attenuated host splenic cytokine transcriptional responses. Collectively, this study identifies PsyrT as a novel RecQ helicase domain-containing TA toxin and an important virulence modulator in P. plecoglossicida, expanding the functional diversity of bacterial TA systems.

Yudong Zheng, Jia-Tong Chen, Yan Teng et al. · 0 citations

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