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| Main Authors: | , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Developmental and comparative immunology
2026
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/41506560/ |
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| _version_ | 1868266102684909570 |
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| author | Liang, Bangyao Meng, Wei Chen, Meihan Miao, Hongfei Ren, Yuhan Liu, Hongyu Liu, Zhenhui Sun, Chen |
| author_facet | Liang, Bangyao Meng, Wei Chen, Meihan Miao, Hongfei Ren, Yuhan Liu, Hongyu Liu, Zhenhui Sun, Chen Liang, Bangyao Meng, Wei Chen, Meihan Miao, Hongfei Ren, Yuhan Liu, Hongyu Liu, Zhenhui Sun, Chen |
| collection | PubMed - marine biology |
| contents | Peroxiredoxin 4 from amphioxus: An antioxidant enzyme with immunomodulatory roles in defense against Vibrio anguillarum. Liang, Bangyao Meng, Wei Chen, Meihan Miao, Hongfei Ren, Yuhan Liu, Hongyu Liu, Zhenhui Sun, Chen Animals Vibrio Peroxiredoxins Lancelets Vibrio Infections Antioxidants Amino Acid Sequence Immunity, Innate Phylogeny Phagocytosis Peroxiredoxin 4 (Prdx4), a typical 2-Cys peroxiredoxin, functions as both an antioxidant enzyme and a regulator of immune processes, yet its roles in early chordates remain unclear. Here, we identified and characterized a Prdx4 homolog from amphioxus (Branchiostoma japonicum), termed BjPrdx4. Sequence analyses revealed conserved catalytic motifs and an N-terminal signal peptide, supporting its classification as Prdx4. BjPrdx4 was constitutively expressed across multiple tissues, with prominent localization in immune-associated tissues, and its expression was markedly induced following Vibrio anguillarum challenge. Infection also triggered BjPrdx4 secretion into the extracellular milieu and altered its oligomeric states. Recombinant BjPrdx4 exhibited robust thiol-dependent peroxidase activity, efficiently eliminating hydrogen peroxide and protecting plasmid DNA from oxidative damage, confirming its antioxidant function. Functionally, extracellular BjPrdx4 preserved gill integrity and reduced bacterial burden during infection. Transcriptomic and qRT-PCR analyses further demonstrated that BjPrdx4 influenced immune-related pathways, including phagocytosis and lysosomal activity, and positively regulated ras expression, suggesting involvement in Ras-MAPK signaling. Together, these findings reveal that BjPrdx4 integrates antioxidant defense with immunomodulatory functions, highlighting its dual role in amphioxus antibacterial immunity and underscoring the evolutionary significance of Prdx4 multifunctionality in basal chordates. |
| format | Artículo científico |
| id | pubmed_41506560 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | Developmental and comparative immunology |
| record_format | pubmed |
| spellingShingle | Peroxiredoxin 4 from amphioxus: An antioxidant enzyme with immunomodulatory roles in defense against Vibrio anguillarum. Liang, Bangyao Meng, Wei Chen, Meihan Miao, Hongfei Ren, Yuhan Liu, Hongyu Liu, Zhenhui Sun, Chen Animals Vibrio Peroxiredoxins Lancelets Vibrio Infections Antioxidants Amino Acid Sequence Immunity, Innate Phylogeny Phagocytosis Peroxiredoxin 4 from amphioxus: An antioxidant enzyme with immunomodulatory roles in defense against Vibrio anguillarum. Liang, Bangyao Meng, Wei Chen, Meihan Miao, Hongfei Ren, Yuhan Liu, Hongyu Liu, Zhenhui Sun, Chen Animals Vibrio Peroxiredoxins Lancelets Vibrio Infections Antioxidants Amino Acid Sequence Immunity, Innate Phylogeny Phagocytosis Peroxiredoxin 4 (Prdx4), a typical 2-Cys peroxiredoxin, functions as both an antioxidant enzyme and a regulator of immune processes, yet its roles in early chordates remain unclear. Here, we identified and characterized a Prdx4 homolog from amphioxus (Branchiostoma japonicum), termed BjPrdx4. Sequence analyses revealed conserved catalytic motifs and an N-terminal signal peptide, supporting its classification as Prdx4. BjPrdx4 was constitutively expressed across multiple tissues, with prominent localization in immune-associated tissues, and its expression was markedly induced following Vibrio anguillarum challenge. Infection also triggered BjPrdx4 secretion into the extracellular milieu and altered its oligomeric states. Recombinant BjPrdx4 exhibited robust thiol-dependent peroxidase activity, efficiently eliminating hydrogen peroxide and protecting plasmid DNA from oxidative damage, confirming its antioxidant function. Functionally, extracellular BjPrdx4 preserved gill integrity and reduced bacterial burden during infection. Transcriptomic and qRT-PCR analyses further demonstrated that BjPrdx4 influenced immune-related pathways, including phagocytosis and lysosomal activity, and positively regulated ras expression, suggesting involvement in Ras-MAPK signaling. Together, these findings reveal that BjPrdx4 integrates antioxidant defense with immunomodulatory functions, highlighting its dual role in amphioxus antibacterial immunity and underscoring the evolutionary significance of Prdx4 multifunctionality in basal chordates. |
| title | Peroxiredoxin 4 from amphioxus: An antioxidant enzyme with immunomodulatory roles in defense against Vibrio anguillarum. |
| topic | Animals Vibrio Peroxiredoxins Lancelets Vibrio Infections Antioxidants Amino Acid Sequence Immunity, Innate Phylogeny Phagocytosis |
| url | https://pubmed.ncbi.nlm.nih.gov/41506560/ |