Comparative Immunology Reports最新文献

{"title":"Effect of chitooligosaccharides on the growth and immune capability of Crassostrea gigas larvae","authors":"Wentong Hao, Bo Wang, Junyan Zhao, Ao Xu, Ning Kong, Lingling Wang, Linsheng Song","doi":"10.1016/j.cirep.2025.200251","DOIUrl":"https://doi.org/10.1016/j.cirep.2025.200251","url":null,"abstract":"• Chitooligosaccharides (COS) promoted the growth of Crassostrea gigas larvae. • COS enhanced the immune capability of C. gigas and increased its survival rate . • COS is expected to be a sustainable alternative to antibiotics in the oyster farming industry. The oyster aquaculture contributes significantly to the aquaculture in China, while recently, it has been suffered by frequent larval mortality caused by pathogenic bacteria. Developing antibiotic-free immunopotentiator is an effective strategy to enhance the immunity of oyster larvae and address the mortality issue. Chitooligosaccharide (COS), an eco-friendly prebiotic, was applied to investigate its effect on the growth and immune capability of Crassostrea gigas larvae. The growth performance of C. gigas larvae was improved by COS treatment at concentrations of 0.1, 1, 10 mg/L. After Vibrio splendidus challenge, larval survival was significantly increased only by the 10 mg/L COS treatment (64.2%). The survival rate in the 10 mg/L COS-treated group was 3.03-fold higher than that of the control group (21.2%), and 1.77-fold, 1.72-fold higher than that of the 0.1 mg/L (36.2%) and 1 mg/L (37.3%) COS-treated groups. After 10 mg/L COS treatment, the catalase (CAT) activity (3.59-fold, p < 0.05), superoxide dismutase (SOD) activity (1.25-fold, p < 0.05) and the total antioxidant capacity (T-AOC) (1.72-fold, p < 0.05) were significantly increased compared to the control group. Larval protein extracts from COS-treated group significantly inhibited the growth of V. splendidus and Staphylococcus aureus . Furthermore, COS reshaped the larval associated microbial composition by reducing the relative abundance of potential pathogenic bacteria, such as Acinetobacter and Vibrio (Proteobacteria). In summary, COS treatment promoted growth, enhanced immune capability and modulated the associated microbial composition in oyster larvae. These findings highlight the potential of COS as a sustainable alternative to antibiotics in the oyster farming industry.","PeriodicalId":516937,"journal":{"name":"Comparative Immunology Reports","volume":"9 1","pages":"200251-200251"},"PeriodicalIF":0.0,"publicationDate":"2025-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147881642","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Expression and functional characterization of three peptidoglycan recognition proteins, PGRP-L1, PGRP-L2 and PGRP-S in snakehead (Channa argus)","authors":"Zhen Yu Zhou, Wei Hao, Pin Nie, Shan Nan Chen, Jing Hou","doi":"10.1016/j.cirep.2025.200248","DOIUrl":"https://doi.org/10.1016/j.cirep.2025.200248","url":null,"abstract":"• Two long-type PGRP and one short PGRP, named as CaPGRP-L1, -L2 and -S were identified from snakehead. • CaPGRP-L1, -L2 showed high expression in the intestine and liver, while CaPGRP-S was abundant in the gill. • Three snakehead PGRPs demonstrated PGN-binding activity, amidase activity and antibacterial activity . • Three snakehead PGRPs are involved in NF-κB signaling. Peptidoglycan recognition proteins (PGRPs) are evolutionarily conserved pattern recognition receptors critical for antibacterial immunity across vertebrates and invertebrates. In this study, two long-type (CaPGRP-L1, -L2) and one short-type (CaPGRP-S) PGRP genes were identified in snakehead ( Channa argus ), an economically important aquaculture species. Sequence analysis revealed that all three PGRPs contain a conserved Zn²⁺-binding site (composed of two His, one Tyr, and one Cys), essential for amidase activity. Tissue distribution profiling showed distinct expression patterns, with high transcript levels detected in liver, intestine or gill. Functional assays demonstrated that recombinant CaPGRP-L1, -L2, and -S bound peptidoglycan (PGN), displayed Zn²⁺-dependent amidase activity, and inhibited Aeromonas hydrophila infection. Furthermore, three PGRPs activated NF-κB promoter reporter plasmid in a dose-dependent manner, while NF-κB subunits c-Rel and p65 upregulated the transcriptional activity of CaPGRP-L1, -L2, and -S luciferase promoters, suggesting that snakehead PGRPs are involved in NF-κB signaling. Collectively, this study has explored the function of snakehead PGRPs, and deepens our understanding on innate immune mechanisms in fish, which should provide a theoretical foundation for the application of snakehead PGRPs in preventing and controlling diseases in aquaculture.","PeriodicalId":516937,"journal":{"name":"Comparative Immunology Reports","volume":"9 1","pages":"200248-200248"},"PeriodicalIF":0.0,"publicationDate":"2025-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147922585","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Genome-wide identification and functional characterization of NOD-like receptors (NLRs) in snakehead (Channa argus)","authors":"Xiaochen Zhu, Beibei Wang, Lu Zhang, Xiaoyan Zhang, Chao Li","doi":"10.1016/j.cirep.2025.200229","DOIUrl":"https://doi.org/10.1016/j.cirep.2025.200229","url":null,"abstract":"• A total of 33 NLR genes were detected in snakehead. • The altered expression patterns of NLR genes indicate their involvement in the immune response to Nocardia seriolae . • The inhibitory effect of NLRC18 on NF-κB activation reached 38%, and the expression level of NLRC18 was upregulated by 339.6-fold after stimulation with iE-DAP. NLR (NOD-like receptor) is a pattern recognition receptors (PRRs) and is crucial in the innate immune response. It identifies pathogen-associated molecular patterns (PAMPs) and modulates associated immune pathways. Snakehead ( Channa argus ) is an economically important fish with rapid growth and high meat content, but research on its NLR family is still incomplete. In this study, a total of 33 NLR genes were identified in snakehead, among which NOD1, NOD2, NLRC5 and MHC class II transactivator (CIITA) belong to the NLR-A subfamily, NLRC1-NLRC4 and NLRC6-NLRC27 belong to the NLR-C subfamily, and NLRX1, APAF1 and NWD1 belong to other subfamilies. Their biological characteristics, phylogenetic relationships, gene structure, conserved motifs, domain organization, expression profiles, and protein-protein interaction networks were characterized. In addition, the expression of NLR genes was observed in different healthy tissues of snakehead, and the expression patterns were diverse. The expression levels were the highest in the blood, intestine and gill. Nocardia seriolae is a key pathogenic bacterium that causes diseases in snakehead. The altered expression patterns of NLR genes indicate their involvement in the immune response to N.seriolae . Finally, it was also detected that the inhibitory effect of NLRC18 on NF-κB activation reached 38%, and the expression level of NLRC18 was upregulated by 339.6-fold after stimulation with iE-DAP. This study offers robust evidence that enhances our understanding of the immune regulatory mechanisms and functional roles of NLR genes in snakehead.","PeriodicalId":516937,"journal":{"name":"Comparative Immunology Reports","volume":"8 1","pages":"200229-200229"},"PeriodicalIF":0.0,"publicationDate":"2025-05-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147888249","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A type I crustin with an inhibitory effect on proteases and strong binding capacity to chitin from Neocaridina denticulata sinensis","authors":"Dandan Feng, Zhu Zhu, Shangpeng Wang, Yuanzhu Gao, Yingwen Li, Yuying Sun, Jiquan Zhang","doi":"10.1016/j.cirep.2025.200226","DOIUrl":"https://doi.org/10.1016/j.cirep.2025.200226","url":null,"abstract":"· This study identifies a new crustin from Neocaridina denticulata sinensis , NdCrus1 · Both native and recombinant NdCrus1 appear to strongly bind chitin · Recombinant NdCrus1 does not inhibit growth of two bacterial pathogens · Recombinant NdCrus1 inhibits proteases under a wide range of temperatures Antimicrobial peptides (AMPs) are crucial immune effectors in the defense against pathogens. Crustins, small molecule antimicrobial peptides found in crustaceans, exhibit antimicrobial and antiviral properties, microbial binding ability, biofilm growth inhibition, and protease inhibition. In this study, we identify and characterize a crustin (named NdCrus1) from Neocaridina denticulata sinensis . The NdCrus1 was expressed in all tested tissues, with the highest expression in the stomach. NdCrus1 shares a high identity with type I crustins and contains a whey acidic protein (WAP) domain, featuring eight cysteine residues that form the conserved ‘‘four-disulfide core’’ structure. Recombinant NdCrus1 (rNdCrus1) did not significantly inhibit Bacillus subtilis and Vibrio parahaemolyticus but possessed an inhibitory effect on proteases under a wide range of temperature conditions. In addition, in vitro binding assays and molecular docking results indicated that NdCrus1 had a strong binding capacity with chitin. These results provide new insights into crustins in the life activities of N. denticulata sinensis and provide references for studying antibacterial activity characteristics and mechanisms in other crustaceans.","PeriodicalId":516937,"journal":{"name":"Comparative Immunology Reports","volume":"8 1","pages":"200226-200226"},"PeriodicalIF":0.0,"publicationDate":"2025-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147330861","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effects of the amino acid mixture, ‘NutriMix’, on growth performance, non-specific immunity and intestinal health in sea cucumber (Apostichopus japonicus)","authors":"Jiali Wu, Chengjie Lv, Xiaojing Lv, Yongliang Liu, Weiwei Zhang, Dinglong Yang, Jianmin Zhao","doi":"10.1016/j.cirep.2025.200217","DOIUrl":"https://doi.org/10.1016/j.cirep.2025.200217","url":null,"abstract":"• NutriMix, a blend of lysine, methionine, and arginine, significantly boosts growth in sea cucumber Apostichopus japonicus . • Optimal dosage of NutriMix can enhance immune response and digestive enzyme activity. • NutriMix improves intestinal health and regulates gut microbiota in sea cucumber Apostichopus japonicus . In the present study, a mixture of amino acids (NutriMix) was used to evaluate its effects on growth performance, non-specific immunity and intestinal health in sea cucumber ( Apostichopus japonicus ). During a 56-day feeding trial, the sea cucumber (0.92 ± 0.05g) was fed with basal diet (control, CT) and treatment diets supplemented at different doses of amino acid mixture, 0.5‰ (AL), 1‰ (AM) and 2‰ (AH) (w/w, parts per thousand). The weight gain rate (WGR) and specific growth rate (SGR) of A. japonicus fed amino acid mixture were significantly increased in the AM group ( P <0.05). Additionally, the trypsin and lipase activities of the intestine were significantly increased in the AM group ( P <0.05). Analysis of the intestinal morphological features indicated that in the AM group, the intestinal structure of sea cucumber was more regular, longer, with intact intestinal villi, and with a complete muscular layer. Also, the muscle and mucosal layers are thicker. Alpha diversity analysis showed that the amino acid mixture-supplemented groups had higher intestinal microbial richness and diversity than the CT group. Furthermore, beta diversity analysis demonstrated distinct bacterial community structures between the amino acid mixture-supplemented groups and the control group, with Proteobacteria, Bacteroidota , and Verrucomicrobiota being the most abundant phyla. Notably, the AM group exhibited significant differences in intestinal microbiota composition, which may play a crucial role in the improved growth performance and health of A. japonicus . In conclusion, dietary addition of amino acid mixture could effectively promote the growth of A. japonicus , achieve cost-sparing effect in aquafeed, improve its digestion and immunity capacity to a certain extent, and actively regulate the intestinal microflora of A. japonicus .","PeriodicalId":516937,"journal":{"name":"Comparative Immunology Reports","volume":"8 1","pages":"200217-200217"},"PeriodicalIF":0.0,"publicationDate":"2025-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147919487","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mindin promotes the production of reactive oxygen species to regulate intestinal microbiota in kuruma shrimp Marsupenaeus japonicus","authors":"Kaimin Zhou, Bao-Rui Zhao, Jie Gao, Yongzhen Zhao, Yueling Zhang, Xian‐Wei Wang","doi":"10.1016/j.cirep.2025.200207","DOIUrl":"https://doi.org/10.1016/j.cirep.2025.200207","url":null,"abstract":"• Mindin plays an antibacterial role in the intestine of marsupenaeus japonicus . • Mindin promotes the production of reactive oxygen species. • Mindin regulates the transcription of dual oxidase 2. The Mindin/Spondin family, as host extracellular matrix components, comprises key immune-related molecules in both mammals and Drosophila . While the detailed mechanisms of Mindin's function and its role in initiating an effective immune response have been elucidated in model animals, its immune regulatory function in invertebrates remains largely unknown. In the present study, we identified and characterized a Mindin homolog from kuruma shrimp ( Marsupenaeus japonicus ), which was significantly up-regulated upon Vibrio anguillarum infection. Our findings revealed that Mindin plays a crucial protective role in the antibacterial response by regulating dual oxidase 2 (Duox2) expression. Mechanistically, Mindin recognizes V. anguillarum through its Tsp domain and simultaneously interacts with cell membrane integrin via its SpN domain. This dual interaction triggers the phosphorylation of extracellular regulated kinase (Erk), leading to the activation and phosphorylation of transcription factor Atf2. The phosphorylated Atf2 translocates to the nucleus where it induces the expression of Duox2, resulting in the production of reactive oxygen species (ROS) that effectively inhibit bacterial growth. By establishing the Mindin/Integrin/Erk/Atf2/Duox2 signaling axis, this study unveils a novel antibacterial mechanism in shrimp and provides new insights into the functional role of Mindin in invertebrate immunity.","PeriodicalId":516937,"journal":{"name":"Comparative Immunology Reports","volume":"8 1","pages":"200207-200207"},"PeriodicalIF":0.0,"publicationDate":"2025-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147897618","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"MsCL-P1: A multifunctional C-type lectin from largemouth bass (Micropterus salmoides) with broad microbe binding and agglutination activities","authors":"Siyi She, Ying Ye, Feng Guo, Shun Yang, Mengmeng Huang, Hui Fei","doi":"10.1016/j.cirep.2025.200201","DOIUrl":"https://doi.org/10.1016/j.cirep.2025.200201","url":null,"abstract":"• MsCL-P1 exhibits PAMP-binding and agglutination capabilities against diverse microorganisms. • MsCL-P1 inhibits growth of various bacteria. • Largemouth bass MsCL-P1 plays a critical role in innate immunity and pathogen defense. C-type lectins are a family of calcium-dependent carbohydrate-recognition domain (CRD) containing proteins that play a pivotal role in innate immunity. In this study, we characterized a novel C-type lectin, MsCL-P1, from the largemouth bass ( Micropterus salmoides ), an economically important fish species in aquaculture. MsCL-P1, a transmembrane protein with a CRD, was identified through liver transcriptome sequencing and further analyzed for its immune functions. The full-length cDNA of MsCL-P1 encodes a polypeptide of 789 amino acids, including one CRD, four coiled coil regions, and two collagen domains. Sequence analysis revealed high similarity among CRD domains from different species, suggesting conserved binding specificity. The recombinant CRD of MsCL-P1 (rCRD) demonstrated binding activity to various pathogen-associated molecular patterns (PAMPs), including lipopolysaccharide (LPS), peptidoglycan (PGN), and glucan (GLU), as determined by ELISA. Furthermore, the rCRD showed significant binding activity towards multiple microbes, including Gram-positive bacteria, Gram-negative bacteria, and fungi. Agglutination assays revealed that rCRD could agglutinate Aeromonas veronii and Saccharomyces cerevisiae , but not Micrococcus luteus . Carbohydrate binding specificity assays indicated that rCRD's agglutination activity could be suppressed by D-mannose and D-galactose. Lastly, antibacterial activity assays showed that rCRD inhibited the growth of M. luteus, E. coli , and A. veronii . These results suggest that MsCL-P1 plays a multifaceted role in the innate immune response of largemouth bass, potentially through recognition of PAMPs, agglutination of microbes, and direct inhibition of microbial growth. This study enhances our understanding of the immune mechanisms in largemouth bass and contributes to the broader knowledge of C-type lectin functions in fish species.","PeriodicalId":516937,"journal":{"name":"Comparative Immunology Reports","volume":"8 1","pages":"200201-200201"},"PeriodicalIF":0.0,"publicationDate":"2025-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147902049","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Glutamate enhances shrimp antibacterial ability by boosting its cellular immunity","authors":"Lei Ma, Wenyong Jiang, Zhiyao Lu, Yanmei Tong, Qingyun Liu, Zhonghua He, Xiuli Chen, Yongzhen Zhao, Fan Wang","doi":"10.1016/j.cirep.2025.200204","DOIUrl":"https://doi.org/10.1016/j.cirep.2025.200204","url":null,"abstract":"","PeriodicalId":516937,"journal":{"name":"Comparative Immunology Reports","volume":"8 1","pages":"200204-200204"},"PeriodicalIF":0.0,"publicationDate":"2025-01-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147331435","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The involvement of CgCaspase-3 in regulating the expressions of proinflammatory cytokines through NF-κB/Rel signaling pathway in oysters","authors":"Zihan Wang, Xiaopeng Li, Jiejie Sun, Shuyi Mu, Wei Wu, Renle Chang, Lingling Wang, Linsheng Song","doi":"10.1016/j.cirep.2025.200203","DOIUrl":"https://doi.org/10.1016/j.cirep.2025.200203","url":null,"abstract":"Cysteinyl aspartate specific proteinase-3 (Caspase-3) is a prominent mediator of apoptosis and participates in the cell death signaling cascade. In our previous study, Cg Caspase-3 identified from Crassostrea gigas was involved in Cg GSDME-dependent pyroptosis. In the present study, Cg Caspase-3 was demonstrated to regulate the expressions of proinflammatory cytokines through nuclear factor kappa B (NF-κB) signaling pathway. In haemocytes of Ac-DEVD-CHO-treated and Cg Caspase-3-RNAi oysters, the nuclear translocation of NF-κB/Rel was inhibited at 24 h after Vibrio splendidus stimulation. The mRNA expressions of interleukins 17s ( Cg IL17–2, Cg IL17–3, and Cg IL17–6), tumor necrosis factor-1 ( Cg TNF-1), high mobility group box-1 protein ( Cg HMGB1) and interferon-like protein ( Cg IFNLP) were significantly decreased in haemocytes of Cg Caspase-3-RNAi or Cg Rel-RNAi oysters, respectively. In addition, the phenomenon of gill swelling and cilia shedding was reduced in Cg Caspase-3-RNAi oysters after V. splendidus stimulation. These results indicated that Cg Caspase-3 was involved in regulating bacteria-induced inflammation through NF-κB/Rel signaling pathway.","PeriodicalId":516937,"journal":{"name":"Comparative Immunology Reports","volume":"8 1","pages":"200203-200203"},"PeriodicalIF":0.0,"publicationDate":"2025-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147913979","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A SH3b domain-containing peptidoglycan recognition protein from Magallana gigas with broad recognition spectrum","authors":"Yinan Li, Hongbo Lu, Chuanyan Yang, Zhuyun Liu, Weilin Wang, Chang Liu, Lingling Wang","doi":"10.1016/j.cirep.2025.200202","DOIUrl":"https://doi.org/10.1016/j.cirep.2025.200202","url":null,"abstract":"• The novel Mg PGRP5 with SH3b and a PGRP domain was identified in M. gigas . • Mg PGRP5 in haemocytes could respond to PGN and LPS. • The amino acid Asp230 and Glu106 were responsible for the binding activity of Mg PGRP-5 for PGN and LPS, respectively. • Mg PGRP-5 was able to bind and agglutinate various microbes. Peptidoglycan recognition protein (PGRP) is a kind of conserved pattern recognition receptors (PRRs) and plays important roles in innate immune response in both invertebrates and vertebrates. In the present study, nine Mg PGRP genes were identified in the updated genome of Magallana gigas , and the cDNA of Mg PGRP5 which was consisted of a SH3b and a PGRP domain was cloned. The mRNA transcripts of Mg PGRP5 were constitutively expressed in haemocytes and all the examined tissues, with the highest expression level in hepatopancreas. Both PGN and LPS stimulation could significantly up-regulated the expression level of Mg PGRP5 mRNA in haemocytes ( p < 0.05). Two amino acids in Mg PGRP5, Asp230 and Glu106, were identified as potential binding sites for PGN and LPS. The Mg PGRP5 protein was mainly located in nucleus of haemocytes, and showed widespread expression in hepatopancreas. The recombinant Mg PGRP5 protein (r Mg PGRP5) displayed strong binding and agglutinated activities to Gram-negative bacteria, Gram-positive bacteria and fungi. These results indicated that Mg PGRP5 could function as PRR with a broad range of recognition spectrum in the innate immune response of oyster.","PeriodicalId":516937,"journal":{"name":"Comparative Immunology Reports","volume":"8 1","pages":"200202-200202"},"PeriodicalIF":0.0,"publicationDate":"2025-01-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147911738","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}