Qiongyao Zeng , Yiyang Tang , Yujun Liu , Ye Yang , Pingyuan Li , Zejun Zhou , Qinbo Qin
{"title":"A recombinant sPLA2 protein promotes gut mucosal barrier against bacterial infection in fish","authors":"Qiongyao Zeng , Yiyang Tang , Yujun Liu , Ye Yang , Pingyuan Li , Zejun Zhou , Qinbo Qin","doi":"10.1016/j.dci.2024.105288","DOIUrl":"10.1016/j.dci.2024.105288","url":null,"abstract":"<div><div>Secreted phospholipase A2 family protein (sPLA2) is associated with immune response and plays a critical role in the regulation of gut homeostasis. However, whether sPLA2 is involved in innate immunity in teleost is essentially unknown. For this purpose, we reported the identification of a classical sPLA2 in grass carp (<em>Ci</em>sPLA2) and elucidated its role in the antibacterial immunity in this study. The result of bioinformatics analysis showed that mammalian sPLA2-IIA is the most similar homologue to <em>Ci</em>sPLA2. <em>CisPLA2</em> is expressed in a variety of tissues, including liver and gut, and is significantly upregulated in response to <em>Aeromonas hydrophila</em> infection. Recombinant <em>Ci</em>sPLA2 protein (r<em>Ci</em>sPLA2) showed significant antibacterial activity against <em>A</em>. <em>hydrophila</em> by enhancing the phagocytosis of host phagocytes <em>in vitro</em>. Moreover, r<em>Ci</em>sPLA2 induces significant expression of the antimicrobial molecules and tight junctions in the gut during bacterial infection. Fish administered with r<em>Ci</em>sPLA2 significantly alleviates the gut permeability and apoptosis. In addition, r<em>Ci</em>sPLA2 preserves the morphology of the gut mucosa and limits the colonization of <em>A</em>. <em>hydrophila</em> in systemic immune organs. These results indicate that <em>Ci</em>sPLA2 plays a crucial role in the regulation of gut mucosal barrier, and thus has a potential application for antimicrobial immunity in fish.</div></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":"162 ","pages":"Article 105288"},"PeriodicalIF":2.7,"publicationDate":"2024-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142616551","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Erin Glass , Stephan L. Robinson , Emily E. Rosowski
{"title":"Zebrafish use conserved CLR and TLR signaling pathways to respond to fungal PAMPs in zymosan","authors":"Erin Glass , Stephan L. Robinson , Emily E. Rosowski","doi":"10.1016/j.dci.2024.105286","DOIUrl":"10.1016/j.dci.2024.105286","url":null,"abstract":"<div><div>Pattern recognition receptors (PRRs) such as C-type lectin receptors (CLRs) and Toll-like receptors (TLRs) are used by hosts to recognize pathogen-associated molecular patterns (PAMPs) in microorganisms and to initiate innate immune responses. While PRRs exist across invertebrate and vertebrate species, the functional homology of many of these receptors is still unclear. In this study, we investigate the innate immune response of zebrafish larvae to zymosan, a β-glucan-containing particle derived from fungal cell walls. Macrophages and neutrophils robustly respond to zymosan and are required for zymosan-induced activation of the NF-κB transcription factor. Full activation of NF-κB in response to zymosan depends on Card9/Syk and Myd88, conserved CLR and TLR adaptor proteins, respectively. Two putative CLRs, Clec4c and Sclra, are both required for maximal sensing of zymosan and NF-κB activation but not required for inflammatory gene expression. Altogether, we identify conserved PRRs and PRR signaling pathways in larval zebrafish that promote recognition of fungal PAMPs. These results inform modeling of human fungal infections in zebrafish and increase our knowledge of the evolution and conservation of PRR pathways in vertebrates.</div></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":"162 ","pages":"Article 105286"},"PeriodicalIF":2.7,"publicationDate":"2024-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142616554","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
D.C.G. Rodrigo , H.M.V. Udayantha , D.S. Liyanage , W.K.M. Omeka , Y.K. Kodagoda , H.A.C.R. Hanchapola , M.A.H. Dilshan , G.A.N.P. Ganepola , W.A.D.L.R. Warnakula , Gaeun Kim , Jeongeun Kim , Jihun Lee , Qiang Wan , Jehee Lee
{"title":"Functional characterization of peroxiredoxin 5 from yellowtail clownfish (Amphiprion clarkii): Immunological expression assessment, antioxidant activities, heavy metal detoxification, and nitrosative stress mitigation","authors":"D.C.G. Rodrigo , H.M.V. Udayantha , D.S. Liyanage , W.K.M. Omeka , Y.K. Kodagoda , H.A.C.R. Hanchapola , M.A.H. Dilshan , G.A.N.P. Ganepola , W.A.D.L.R. Warnakula , Gaeun Kim , Jeongeun Kim , Jihun Lee , Qiang Wan , Jehee Lee","doi":"10.1016/j.dci.2024.105289","DOIUrl":"10.1016/j.dci.2024.105289","url":null,"abstract":"<div><div>Peroxiredoxin 5 (<em>Prdx5</em>) is the last recognized member of Prdx family. It is a unique, atypical, 2-Cys antioxidant enzyme, protecting cells from death caused by reactive oxygen species (ROS). In this study, the Prdx5 ortholog of <em>Amphiprion clarkii</em> (<em>AcPrdx5</em>) was identified and characterized to explore its specific structural features and functional properties. The open reading frame of AcPrdx5 is 573 bp long and encodes 190 amino acids containing a mitochondrial targeting sequence, thioredoxin domain, and two conserved cysteine residues responsible for antioxidant function. The predicted molecular weight and theoretical isoelectric point of AcPrdx5 are 20.3 kDa and 9.01, respectively. AcPrdx5 sequences were found to be highly conserved across the other orthologs from various organisms and it distinctively clustered within the fish <em>Prdx5</em> subclade of the phylogenetic tree. The expression of <em>AcPrdx5</em> was ubiquitously detected among twelve tested tissues, with the highest level in the brain. Furthermore, the mRNA levels of <em>AcPrdx5</em> in the blood and head-kidney tissues were significantly (<em>p < 0.05</em>) upregulated following polyinosinic-polycytidylic acid (Poly I:C), lipopolysaccharide (LPS), and <em>Vibrio harveyi</em> immune challenge<em>.</em> A concentration-dependent antioxidant potential of recombinant AcPrdx5 was observed in insulin disulfide bond reduction, heavy metal detoxification, free radical and hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) scavenging assays. Additionally, AcPrdx5 overexpression in fathead minnow (FHM) cells upregulated the antioxidant-associated gene (Rrm1, MAPK, SOD2, and PRDX1) expression after H<sub>2</sub>O<sub>2</sub> treatment, and promoted cell viability upon arsenic (As) exposure. In macrophages, AcPrdx5 overexpression effectively suppressed substantial nitric oxide production under lipopolysaccharide treatment. Collectively, our results suggest that AcPrdx5 may play roles in both antioxidant defense system and innate immune response against pathogenic invasions in <em>A</em>. <em>clarkii</em>.</div></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":"162 ","pages":"Article 105289"},"PeriodicalIF":2.7,"publicationDate":"2024-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142616552","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Victoria L. Rhodes , Robert M. Waterhouse , Kristin Michel
{"title":"The molecular toll pathway repertoire in anopheline mosquitoes","authors":"Victoria L. Rhodes , Robert M. Waterhouse , Kristin Michel","doi":"10.1016/j.dci.2024.105287","DOIUrl":"10.1016/j.dci.2024.105287","url":null,"abstract":"<div><div>Innate immunity in mosquitoes has received much attention due to its potential impact on vector competence for vector-borne disease pathogens, including malaria parasites. The nuclear factor (NF)-κB-dependent Toll pathway is a major regulator of innate immunity in insects. In mosquitoes, this pathway controls transcription of the majority of the known canonical humoral immune effectors, mediates anti-bacterial, anti-fungal and anti-viral immune responses, and contributes to malaria parasite killing. However, besides initial gene annotation of putative Toll pathway members and genetic analysis of the contribution of few key components to immunity, the molecular make-up and function of the Toll pathway in mosquitoes is largely unexplored. To facilitate functional analyses of the Toll pathway in mosquitoes, we report here manually annotated and refined gene models of Toll-like receptors and all putative components of the intracellular signal transduction cascade across 19 anopheline genomes, and in two culicine genomes. In addition, based on phylogenetic analyses, we identified differing levels of evolutionary constraint across the intracellular Toll pathway members, and identified a recent radiation of TOLL1/5 within the <em>Anopheles gambiae</em> complex. Together, this study provides insight into the evolution of TLRs and the putative members of the intracellular signal transduction cascade within the genus <em>Anopheles</em>.</div></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":"162 ","pages":"Article 105287"},"PeriodicalIF":2.7,"publicationDate":"2024-11-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142616555","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Characterization of a fish-specific immunoglobulin-like domain-containing protein (Igldcp) in zebrafish (Danio rerio) induced after nodavirus infection","authors":"Nieves Martínez-López, Patricia Pereiro, Amaro Saco, Raquel Lama, Antonio Figueras, Beatriz Novoa","doi":"10.1016/j.dci.2024.105285","DOIUrl":"10.1016/j.dci.2024.105285","url":null,"abstract":"<div><div>One of the most highly induced genes in zebrafish (<em>Danio rerio</em>) larvae after infection with the nodavirus red-spotted grouper nervous necrosis virus (RGNNV) was a member of the immunoglobulin superfamily (IgSF), which has remained uncharacterized and erroneously annotated in zebrafish and other fish species as <em>galectin 17</em> (<em>lgals17</em>). We characterized this gene and named it <em>immunoglobulin (Ig)-like domain-containing protein</em> (<em>igldcp</em>), a new member of the IgSF that does not possess orthologs in mammals. Igldcp expression is induced by viral infection and it belongs to the group of interferon-stimulated genes (ISGs). <em>In vitro</em> overexpression of <em>igldcp</em> decreased RGNNV replication, whereas <em>in vivo</em> knockdown of this gene had the opposite effect, resulting in increased larval mortality. RNA-Seq analyses of larvae overexpressing <em>igldcp</em> in the absence or presence of infection with RGNNV showed that the main processes affected by Igldcp could be directly involved in the regulation of various cellular processes associated with the modulation of the immune system.</div></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":"162 ","pages":"Article 105285"},"PeriodicalIF":2.7,"publicationDate":"2024-11-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142603423","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Xue Kong , Wei Wang , Sunan Xia , Ying Zhi , Yuefeng Cai , Haibin Zhang , Xin Shen
{"title":"Molecular and functional characterization of short peptidoglycan recognition proteins in Vesicomyidae clam","authors":"Xue Kong , Wei Wang , Sunan Xia , Ying Zhi , Yuefeng Cai , Haibin Zhang , Xin Shen","doi":"10.1016/j.dci.2024.105284","DOIUrl":"10.1016/j.dci.2024.105284","url":null,"abstract":"<div><div>Within cold seep environments, the Vesicomyidae clam emerges as a prevalent species, distinguished by its symbiotic relationship with microorganisms housed within its organ gill. Given the extreme conditions and the symbiotic nature of this association, investigating the host's immune genes, particularly immune recognition receptors, is essential for understanding their role in facilitating host-symbiotic interactions. Three short peptidoglycan recognition proteins (PGRPs) were identified in the clam. AmPGRP-S1, -S2, and -S3 were found to possess conserved amidase binding sites and Zn<sup>2+</sup> binding sites. Quantitative Real-time PCR (qRT-PCR) analysis revealed differential expression patterns among the PGRPs. AmPGRP-S1 and AmPGRP-S2 exhibited elevated expression levels in the gill, while AmPGRP-S3 displayed the highest expression in the adductor muscle. Functional experiments demonstrated that recombinant AmPGRP-S1, -S2, and -S3 (rAmPGRPs) exhibited binding capabilities to both L-PGN and D-PGN (peptidoglycan). Notably, rAmPGRP-S1 and -S2 possessed Zn<sup>2+</sup>-independent amidase activity, while rAmPGRP-S3 lacked this enzymatic function. rAmPGRPs were shown to bind to five different bacterial species. Among these, rAmPGRP-S1 inhibited <em>Escherichia coli</em> and <em>Bacillus subtilis</em>, while rAmPGRP-S2 and -S3 inhibited <em>Bacillus subtilis</em> in the absence of Zn<sup>2<em>+</em></sup>. In the presence of Zn<sup>2+</sup>, rAmPGRP-S1 and -S2 exhibited enhanced inhibitory activity against <em>Staphylococcus aureus</em> or <em>Bacillus subtilis</em>. These findings suggest that AmPGRPs may play a pivotal role in mediating the interaction between the host and endosymbiotic bacteria, functioning as PGN and microbe receptors, antibacterial effectors, and regulators of host-microbe symbiosis. These results contribute to our understanding of the adaptive mechanisms of deep-sea organisms to the challenging cold seep environments.</div></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":"162 ","pages":"Article 105284"},"PeriodicalIF":2.7,"publicationDate":"2024-11-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142567814","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Molecular depiction and functional delineation of E3 ubiquitin ligase MARCH5 in yellowtail clownfish (Amphiprion clarkii)","authors":"B.P.M. Vileka Jayamali , H.M.S.M. Wijerathna , D.M.K.P. Sirisena , H.A.C.R. Hanchapola , W.A.D.L.R. Warnakula , U.P.E. Arachchi , D.S. Liyanage , Sumi Jung , Qiang Wan , Jehee Lee","doi":"10.1016/j.dci.2024.105283","DOIUrl":"10.1016/j.dci.2024.105283","url":null,"abstract":"<div><div>Membrane-associated Ring-CH 5 (MARCH5) is a mitochondrial E3 ubiquitin ligase playing a key role in the regulation of mitochondrial dynamics. In mammals, MARCH5 negatively regulates mitochondrial antiviral signaling (MAVS) protein aggregation during viral infection and hampers downstream type I interferon signaling to prevent excessive immune activation. However, its precise functional role in the teleost immune system remains unclear. This study investigated the molecular characteristics and immune response of the MARCH5 ortholog in <em>Amphiprion clarkii</em> (<em>A. clarkii</em>; AcMARCH5). The predicted AcMARCH5 protein sequence consists of 287 amino acids with a molecular weight of 32.02 kDa and a theoretical isoelectric point of 9.11. It contains four C-terminal transmembrane (TM) domains and an N-terminal RING cysteine-histidine (CH) domain, which directly regulates ubiquitin transfer. Multiple sequence alignment revealed a high level of conservation between AcMARCH5 and its orthologs in other vertebrate species. Under normal physiological conditions, <em>AcMARCH5</em> showed the highest mRNA expression in the muscle, brain, and kidney tissues of <em>A. clarkii</em>. Upon stimulation with polyinosinic:polycytidylic acid (Poly I:C), lipopolysaccharide (LPS), and <em>Vibrio harveyi</em>, <em>AcMARCH5</em> expression was drastically modulated. Functional assays showed that overexpression of AcMARCH5 in fathead minnow (FHM) cells downregulated antiviral gene expression, accompanied by enhanced viral hemorrhagic septicemia virus (VHSV) replication. In murine macrophages, AcMARCH5 overexpression markedly reduced the production of pro-inflammatory cytokines in response to poly I:C treatment. Additionally, AcMARCH5 exhibited an anti-apoptotic effect in H<sub>2</sub>O<sub>2</sub>-treated FHM cells. Collectively, these results suggest that AcMARCH5 may play a role in maintaining cellular homeostasis under disease and stress conditions in <em>A. clarkii</em>.</div></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":"162 ","pages":"Article 105283"},"PeriodicalIF":2.7,"publicationDate":"2024-10-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142557392","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Dysregulated proinflammatory cytokines and immune-related miRNAs in ASK cells exposed to 17⍺-Ethynyl estradiol and 4-nonylphenol","authors":"Carolina Salazar , Nicolás Ojeda , Luis Mercado","doi":"10.1016/j.dci.2024.105282","DOIUrl":"10.1016/j.dci.2024.105282","url":null,"abstract":"<div><div>Endocrine Disruptor Compounds (EDCs) in the aquatic environment have acquired pronounced relevance due to their toxic effect on the aquatic flora and fauna. Xenoestrogens are EDCs that possess estrogenic activity and, thus, disrupt normal estrogen signaling, affecting different functions, such as immune system processes. Two relevant xenoestrogens discarded into fresh and seawater are 4-nonylphenol (NP) and 17⍺-Ethynyl Estradiol (EE2). Considering that the piscicultures of <em>Salmo salar</em> can be located at sites of potential exposure to xenoestrogen-containing effluxes, it is crucial to understand the effect of xenoestrogens on the immune response and its possible molecular mechanism in this species. Our studies reveal an increase in the expression of the receptor <em>era</em> and <em>erb</em> at early times of exposure, a disrupted expression of pro-inflammatory cytokines (<em>il1b</em> and <em>tnfa</em>), an upregulation of ssa-miR-146a-5p, ssa-miR-125 b-5p, and downregulation of ssa-miR-145–5p in ASK cells exposed to estrogen and xenoestrogen, could potentially lead to new strategies for mitigating the effects of xenoestrogens on <em>Salmo salar</em> immune response.</div></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":"162 ","pages":"Article 105282"},"PeriodicalIF":2.7,"publicationDate":"2024-10-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142496903","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"CqProfilin enhances WSSV infection by promoting viral intracellular transport through binding to both viral nucleocapsid and actin cytoskeleton","authors":"Dong-li Li , Wen-lin Wu , Hai-peng Liu","doi":"10.1016/j.dci.2024.105281","DOIUrl":"10.1016/j.dci.2024.105281","url":null,"abstract":"<div><div>White spot syndrome virus (WSSV) is a large nuclear-replicating DNA virus of crustaceans such as shrimp and crayfish; however, the molecular mechanisms facilitating its transport from the invasion site to the cell nucleus have not yet been well elucidated. In this study, a <em>Cq</em>Profilin (<em>Cq</em>PFN) with a conserved PROF domain was identified from the red claw crayfish <em>Cherax quadricarinatus</em>. <em>CqPFN</em> was ubiquitously expressed in all examined tissues and hemocyte, with the highest levels in the hemocyte, followed by hematopoietic tissue (Hpt) from which the hemocyte were derived in crayfish. The transcript of WSSV genes such as <em>IE1</em> and <em>VP28</em> was obviously decreased both <em>in vivo</em> in hemocyte and Hpt, as well as <em>in vitro</em> in cultured Hpt cells, after <em>CqPFN</em> gene silencing; in contrast, the expression of viral genes was significantly increased by the introduction of a recombinant <em>Cq</em>PFN protein in Hpt cells <em>in vitro</em>. Moreover, <em>Cq</em>PFN was clearly colocalized with the main viral nucleocapsid protein VP664 and F-actin cytoskeleton, respectively, during the early stage of WSSV infection in Hpt cells. In addition, <em>Cq</em>PFN was confirmed to interact with a truncated VP664<sup>2,405-2,535</sup> and another viral nucleocapsid protein VP15 of WSSV and <em>Cq</em>β-Actin from Hpt by co-immunoprecipitation assays. Further studies found that VP664 also colocalized with F-actin in the Hpt cell cytoplasm after WSSV infection, suggesting that the actin cytoskeleton was involved in the intracellular transport of incoming viral nucleocapsid. Taken together, <em>Cq</em>PFN might combine with the actin cytoskeleton to promote WSSV infection through binding with viral nucleocapsid proteins VP664 and VP15, promoting intracellular transport of viral incoming nucleocapsid for further releasing genome into the nucleus for transcription. Collectively, these results provided an understanding of the WSSV pathogenesis, which will contribute to the development of an antiviral strategy against WSSV disease.</div></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":"162 ","pages":"Article 105281"},"PeriodicalIF":2.7,"publicationDate":"2024-10-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142460364","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Sara Pedrazzoli, Giulia Graziosi, Roberta Salaroli, Elena Catelli, Caterina Lupini
{"title":"Dynamic alterations in T-lymphocyte subsets assessed by flow cytometry in chickens following exposure to infectious bursal disease virus: A systematic review","authors":"Sara Pedrazzoli, Giulia Graziosi, Roberta Salaroli, Elena Catelli, Caterina Lupini","doi":"10.1016/j.dci.2024.105280","DOIUrl":"10.1016/j.dci.2024.105280","url":null,"abstract":"<div><div>Infectious bursal disease virus (IBDV) is a significant pathogen in poultry, causing acute immunosuppressive disease in young chickens. While B-lymphocyte involvement in IBDV pathogenesis is known, the role of T-cells is incompletely understood. This systematic review presents the alterations in chicken T-lymphocyte subsets after IBDV exposure, assessed by flow cytometry analysis. Four databases were queried for identifying eligible studies focused on experimental infections measuring T-lymphocyte changes in the bursa of Fabricius, spleen, thymus, and peripheral blood mononuclear cells. Of 488 studies found, 25 met the pre-established criteria and were included in the qualitative synthesis of results. Most studies analysed T-lymphocyte responses during the acute phase of IBDV infection, primarily focusing on CD4<sup>+</sup> and CD8<sup>+</sup> T-cells. Other subsets, such as γδ T-cells and double-positive CD4<sup>+</sup>CD8<sup>+</sup> T-cells, were less frequently investigated. An increase in T-lymphocytes was noted in the bursa of Fabricius, suggesting their active role in viral clearance. In the spleen, CD4<sup>+</sup> T-cells commonly increased, while CD8<sup>+</sup> responses varied among studies. Increased levels in T-cells were also noted during the chronic infection in the bursa of Fabricius, possibly due to persistent viral antigens. Overall, variations in flow cytometry methods and T-cell output reporting were noted among studies.</div><div>Based on the data collected, further investigation into diverse T-cell subpopulations beyond CD4<sup>+</sup> and CD8<sup>+</sup> is needed, as well as the standardization of flow cytometry assays in chickens.</div></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":"162 ","pages":"Article 105280"},"PeriodicalIF":2.7,"publicationDate":"2024-10-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142460365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}