Veterinary Research最新文献

{"title":"Cooperation between Adh and OR5M11 contributes to the lung pathogenicity of Actinobacillus pleuropneumoniae by facilitating the NLRP3-mediated inflammatory response.","authors":"Bo Wen, Xiaoli Yin, Xinhe Zhang, Chunling Zhu, Xiaofeng Li, Yilin Bai, Huarun Sun, Zhiyi Liu, Shuwen Ji, Ruibiao Wang, Chenru Yu, Jiaqi Wang, Longfei Zhang, Jiyuan Shen, Jianhe Hu, Yueyu Bai, Huihui Zhang, Ke Ding, Lei Wang","doi":"10.1186/s13567-026-01845-4","DOIUrl":"https://doi.org/10.1186/s13567-026-01845-4","url":null,"abstract":"<p><p>Actinobacillus pleuropneumoniae (A. pleuropneumoniae) is the etiologic agent of porcine pleuropneumonia, a severe respiratory disease characterized by hemorrhagic, necrotizing lung lesions that cause significant economic losses on the global swine industry. However, the molecular mechanisms underlying the lung pathogenicity of A. pleuropneumoniae remain unclear. Here we demonstrate that A. pleuropneumoniae infection induces lung injury through activating the NLRP3-mediated inflammatory response mediated by the YadA-like head region (Adh) of Apa1, a bacterial adhesin that mediates attachment to host cells. Importantly, we show that Adh triggers the NLRP3-mediated inflammatory response by engaging olfactory receptor family 5 subfamily M member 11 (OR5M11), a host receptor previously shown to interact with Adh. Furthermore, OR5M11 contributes to the Adh-activated inflammatory response by promoting mitochondrial DNA release. Taken together, our results provide new insights into the pathogenesis of A. pleuropneumoniae, particularly regarding NLRP3-mediated inflammatory pathology.</p>","PeriodicalId":23658,"journal":{"name":"Veterinary Research","volume":"57 1","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13633639/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149115320","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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":"Rethinking Mycoplasma hyopneumoniae adhesion: a glycocalyx-mediated infectious niche model in porcine respiratory infection.","authors":"Yuan Zhao, Anxiong Huang, Xingchi Kan, Wei Wang, Suhua Guan, Xiaochun Tang, Guoqing Shao","doi":"10.1186/s13567-026-01836-5","DOIUrl":"https://doi.org/10.1186/s13567-026-01836-5","url":null,"abstract":"<p><p>Mycoplasma hyopneumoniae (Mhp) is the primary etiological agent of porcine enzootic pneumonia and establishes infection through close association with the respiratory ciliated epithelium. Classical models of Mhp colonization have focused mainly on specific interactions between adhesins, particularly P97, and ciliary receptors. Although this framework has provided important insights into ciliary attachment, increasing evidence indicates that Mhp adhesion involves multiple surface proteins and host ligands, including sulfated glycosaminoglycans (GAGs), fibronectin, plasminogen (Plg) and extracellular actin. In this review, we synthesize current evidence and propose a glycocalyx-mediated infectious niche framework for early Mhp colonization. Within this framework, sulfated glycans within the respiratory glycocalyx may contribute to bacterial positioning at the airway interface, while multiligand adhesin interactions may contribute to attachment and Plg-binding surface proteins may facilitate host-factor recruitment. Among these interactions, plasminogen recruitment provides a potential link between adhesion and local interface modification, including possible extracellular matrix remodeling and epithelial injury. Other processes, including potential GAG-mediated local retention, host glycan-dependent variation in attachment and glycocalyx remodeling, remain hypotheses requiring further validation. By distinguishing experimentally supported interactions from mechanistic inferences, this review presents Mhp colonization as a dynamic host-pathogen interface process rather than a simple adhesin-receptor event. This framework provides a basis for future investigation of early colonization mechanisms and anti-adhesion strategies in porcine enzootic pneumonia.</p>","PeriodicalId":23658,"journal":{"name":"Veterinary Research","volume":"57 1","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13632039/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149115504","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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":"Development of a cross-protective subunit cocktail vaccine against diverse serotypes of Glaesserella parasuis infection in pigs.","authors":"Fengyang Li, Yan Gong, Ziheng Li, Zhen Wang, Zengshuai Wu, Di Zhang, Peng Zhang, Zhichao Lu, Hong Chu, Kaixin Zhang, Diansong Li, Na Li, Liancheng Lei","doi":"10.1186/s13567-026-01846-3","DOIUrl":"10.1186/s13567-026-01846-3","url":null,"abstract":"<p><p>Glässer's disease, caused by Glaesserella parasuis (GPS), causes substantial economic losses in the swine industry worldwide. This situation is largely attributable to the poor cross-protective efficacy of currently available vaccines. In this study, a multi-antigen cocktail subunit vaccine against GPS infection was developed. In silico antigenicity analysis, the immunoprotective efficacy, and antibody titers of 14 GPS antigens were assessed in a murine model. Finally, VacJ, PtsG, and GAPDH were identified as the component of the cocktail vaccine, with Gel-01 as the optimal adjuvant. Immunization of the cocktail vaccine induced robust humoral and cellular immune responses. The vaccine conferred effective cross-protection against lethal-dose GPS4 and GPS5 infections in mice. As supported by a pilot study, it also demonstrated favorable immunoprotective efficacy against GPS infection in piglets. Furthermore, immune sera from vaccinated mice significantly inhibited the growth of GPS4 and GPS5. Overall, these results suggested that the subunit cocktail vaccine established in this study exhibits great potential for preventing GPS infection under experimental conditions, and further large‑scale pig trials are still required to validate its practical applicability in field production.</p>","PeriodicalId":23658,"journal":{"name":"Veterinary Research","volume":"57 1","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13617811/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149070068","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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":"Recombinant GI-19 infectious bronchitis virus induction of humoral immunosuppression with reduced HI antibody response following Newcastle disease virus vaccination and bursal cell apoptosis.","authors":"Chenyan Wang, Weijia Zhang, Bo Hou","doi":"10.1186/s13567-026-01839-2","DOIUrl":"10.1186/s13567-026-01839-2","url":null,"abstract":"<p><p>Pathological changes and viral presence in the bursa of Fabricius (BF) have been reported, but the immunosuppression of infectious bronchitis virus (IBV) remains poorly characterized. Here, we systematically evaluated the pathogenicity of two GI-19 lineage IBV isolates, CK/CH/FJ-B3/2023 (bursal origin) and CK/CH/FJ-T5/2023 (tracheal origin), in 7-day-old specific pathogen-free (SPF) chicks, including further assessments of serum cytokines and the bursal apoptosis. We further assessed the impacts of these two IBV isolates on the Newcastle disease virus (NDV) inactivated vaccine-induced hemagglutination inhibition (HI) antibody response. This study reveals that both GI-19 lineage IBV isolates, which originated from the recombination of the 4/91 vaccine strain, exhibit bursa-tropism, inducing bursal pathological atrophy, prolonged viral detection [up to 35 days post-infection (dpi)] and delayed seroconversion until 14 dpi. Notably, IBV infection induces humoral immunosuppression in SPF chickens, evidenced by a ≥ 1log₂ reduction in NDV-HI antibody titers at 14 and 28 dpi, with antibody production recovering to normal levels by 35 dpi. This is accompanied by a sustained systemic proinflammatory response characterized by persistent upregulation of tumor necrosis factor-α (TNF-α), interleukin 1β (IL-1β), IL-6, and interferon-gamma (IFN-γ) in the serum of infected chicks up to 28 dpi. Early-onset bursal apoptosis was detected as early as 1 dpi, with the bursal apoptosis index significantly higher than that of the negative control throughout the observation period. These findings highlight the humoral immunosuppression induced by IBV variants. Further characterization of IBV types is warranted to elucidate IBV immunosuppressive mechanisms.</p>","PeriodicalId":23658,"journal":{"name":"Veterinary Research","volume":"57 1","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13602560/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149040799","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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":"Effect of Brucella effector protein BtpB regulating apoptosis by targeting host protein YWHAZ.","authors":"Lei Zhang, Yuxin Lv, Jingjing Chen, Yueting Wang, Yumeng Zhou, Yuxin Sun, Jingbo Gao, Yuqi Wang, Huan Zhang, Zeliang Chen","doi":"10.1186/s13567-026-01840-9","DOIUrl":"10.1186/s13567-026-01840-9","url":null,"abstract":"<p><p>Brucella is a successful intracellular bacteria, regulating various physiological activities within host cells by secreting multiple virulence factors. However, the specific molecular mechanisms underlying these processes remain unclear. Through interactions with host proteins, Brucella can influence cellular physiological processes to evade immune responses and enhance the bacteria survival and reproductive abilities. The type IV secretion system (T4SS) of Brucella plays a significant role in the process of Brucella infecting cells. This study revealed the interaction between BtpB and YWHAZ (14-3-3ζ) by analyzing the interaction network of 112 host proteins interacting with Brucella effector protein BtpB. Furthermore, we discovered that BtpB regulates the expression of YWHAZ protein and the deletion of its TIR domain abolishes this interaction as well as the effect on YWHAZ protein expression. Moreover, BtpB activates pro-apoptotic markers leading to apoptosis induction in cells. Our results provide mechanistic evidence that BtpB-dependent apoptosis regulation is contingent upon interaction with YWHAZ, and further characterize YWHAZ as a host factor governing Brucella's intracellular survival capacity. This study provides valuable understanding of the immune response mechanism against intracellular bacterial infections in hosts and offers a theoretical basis for future prevention and treatment strategies for Brucellosis.</p>","PeriodicalId":23658,"journal":{"name":"Veterinary Research","volume":"57 1","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13602538/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149040756","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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":"SAMSN1 restricts Japanese encephalitis virus replication by recruiting TRIM21 to degrade viral proteins and activate the interferon pathway.","authors":"Chen Wang, Wenzhen Qin, Xingya Wang, Xinyu Yang, Wu Tong, Hai Yu, Guangzhi Tong, Tongling Shan, Ning Kong, GuangXu Xing, Hao Zheng","doi":"10.1186/s13567-026-01822-x","DOIUrl":"10.1186/s13567-026-01822-x","url":null,"abstract":"<p><p>Japanese encephalitis virus (JEV), a zoonotic mosquito-transmitted flavivirus, induces human encephalitis and swine reproductive diseases. No antiviral drugs or treatments exist for flavivirus infections, which cause severe symptoms. Even though some host proteins can suppress flavivirus proliferation, the virus can inhibit this antiviral effect. This study identified a host protein SAMSN1 (SAM domain, SH3 domain, and nuclear localization signal 1; also referred to as HACS1, SLY2, and NASH1) having antiviral activity during JEV replication. SAMSN1 was upregulated during JEV infection. The expression of SAMSN1 inhibits JEV replication by binding and degrading JEV-encoded nonstructural proteins (NS1, NS5) through the proteasome and the SAMSN1-TRIM21-p62 autophagy protein degradation pathways. SAMSN1 induced expression of type I interferon through the RIG-I/MyD88-TBK1-IRF3 axis in the JEV infection process. Current findings reveal a novel role of SAMSN1 in inhibiting JEV replication and proliferation, through viral protein degradation and interferon pathway upregulation.</p>","PeriodicalId":23658,"journal":{"name":"Veterinary Research","volume":"57 1","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13595537/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149026040","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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":"Mapping of three novel linear B-cell epitopes on the VP7 protein of epizootic hemorrhagic disease virus with monoclonal antibodies.","authors":"Xinbing Hu, Yunru Zhong, Yingjuan He, Mingxin Zhang, Fanhua Meng, Yu Zhang, Zhancheng Tian, Guiquan Guan, Jijun He, Youjun Shang, Jun Ai, Junzheng Du","doi":"10.1186/s13567-026-01842-7","DOIUrl":"10.1186/s13567-026-01842-7","url":null,"abstract":"<p><p>Epizootic hemorrhagic disease virus (EHDV) is an important Orbivirus transmitted by culicoides midges. EHDV poses a significant threat to ruminant production worldwide. The VP7 protein is a highly conserved, group-specific antigen of EHDV, which serves as a key target for serological diagnosis. In this study, the recombinant VP7 (r-VP7) protein of EHDV-1 was expressed in an Escherichia coli expression system and used to immunize BALB/c mice. Four hybridoma cell lines secreting monoclonal antibodies (mAbs) against VP7 were successfully generated by the hybridoma technique, and named 5D1, 6A7, 7B11, and 7C4. Indirect ELISA, western blot analysis, and immunofluorescence assays demonstrated that all four mAbs specifically recognized both the r-VP7 protein and the native VP7 protein in EHDV-1-infected BHK-21 cells, with favorable reactivity and specificity. The VP7 protein was progressively truncated and expressed as a series of GST fusion proteins, and the linear B-cell epitopes recognized by these mAbs were precisely identified by western blotting. The results showed that 5D1 and 7B11 recognized the epitope ⁸³DYIQNLATIGVLATPEI⁹⁹, 7C4 recognized ¹²¹PDRQPFGYFL¹³⁰, and 6A7 recognized ²²⁹APVNVNNPGQ²³⁸. Sequence alignment and cross-reactivity assays revealed that the three epitopes were highly conserved among EHDV serotypes and showed no cross-reactivity with the VP7 proteins of African horse sickness virus (AHSV) or bluetongue virus (BTV). Three-dimensional structural analysis indicated that all three epitopes were exposed on the surface of the VP7 trimer and were located in distinct structural domains. In summary, this study successfully generated four specific mAbs against the EHDV VP7 protein and identified three novel linear B-cell epitopes, providing a foundation for the development of specific EHDV serological diagnostic methods and epitope-based vaccines.</p>","PeriodicalId":23658,"journal":{"name":"Veterinary Research","volume":"57 1","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13589380/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149008590","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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":"Bovine viral diarrhea virus (BVDV) relies on cellular lipid droplet biogenesis and lipolysis to provide energy for viral replication.","authors":"Xiaoran Xiong, Yi Liu, Yaohong Zhu, Jiufeng Wang, Guiyan Yang","doi":"10.1186/s13567-026-01834-7","DOIUrl":"10.1186/s13567-026-01834-7","url":null,"abstract":"<p><p>Bovine viral diarrhea virus (BVDV), one of the most important viral pathogens in cattle, causes serious economic losses due to immunosuppression and persistent infections. Previous studies have shown a tight connection between virus infection and lipid metabolism, particularly in the formation and degradation of lipid droplets (LDs). However, the pathogenic mechanism of BVDV infection and the molecular mechanisms by which viral proteins reprogram lipid metabolism remain unclear. We found that BVDV increased cellular LD accumulation by enhancing the production of new lipids, accelerating exogenous fatty acid uptake, and elevating diacylglycerol acyltransferase (DGAT)-dependent esterification of fatty acids (FAs). The generated LDs subsequently release free fatty acids (FFAs) via adipose triglyceride lipase/hormone-sensitive lipase (ATGL/HSL)-dependent lipolysis. This lipolysis-dependent release of FFAs is accelerated and transferred to mitochondria for oxidation by increasing contact between LDs and mitochondria, thereby promoting viral replication. Furthermore, BVDV core protein targets the surface of LDs, increasing and recruiting fatty acid synthase (FASN) and ATGL to promote LD mobilization. Meanwhile, the core protein interacts with mitochondria, linking mitochondria to LDs and facilitating the release of FAs for efficient fatty acid oxidation. Collectively, this study demonstrates that the BVDV core protein regulates cellular lipid metabolism to support BVDV replication, contributing to understanding the pathogenetic mechanisms by which BVDV interacts with host cells.</p>","PeriodicalId":23658,"journal":{"name":"Veterinary Research","volume":"57 1","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13589865/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149008655","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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":"Mechanisms of antibody-dependent enhancement and its research progress in animal coronaviruses.","authors":"Zhiding Zhou, Yueyue Liu, Meilin Yang, Cunyi Qiu, Jing Xia, Yong Huang, Yefei Zhou","doi":"10.1186/s13567-026-01837-4","DOIUrl":"10.1186/s13567-026-01837-4","url":null,"abstract":"<p><p>Animal coronaviruses are associated with serious diseases in livestock and poultry, resulting in substantial economic losses worldwide. Antibody-dependent enhancement (ADE) is a phenomenon whereby pre‑existing pathogen specific antibodies may paradoxically exacerbate viral infections. In this review, we synthesize current classifications of ADE mechanisms, presenting a unified framework comprising two major categories subdivided into five distinct mechanistic subsets. Given the limited research on ADE in animal coronaviruses, we use SARS‑CoV‑2 as a case study to explore five potential ADE mechanisms associated with coronavirus infection. This review aims to provide a valuable reference for elucidating ADE mechanisms in animal coronaviruses.</p>","PeriodicalId":23658,"journal":{"name":"Veterinary Research","volume":"57 1","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13580011/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148983586","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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":"From immature to mature epithelium: unveiling structural dynamics and transcriptional programs in rainbow trout intestinal barrier.","authors":"Andrea Talamilla-Espinoza, Francisca Vera-Tamargo, Mario Caruffo, Miltha Hidalgo, Daniela Ortiz, Leonardo Rodríguez, Dinka Mandakovic, Ana Riveros, Omar Porras, Rodrigo Pulgar","doi":"10.1186/s13567-026-01766-2","DOIUrl":"10.1186/s13567-026-01766-2","url":null,"abstract":"<p><p>The intestinal epithelium is crucial for nutrient absorption, immune defense, and barrier function in farmed fish. However, the molecular mechanisms underlying its development and maturation in salmonids remain poorly characterized, hindering our ability to address pervasive gut health challenges in aquaculture. In this study, we use the RTgutGC cell line to implement an epithelial maturation model with the aim of characterizing the global transcriptional program in rainbow trout (Oncorhynchus mykiss). We evaluated in vitro culture conditions to generate a polarized epithelial barrier with high transepithelial electrical resistance (TEER = 75.8 Ω × cm²), low permeability (6.2 × 10^-6 cm/s), and well-defined apical specializations, including microvilli-like structures and clusters of these structures (brush border). Comparative transcriptomic profiling between immature (7 days post-seeding, dps) and mature (28 dps) epithelia revealed 3,817 differentially expressed genes (DEGs). Functional enrichment analysis showed that maturation was characterized by the downregulation of proliferative and ribosomal pathways and the concerted upregulation of processes critical for barrier function, including transmembrane transport, proteolysis, cell adhesion, extracellular matrix organization, and tight junction assembly. We identified a core set of 60 genes indicators of epithelial maturation, encompassing solute transporters (slc26a6, slc43a2), tight junction proteins (tjp1, cldn1, cldn3, cldn5, cldn18, among others), and structural components essential for microvilli formation and polarization (cdhr5b, pard6a). By integrating ultrastructural, functional, and transcriptomic data, this study established a framework for future mechanistic investigations into gut development and maturation in vitro. This set of mature epithelium indicators has diverse applications, such as the design of nutritional and pharmacological interventions to improve gut health and resilience in farmed fish.</p>","PeriodicalId":23658,"journal":{"name":"Veterinary Research","volume":"57 1","pages":""},"PeriodicalIF":3.8,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13576363/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148978169","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}