Veterinary microbiology最新文献

{"title":"ZCCHC3 inhibits PEDV proliferation by degrading nuclear coat proteins via the proteasome pathway","authors":"Zuyao Zhang ,&nbsp;Shuangyang Wang ,&nbsp;Huihui Sun ,&nbsp;Jie Li ,&nbsp;Jun Wang ,&nbsp;Yangfan Li ,&nbsp;Haichen Lin ,&nbsp;Xuan Wang ,&nbsp;Ruimin Bi ,&nbsp;Zongyi Bo ,&nbsp;Haixiao Shen ,&nbsp;Liang Li ,&nbsp;Pei Sun","doi":"10.1016/j.vetmic.2025.110449","DOIUrl":"10.1016/j.vetmic.2025.110449","url":null,"abstract":"<div><div>Porcine epidemic diarrhea virus (PEDV) infection in pigs is characterized by vomiting, dehydration, and diarrhoea. The structural proteins of PEDV play crucial roles in viral entry, release, assembly, outgrowth, and host immune regulation. Similar to other viruses, PEDV primarily relies on host cellular mechanisms for productive infection. However, the host factors associated with PEDV infection remain undefined. Therefore, an in-depth understanding of the pathogenic mechanisms of PEDV is essential for comprehending this disease. Zinc-containing finger CCHC-type protein 3 (ZCCHC3) is an antiviral factor known to interact with RIG-I and cGAS, inhibiting the replication of pseudorabies virus (PRV). In this study, we investigated the role of porcine ZCCHC3 in PEDV proliferation. We first demonstrated that the expression of ZCCHC3 in LLC-PK1 cells is downregulated upon PEDV infection. Overexpression of ZCCHC3 inhibited PEDV replication, whereas knockdown of ZCCHC3 increased viral titer and N protein levels. Further studies revealed that ZCCHC3 interacts and co-localizes with N proteins, and that ZCCHC3-mediated antiviral effects depend on its zinc finger protease activity. Taken together, these findings provide valuable insights into the role of ZCCHC3 in PEDV proliferation and enhance our understanding of host-virus interactions.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"304 ","pages":"Article 110449"},"PeriodicalIF":2.4,"publicationDate":"2025-03-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143592363","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to \"African swine fever virus maintains de novo global cellular protein synthesis and inhibits stress granules formation via dephosphorylating eIF2α\" [Vet. Microbiol. 290 (2024) 109988].","authors":"Han Gao, Xiaopeng Gao, Xing Liu, Yizhuo Luo, Jianhao Zhong, Jing Liu, Luling Yan, Heng Wang, Lang Gong, Guihong Zhang, Zezhong Zheng, Yankuo Sun","doi":"10.1016/j.vetmic.2025.110458","DOIUrl":"https://doi.org/10.1016/j.vetmic.2025.110458","url":null,"abstract":"","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":" ","pages":"110458"},"PeriodicalIF":2.4,"publicationDate":"2025-03-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143587295","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The depletion of TFAM and p-β-catenin(S552) in mitochondria in response to BoAHV-1 productive infection leads to decreased mitochondrial biogenesis","authors":"Jiayu Lin ,&nbsp;Xiaotian Fu ,&nbsp;Xuan Li ,&nbsp;Xiuyan Ding ,&nbsp;Shitao Li ,&nbsp;Filomena Fiorito ,&nbsp;Liqian Zhu","doi":"10.1016/j.vetmic.2025.110454","DOIUrl":"10.1016/j.vetmic.2025.110454","url":null,"abstract":"<div><div>Varicellovirus bovinealpha (BoAHV) types 1(BoAHV-1) is one of the most significant viruses affecting cattle, causing substantial economic losses in the global cattle industry. Virus productive infection in cell cultures leads to mitochondrial dysfunction, resulting in the overproduction of reactive oxygen species (ROS), which act as inflammatory mediators and exert cytotoxic effects. But the underlying mechanisms remain poorly understood. Mitochondrial transcription factor A (TFAM) is a critical transcriptional activator of the mitochondrial DNA and plays a vital role in mitochondrial biogenesis. In this study, we report that virus acute infection in calves (at 4 days post-infection) increases TFAM protein expression and its accumulation in the peri-nuclear region in a subset of trigeminal ganglia (TG) neurons. Similarly, virus productive infection at later stages in MDBK cells also leads to increased TFAM protein expression and its accumulation in the nucleus. Using TFAM-specific siRNAs, we revealed that TFAM plays a significant role in BoAHV-1 productive infection. Consistent with decreased mitochondrial biogenesis, TFAM protein accumulation in mitochondria was significantly reduced following viral infection, which is corroborated by the reduced accumulation of TOM70 and Tim44 proteins in mitochondria. These proteins are key components of the mitochondrial membrane transport system that facilitates the translocation of TFAM into mitochondria. Interestingly, we found that a subset of β-catenin resides in mitochondria, and viral infection decreases the accumulation of transcriptionally active β-catenin, p-β-catenin(S552), in mitochondria. This may contribute to decreased mitochondrial biogenesis, as the β-catenin-specific inhibitor iCRT14 reduces the protein expression of Cytb, a key regulator of mitochondrial biosynthesis. Collectively, we suggest that the depletion of both TFAM and p-β-catenin(S552) in mitochondria may contribute to the mitochondrial dysfunction induced by BoAHV-1 productive infection.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"304 ","pages":"Article 110454"},"PeriodicalIF":2.4,"publicationDate":"2025-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143592364","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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":"Modification of the splice acceptor in CD163 exon 7 of pigs is insufficient to confer resistance to PRRSV","authors":"Kassandra Durazo-Martínez ,&nbsp;Jayeshbhai Chaudhari ,&nbsp;Luke M. Sherry ,&nbsp;Dennis A. Webster ,&nbsp;Kyra Martins ,&nbsp;Jonathan R. Bostrom ,&nbsp;Daniel F. Carlson ,&nbsp;Tad S. Sonstegard ,&nbsp;Hiep L.X. Vu","doi":"10.1016/j.vetmic.2025.110450","DOIUrl":"10.1016/j.vetmic.2025.110450","url":null,"abstract":"<div><div>CD163 is the primary receptor for PRRSV, and its SRCR5 domain, encoded by exon 7, is crucial for supporting PRRSV infection. Previous studies have used CRISPR/Cas9 technology to remove exon 7 from the host genome, and the edited pigs were completely resistant to PRRSV infection. In this study, we used CRISPR/Cas9 technology mimicking an adenine base editor (ABE) to edit the splice acceptor site of exon 7, rendering it nonfunctional. This alteration was intended to cause exon 6 to join directly to exon 8 during mRNA processing, resulting in a mature mRNA transcript that lacks exon 7, which encodes the SRCR5 domain. Piglets carrying the exon 7 splice site modification (CD163Ex7-ABE) were successfully generated. However, these pigs remained fully susceptible to infection with a PRRSV-2 isolate. Analysis of CD163 mRNA from the CD163Ex7-ABE pigs revealed that they predominantly expressed a mature CD163 mRNA lacking exon 7. However, due to cryptic splice sites, two additional mRNA isoforms were expressed, including an in-frame variant containing all of exon 7 and an extra 48 base pairs. This likely resulted in the expression of a full-length CD163 with a 16-amino-acid insertion upstream of the SRCR5 domain, which was sufficient to render the animals susceptible to PRRSV. Overall, our results demonstrate that merely modifying the splice acceptor site of CD163 exon 7 is not sufficient to generate PRRSV-resistant pigs.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"304 ","pages":"Article 110450"},"PeriodicalIF":2.4,"publicationDate":"2025-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143592365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"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":"VAPA suppresses BEFV and VSV-induced type I IFNs signaling response by targeting JAK1 for NEDD4-mediated ubiquitin-proteasome degradation","authors":"Tianhua Chen ,&nbsp;Xingyu Li ,&nbsp;Peili Hou,&nbsp;Hongbin He,&nbsp;Hongmei Wang","doi":"10.1016/j.vetmic.2025.110456","DOIUrl":"10.1016/j.vetmic.2025.110456","url":null,"abstract":"<div><div>VAMP-associated protein A (VAPA) binds to various proteins involved in multiple cellular processes, however, its role in the regulation of type I interferons (IFN-I) signaling has not been elucidated. In this study, we demonstrate that VAPA negatively regulates the IFN-I signaling during bovine epidemic fever virus (BEFV) and vesicular stomatitis virus (VSV) infection. Upon treatment with IFN-β, VAPA negatively regulates the JAK-STAT signaling pathway. Further studies show that VAPA inhibits the IFN-I signaling by promoting the degradation of JAK1 through the ubiquitin-proteasome system during BEFV and VSV infection. Mechanistically, VAPA facilitates the interaction between the E3 ubiquitin ligase NEDD4 and JAK1, thereby enhancing the ubiquitination and subsequent degradation of JAK1. Furthermore, viral titers are markedly reduced, and the promoting effect of VAPA on VSV or BEFV replication is attenuated in NEDD4-deficient cells. Taken together, our findings reveal a novel role for VAPA in negatively regulating the IFN-I signaling response and provide a molecular basis for the design of targeted antiviral agents.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"304 ","pages":"Article 110456"},"PeriodicalIF":2.4,"publicationDate":"2025-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143609914","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"HnRNPM inhibits pseudorabies virus replication by inducing apoptosis in infected cells","authors":"Xiaoxiao Zhao ,&nbsp;Yan Qiao ,&nbsp;Songjie Fan ,&nbsp;Xiaotian Chang ,&nbsp;Jiafu Zhao ,&nbsp;Kai Zhong ,&nbsp;Yingqian Han ,&nbsp;Heshui Zhu ,&nbsp;Chao Zhang","doi":"10.1016/j.vetmic.2025.110455","DOIUrl":"10.1016/j.vetmic.2025.110455","url":null,"abstract":"<div><div>Heterogeneous nuclear ribonucleoproteins (hnRNPs) are a family of RNA-binding proteins that play crucial roles in RNA processing, transcriptional regulation, nucleocytoplasmic transport, and apoptosis. As a member of the hnRNP family, heterogeneous nuclear ribonucleoprotein M (hnRNPM) has been implicated in diverse cellular processes, including the regulation of tumor-associated gene expression, promotion of angiogenesis, enhancement of tumor cell invasion and metastasis, and modulation of RNA virus replication. However, the interaction between hnRNPM and pseudorabies virus (PRV) remains unexplored. In this study, we demonstrated that hnRNPM overexpression in PK15 and 3D4/21 cells significantly inhibited PRV replication, whereas hnRNPM knockdown enhanced viral replication. Although PRV infection did not alter total cellular hnRNPM levels, it induced the nuclear translocation of hnRNPM. Mechanistically, hnRNPM promoted apoptosis in PRV-infected cells by upregulating the expression of cleaved caspase-3, −6, and −7, as well as Bax, while downregulating Bcl-2. This apoptosis induction consequently suppressed PRV replication. Furthermore, hnRNPM was found to colocalize with caspase-6. Our findings reveal that hnRNPM inhibits PRV replication by inducing apoptosis in infected cells. These results not only enhance our understanding of PRV-host interactions but also highlight hnRNPM as a promising therapeutic target for the development of antiviral strategies against PRV.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"304 ","pages":"Article 110455"},"PeriodicalIF":2.4,"publicationDate":"2025-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143579363","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Porcine GM-CSF and APS as a novel complex immunostimulant improves the immune effect of pseudorabies inactivated vaccine","authors":"Peng Chen ,&nbsp;Wuchao Zhang ,&nbsp;Yanan Cui ,&nbsp;Maoyuan Sun ,&nbsp;Xiaofeng Dong ,&nbsp;Wei Li ,&nbsp;Mandi Liu ,&nbsp;Baishi Lei ,&nbsp;Yu Lu ,&nbsp;Wanzhe Yuan ,&nbsp;Kuan Zhao","doi":"10.1016/j.vetmic.2025.110453","DOIUrl":"10.1016/j.vetmic.2025.110453","url":null,"abstract":"<div><div>Currently, pseudorabies (PR) is mainly controlled with attenuated and inactivated vaccines. In the case of inactivated vaccines, immunostimulants play a crucial role in triggering the host immune response. In this study, granulocyte-macrophage colony-stimulating factor (GM-CSF) and astragalus polysaccharide (APS) were investigated as a novel complex immunostimulant in inactivated PR vaccine. The findings indicated that neither porcine GM-CSF (pGM-CSF) nor APS exhibited any cytotoxic effect on cells. In addition, the PR vaccine+pGM-CSF+APS group exhibited higher levels of PRV-specific gB and neutralizing antibodies. Moreover, the group treated with pGM-CSF+APS immunostimulants demonstrated a notable increase in the production of IL-4, IL-10, IL-2, IFN-γ. After PRV challenge, the PR vaccine with pGM-CSF and APS alleviated clinical symptoms and reduced mortality. Additionally, the complex immunostimulant group showed a lower viral DNA copy number in various tissues compared to the PR vaccine alone group, as well as the groups treated with PR vaccine+pGM-CSF and PR vaccine+APS. Moreover, mice challenged with PRV in the PR Vaccine+pGM-CSF+APS group reduced substantial tissue lesions than other groups. These results demonstrate the potential of pGM-CSF and APS when used together as complex immunostimulant to enhance both humoral and cellular immune responses to inactivated vaccines, providing novel perspectives for the further development of immunostimulants.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"304 ","pages":"Article 110453"},"PeriodicalIF":2.4,"publicationDate":"2025-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143562318","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Subunit vaccine of PCV3 capsid protein produced by sf9 cells with double knockout of Caspase-1 and Dronc induces strong immune response in mice","authors":"Shuo Li ,&nbsp;Ruihong Guo ,&nbsp;Yinxiang Fang ,&nbsp;Chunhong Zhang ,&nbsp;Linyu Jiang ,&nbsp;Weixin Jia ,&nbsp;Zhangyong Ning","doi":"10.1016/j.vetmic.2025.110452","DOIUrl":"10.1016/j.vetmic.2025.110452","url":null,"abstract":"<div><div>Porcine circovirus type 3 (PCV3) associated with multisystemic clinicopathological diseases in swine herds has caused economic losses and there is no available commercial vaccine. Production of PCV3 capsid protein (Cap) by <em>Spodoptera frugiperda 9</em> (sf9) cells using baculovirus expression vector system (BEVS) is a valid strategy to develop vaccines. Here, we report that subunit vaccine of PCV3 produced by sf9 cells with double knockout of <em>Caspase-1</em> and <em>Dronc</em> genes induces strong immune response in mice. Three kinds of knockout sf9 cells aimed at <em>Caspase-1</em> gene, <em>Dronc</em> gene and both genes were successfully generated by clustered regularly interspaced short palindromic repeats-associated protein 9 (CRISPR-Cas9) system, and sequence analysis confirmed this. The anti-apoptosis ability of three kinds of knockout sf9 cells was assessed, and double knockout sf9 cells are the best. The expression of PCV3 Cap was enhanced in double knockout sf9 cells compared to wild type sf9 cells, and subunit vaccines were produced by PCV3 Cap expressed from double knockout sf9 cells and wild type cells, respectively. Results of immunological experiment in mice showed subunit vaccine of PCV3 Cap from double knockout sf9 cells induces higher level of serum antibody, stimulates lymphocyte proliferation and enhances expression of IL-2, IFN-γ, IL-4 and IL-10 compared to wild type cells. These results present knockout sf9 cells to enhance the expression of protein in BEVS, and provide a technical platform for vaccine development of PCV3.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"304 ","pages":"Article 110452"},"PeriodicalIF":2.4,"publicationDate":"2025-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143562319","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Constructions and immunogenicity evaluations of two porcine epdemic diarrhea virus-like particle vaccines","authors":"Hong Xu ,&nbsp;Mengdi Yang ,&nbsp;Shiyu Liu ,&nbsp;Fangyuan Zheng ,&nbsp;YuPeng Li ,&nbsp;Yunchuan Li ,&nbsp;Chuanhong Wang ,&nbsp;Jiali Qian ,&nbsp;Yongxiang Zhao ,&nbsp;Shanshan Yang ,&nbsp;Min Sun ,&nbsp;Xu Song ,&nbsp;Rongli Guo ,&nbsp;Jinzhu Zhou ,&nbsp;Baochao Fan ,&nbsp;Bin Li","doi":"10.1016/j.vetmic.2025.110451","DOIUrl":"10.1016/j.vetmic.2025.110451","url":null,"abstract":"<div><div>Porcine epidemic diarrhea virus (PEDV), a swine enteropathogenic coronavirus, causing acute diarrhea, dehydration, and up to 100 % mortality in neonatal suckling piglets, leading to huge economic losses in the global swine industry. Vaccination remains the most promising and effective way to prevent and control PEDV. In this study, we produced PEDV virus-like particles (VLPs) composed of S, M, and E proteins with a baculovirus expression system and a mammalian expression system. The S, M, and E proteins were effectively expressed and successfully assembled into VLPs. Subsequently, S subunits and commercially inactivated vaccines were selected and compared with two VLPs vaccines for immune efficacy through mouse immunization. The results showed that both VLPs induced higher levels of IgG, IgA, and neutralizing antibody titers, lymphocyte proliferation indexes and T, B cell ratios. Compared with the baculovirus VLPs, the mammalian VLPs exhibited better effects in inducing neutralizing antibodies, lymphocyte proliferations, and IFN-γ. These data indicated that the PEDV VLPs vaccine constructed using the mammalian expression system has better immune efficacy and has the potential to serve as a novel PEDV vaccine.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"303 ","pages":"Article 110451"},"PeriodicalIF":2.4,"publicationDate":"2025-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143548800","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Extracellular vesicles engineered to directly target encephalomyocarditis virus ameliorates multi-organ viremia in a lethal infection model","authors":"Jiayu Yue ,&nbsp;Yanmei Yang ,&nbsp;Adi Idris ,&nbsp;Wenjing Jin ,&nbsp;Yaxin Zhang ,&nbsp;Yongfang Chen ,&nbsp;Xiangrong Li ,&nbsp;Huixia Li ,&nbsp;Shasha Li ,&nbsp;Yanqiao Wen ,&nbsp;Ruofei Feng ,&nbsp;Jingying Xie","doi":"10.1016/j.vetmic.2025.110448","DOIUrl":"10.1016/j.vetmic.2025.110448","url":null,"abstract":"<div><div>The outbreak and prevalence of encephalomyocarditis virus (EMCV) causes significant global mortality and morbidity to the pig industry. Though the current and most effective approach to control EMCV outbreak are done through inactivated vaccines, we have yet to see an effective antiviral agent that directly targets EMCV. Here, we present a molecular therapy consisting of extracellular vesicles (EVs) decorated with EMCV-specific single-chain variable fragment (scFv), engineered on the external loop of the EVS transmembrane domain CD63. These EMCV-scFv enriched EVs directly neutralizes infectious EMCV, thereby inhibiting viral proliferation <em>in vitro</em>. Importantly, we demonstrate that systemic delivery of these EVs reduced multi-organ viremia and clinically rescued EMCV infected mice <em>in vivo</em>. This is the first demonstration of the use of direct acting molecularly engineered EVs to target EMCV infection.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"304 ","pages":"Article 110448"},"PeriodicalIF":2.4,"publicationDate":"2025-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143609915","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}