Veterinary microbiology最新文献

{"title":"Optineurin inhibits IBDV replication via interacting with VP1","authors":"Zhixuan Xiong ,&nbsp;Qinghua Zeng ,&nbsp;Ying Hu ,&nbsp;Chongde Lai ,&nbsp;Huansheng Wu","doi":"10.1016/j.vetmic.2024.110261","DOIUrl":"10.1016/j.vetmic.2024.110261","url":null,"abstract":"<div><div>Avibirnavirus, specifically Infectious Bursal Disease Virus (IBDV), is a highly contagious pathogen that causes significant economic losses in the poultry industry. The polymerase protein VP1 of IBDV is critical to the viral life cycle, facilitating the synthesis of viral mRNA and the genome. Previous studies have suggested that various host factors influence the regulation of IBDV polymerase activity. In this study, we identified that IBDV infection induces the expression of optineurin (OPTN), a mitophagy receptor and a protein associated with amyotrophic lateral sclerosis (ALS), as well as a negative regulator of interferon I production. The induced expression of OPTN acts as a suppressor of IBDV replication, a function dependent on its ubiquitin-binding domain (UBAN). Furthermore, we demonstrated that OPTN exerts its antiviral effects through direct interactions with VP1 and VP3, which inhibit the polymerase activity of VP1 by preventing K63-linked ubiquitination of VP1. To our knowledge, this study is the first to report that OPTN, upregulated during IBDV infection, functions as a novel antiviral host factor that limits the virus's replicative capacity, offering a potential target for anti-IBDV therapeutic strategies.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"298 ","pages":"Article 110261"},"PeriodicalIF":2.4,"publicationDate":"2024-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142322892","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":"Response of Mycobacterium avium subsp. paratuberculosis isolates to reactive oxygen stress generated by treatment with copper ions","authors":"P. Steuer ,&nbsp;H.W. Barkema ,&nbsp;C. Tejeda ,&nbsp;J.M. Hernández ,&nbsp;F. Ulloa ,&nbsp;M. Salgado","doi":"10.1016/j.vetmic.2024.110251","DOIUrl":"10.1016/j.vetmic.2024.110251","url":null,"abstract":"<div><div>Copper (Cu) ions have been recognized for their efficacy in inactivating bacteria, including <em>Mycobacterium avium</em> subsp. <em>paratuberculosis</em> (MAP), the causative agent of Johne’s disease (JD) known for its resilience to unfavorable conditions. However, the response of MAP isolates isolated from cows to Cu exposure remains inadequately understood, as their responses may differ from those of laboratory-adapted reference strains. In this study, we examined the response of MAP isolates obtained from MAP-infected and affected cows to Cu ion treatment, comparing that with the response of the reference strain ATCC 19698 to the same treatment. Three MAP field isolates and the MAP reference strain were exposed to Cu ions, and their viability, protein/lipid damage, ROS production, and gene expression were evaluated in triplicate. Survival differed among isolates, with an isolate from a cow with clinical JD exhibiting increased tolerance to Cu exposure. While Cu treatment induced lipid peroxidation and ROS production across all isolates, genes associated with Cu detoxification and virulence were upregulated, particularly in the reference strain. Whole genome sequencing analysis revealed that, despite genomic similarities between field isolates and the reference strain ATCC 19698, there were differences regarding the presence/absence of genes related with certain virulence factors. Further research on Cu exposure with larger numbers of MAP isolates is needed to explain the stress-induced responses that influence MAP survival during natural infections and in challenging environments.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"298 ","pages":"Article 110251"},"PeriodicalIF":2.4,"publicationDate":"2024-09-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142376109","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":"Lumpy skin disease virus enters into host cells via dynamin-mediated endocytosis and macropinocytosis","authors":"Shasha Wang ,&nbsp;Pengyuan Cheng ,&nbsp;Ke Guo ,&nbsp;Shanhui Ren ,&nbsp;Berihun Afera Tadele ,&nbsp;Zhengji Liang ,&nbsp;Yuefeng Sun ,&nbsp;Xiangping Yin ,&nbsp;Xiangwei Wang","doi":"10.1016/j.vetmic.2024.110254","DOIUrl":"10.1016/j.vetmic.2024.110254","url":null,"abstract":"<div><div>Lumpy skin disease virus (LSDV), a ruminant poxvirus of the Capripoxvirus genus, is the etiologic agent of an economically important cattle disease categorized as a notifiable disease by the World Organization for Animal Health. However, the endocytic pathway and their regulatory molecules have not been characterized for LSDV. In the present study, specific pharmacological inhibitors were used to analyze the mechanism of LSDV entry into Mardin-Darby Bovine Kidney cell (MDBK) and bovine mammary epithelial cell (BMEC). The results showed that LSDV entered MDBK and BMEC cells depends on low-pH conditions and dynamin. However, the inhibitor of caveolae- and clathrin-mediated endocytosis cann’t inhibit LSDV entry into MDBK and BMEC cells. Furthermore, treatment with specific inhibitors demonstrated that LSDV entry into MDBK and BMEC cells via macropinocytosis depended on the Na1/H1 exchanger (NHE) but not phosphatidylinositol 3-kinase (PI3K). In addition, results demonstrated that these inhibitors inhibited LSDV entry but did not have effect on LSDV binding. Taken together, our study demonstrated that LSDV enters MDBK and BMEC cells through macropinocytosis pathway in a low-PH- and dynamin-dependent manner while independent on PI3K. Results presented in this study potentially provides insight into the entry mechanisms of LSDV, and it may facilitate the development of therapeutic interventions.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"298 ","pages":"Article 110254"},"PeriodicalIF":2.4,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142296600","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":"An effective vaccine against influenza A virus based on the matrix protein 2 (M2)","authors":"Federico A. Zuckermann ,&nbsp;Yelena V. Grinkova ,&nbsp;Robert J. Husmann ,&nbsp;Melissa Pires-Alves ,&nbsp;Suzanna Storms ,&nbsp;Wei-Yu Chen ,&nbsp;Stephen G. Sligar","doi":"10.1016/j.vetmic.2024.110245","DOIUrl":"10.1016/j.vetmic.2024.110245","url":null,"abstract":"<div><p>The ever-increasing antigenic diversity of the hemagglutinin (HA) of influenza A virus (IAV) poses a significant challenge for effective vaccine development. Notably, the matrix protein 2 (M2) is a highly conserved 97 amino acid long transmembrane tetrameric protein present in the envelope of IAV. More than 99 % of IAV strains circulating in American swine herds share the identical pandemic (pdm) isoform of M2, making it an ideal target antigen for a vaccine that could elicit broadly protective immunity. Here, using soluble nanoscale membrane assemblies termed nanodiscs (NDs), we designed this membrane mimetic nanostructures displaying full-length M2 in its natural transmembrane configuration (M2ND). Intramuscular (IM) immunization of swine with M2ND mixed with conventional emulsion adjuvant elicited M2-specific IgG antibodies in the serum that recognized influenza virions and M2-specific interferon-γ secreting cells present in the blood. Intranasal (IN) immunization with M2ND adjuvanted with a mycobacterial extract elicited M2-specific IgA in mucosal secretions that also recognized IAV. Immunization with an influenza whole inactivated virus (WIV) vaccine supplemented with a concurrent IM injection of M2ND mixed with an emulsion adjuvant increased the level of protective immunity afforded by the former against a challenge with an antigenically distinct H3N2 IAV, as exhibited by an enhanced elimination of virus from the lung. The lone IM administration of the M2ND vaccine mixed with an emulsion adjuvant provided measurable protection as evidenced by a &gt;10-fold reduction or complete elimination of the challenge virus from the lung, but it did not diminish the viral load in nasal secretions nor the extent of pneumonia that ensued after the virus challenge. In contrast, an improved formulation of the M2ND vaccine that incorporated synthetic CpG oligodeoxynucleotides (CpG-ODN) in the nanostructures administered alone, via the IN and IM routes combined, provided a significant level of protective immunity against IAV as evidenced by a decreased viral load in both the upper and lower respiratory tracts and fully eliminated the occurrence of pneumonia in 89 % of the pigs immunized with this biologic. Notably, to be effective, the M2 protein must be displayed in the ND assemblies, as shown by the observation that simply mixing M2 with empty NDs incorporating CpG-ODN (eND-CpG-ODN) did not provide protective immunity. This novel M2-based vaccine offers great promise to help increase the breadth of protection afforded by conventional WIV vaccines against the diversity of IAV in circulation and, plausibly, as a broadly protective stand-alone biologic.</p></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"298 ","pages":"Article 110245"},"PeriodicalIF":2.4,"publicationDate":"2024-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0378113524002670/pdfft?md5=f17442ba9a5b5468e40aac6d7b858f07&pid=1-s2.0-S0378113524002670-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142242412","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":"The evolution and diversity of porcine reproductive and respiratory syndrome virus in China","authors":"Lei Zhou ,&nbsp;Jun Han ,&nbsp;Hanchun Yang","doi":"10.1016/j.vetmic.2024.110252","DOIUrl":"10.1016/j.vetmic.2024.110252","url":null,"abstract":"<div><p>The porcine reproductive and respiratory syndrome virus (PRRSV) has emerged as a significant pathogen in the global pork industry since the late 1980s, causing substantial economic losses due to its high contagiousness and genetic variability. China, with its complex epidemiological landscape, has witnessed the emergence of four distinct lineages of PRRSV-2 (Lineages 1, 3, 5, and 8) and occasional occurrences of PRRSV-1. This review summarizes the historical context and epidemiological trends that have led to the diversification of PRRSV in China, discusses the evolutionary dynamics behind the establishment of diverse genetic variants, as well as the impact of recombination and modified live vaccines (MLVs) on the virus's rapid evolution. The implications for disease management, including strategies to reduce the complexity of PRRSV epidemics and improve prevention and control measures, are also suggested. Understanding the evolutionary pattern and factors contributing to PRRSV diversity is crucial for enhancing our knowledge, control capabilities, and prevention strategies, which could be integrated into swine health management practices.</p></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"298 ","pages":"Article 110252"},"PeriodicalIF":2.4,"publicationDate":"2024-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142242478","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":"Intermolecular disulfide bond of PRRSV GP5 and M facilitates VLPs secretion and cell binding","authors":"Xinnuo Lei ,&nbsp;Yifan Jiang ,&nbsp;Wanting Yu ,&nbsp;Xiuyue Chen ,&nbsp;Yiwen Qin ,&nbsp;Naidong Wang ,&nbsp;Yi Yang","doi":"10.1016/j.vetmic.2024.110249","DOIUrl":"10.1016/j.vetmic.2024.110249","url":null,"abstract":"<div><p>Porcine reproductive and respiratory syndrome virus (PRRSV), the causative agent of porcine reproductive and respiratory syndrome (PRRS), continues to significantly impact on the global swine industry. GP5 and M are the primary structural proteins of PRRSV, playing crucial roles in the processes of virus attachment, entry, assembly and budding. The co-expression of GP5 and M can result in the formation of virus-like particles (VLPs). However, the underlying mechanisms remain incompletely understood. This study investigated the role of GP5-M interaction in VLPs secretion and cell binding. VLPs were generated by co-expressing GP5 and M via recombinant baculoviruses in Sf9 cells and confirmed by transmission electron microscopy. The secretion of VLPs was modulated by the expression levels of GP5 and M. Using the BirA technique, the GP5-M interaction was confirmed in Sf9 cells. Disruption of the N-terminally intermolecular disulfide bond between GP5 and M weakened, but did not completely abolish, the interaction between the proteins, leading to reduced VLPs secretion. Notably, the absence of this intermolecular disulfide bond resulted in the loss of VLPs’ ability to bind to MARC-145 cells. In summary, our findings reveal the critical function of the intermolecular disulfide bond in GP5-M interaction, which significantly contributes to VLPs secretion and cell binding, and suggest potential interaction sites between GP5 and M.</p></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"298 ","pages":"Article 110249"},"PeriodicalIF":2.4,"publicationDate":"2024-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142173814","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":"Yak DEFB123 alleviates lung injury caused by Klebsiella pneumoniae through MAPKs signaling pathway","authors":"Nanchi Zhang ,&nbsp;Yao Zheng ,&nbsp;Yong Wei ,&nbsp;Li Wang ,&nbsp;Xiwen Chen ,&nbsp;Juan Li","doi":"10.1016/j.vetmic.2024.110248","DOIUrl":"10.1016/j.vetmic.2024.110248","url":null,"abstract":"<div><p>Beta-defensins, such as β-defensin 123 (DEFB123), are vital components of the immune system's defense against infections due to their strong antimicrobial properties and capacity for modulating the body's immunological responses. In this study, we successfully cloned and analyzed the yak DEFB123 gene sequence. Subsequently, we obtained recombinant protein DEFB123 (rDEFB123) through prokaryotic expression. Our results demonstrate that rDEFB123 effectively inhibits the growth of <em>Escherichia coli</em>, <em>Klebsiella pneumoniae</em>, and <em>Staphylococcus aureus</em>. Furthermore, rDEFB123 enhances the phagocytic activity of macrophages by regulating specific factors. In a mouse model infected with <em>Klebsiella pneumoniae</em>, the administration of rDEFB123 showed significantly lower levels of serum ALT and AST compared to the control group. Moreover, IFN-γ and IgG were significantly increased in the rDEFB123-treated groups, indicating an enhanced immune response. In the MAPKs signaling pathway of the infected mouse lungs, the expressions of JNK, TRAF2, TRAF6, MIF, and IL-1β genes were downregulated in the rDEFB123-treated groups. Moreover, the levels of p-JNK protein were significantly decreased in these groups as well. <em>Klebsiella pneumoniae</em> caused systemic infection with organ damage in mice. However, the administration of rDEFB123 suppressed the expressions of inflammatory factors, thereby mitigating organ injury and regulating the activity of apoptosis-related factors to enhance immunity. These findings provide valuable theoretical data for future exploration of the functionality and potential applications of DEFB123 in yak.</p></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"298 ","pages":"Article 110248"},"PeriodicalIF":2.4,"publicationDate":"2024-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142167846","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":"Evaluating the ability of non-tuberculous mycobacteria to induce non-specific reactions in bovine tuberculosis diagnostic tests in guinea pigs and cattle","authors":"Alberto Gomez-Buendia ,&nbsp;Javier Ortega ,&nbsp;Alberto Diez-Guerrier ,&nbsp;Aaron Rendahl ,&nbsp;Jose Luis Saez ,&nbsp;Javier Bezos ,&nbsp;Beatriz Romero ,&nbsp;Julio Alvarez","doi":"10.1016/j.vetmic.2024.110250","DOIUrl":"10.1016/j.vetmic.2024.110250","url":null,"abstract":"<div><p>Limitations in diagnostic test performance are one of the major challenges hampering the eradication of bovine tuberculosis (bTB). Non-tuberculous mycobacteria (NTM) are considered one of the main causes of non-specific reactions in the intradermal tuberculin test, the most widely used bTB diagnostic test. To determine the role of NTMs in bTB misdiagnosis in Spain, an experimental study including the NTM species most commonly found in bTB-positive animals from bTB-free farms in the country (<em>M. avium</em> subsp. <em>avium</em> (<em>Maa</em>), “<em>Mycobacterium avium</em> subsp. <em>hominissuis”</em> (<em>Mah</em>), <em>M. bourgelatii</em>, <em>M. intermedium</em>, <em>M. kansasii</em> and <em>M. nonchromogenicum</em>) was carried out on guinea pigs and cattle. First, guinea pigs were sensitized with the selected NTMs, and six weeks post-sensitization four antigen mixtures (bovine-PPD, avian-PPD, P22 and ESAT6-CFP10) were inoculated intradermally and their effect was measured 24- and 48-h post-inoculation. Larger erythematous reactions were observed in guinea pigs sensitized with <em>Mah</em>, <em>M. kansasii</em>, and <em>Maa</em>, with significant differences in the reactions measured at the bovine-PPD inoculation site for the two first bacteria compared with other NTMs. The sensitization process was repeated in cattle, and five months post-sensitization the same antigen mixtures were inoculated in the cervical region and responses were measured at 48- and 72-h post-inoculation. A significantly higher increase in the skinfold thickness measured at the bovine-PPD inoculation site was observed in calves sensitized with <em>Mah</em>, <em>Maa</em>, <em>M. intermedium</em> and <em>M. kansasii</em>. These results demonstrate that certain NTM species may play a more significant role in bTB diagnostic interferences and show that results obtained in guinea pig and bovine models do not always coincide.</p></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"298 ","pages":"Article 110250"},"PeriodicalIF":2.4,"publicationDate":"2024-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0378113524002724/pdfft?md5=3e16b4809e27f28b1b35b0d50497ccb3&pid=1-s2.0-S0378113524002724-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142167845","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":"Host restriction factor Rab11a limits Porcine deltacoronavirus invasion of cells via fusion peptide-mediated membrane fusion","authors":"Cailiang Song ,&nbsp;Hao Li ,&nbsp;Yun Han ,&nbsp;Kailu Wang ,&nbsp;Wenjun Yan ,&nbsp;Xin Yang ,&nbsp;Anyun Zhang ,&nbsp;Hongning Wang","doi":"10.1016/j.vetmic.2024.110246","DOIUrl":"10.1016/j.vetmic.2024.110246","url":null,"abstract":"<div><p>Porcine deltacoronavirus (PDCoV) poses a serious threat to pork industry and has the potential for cross-species transmission. Yet, the invasion mechanisms and host factors involved are still unknown. In the present work, using siRNA interference and co-immunoprecipitation, we identified Annexin A2 (ANXA2), Prohibitin-2 (PHB2), or Caveolin-2 (CAV2) as host factors positively regulating the internalization of PDCoV. We further found that Rab11a co-localized with PDCoV S and inhibited PDCoV internalization. Subsequently, a pseudoviral infection model (LV-PDCoV S-GFP) was constructed, and ANXA2 or CAV2 promoted PDCoV invasion by downregulating Rab11a. Our results also indicated that ANXA2, CAV2, and Rab11a interact with the S protein via S-FP, thereby regulating virus-host membrane fusion. Through LV-PDCoV S-GFP infection, we found that Rab11a may act as a host restriction factor, and it could regulate the invasion efficiency of PDCoV by adding of exogenous GTP. These findings revealed that Rab11a was an exciting target to restrict fusion of PDCoV with host cell membranes.</p></div><div><h3>Availability of data and material</h3><p>Not applicable.</p></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"298 ","pages":"Article 110246"},"PeriodicalIF":2.4,"publicationDate":"2024-09-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142150722","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":"A recombinant pseudorabies virus surface - displaying the classical swine fever E2 protein induces specific antibodies rapidly","authors":"Xinyu Zhang ,&nbsp;Hongxia Wu ,&nbsp;Tianqi Gao ,&nbsp;Yongfeng Li ,&nbsp;Dailang Zhong ,&nbsp;Mingzhi Li ,&nbsp;Shuwen Li ,&nbsp;Caoyuan Ma ,&nbsp;Assad Moon ,&nbsp;Qiang Fu ,&nbsp;Hua-Ji Qiu ,&nbsp;Yuan Sun","doi":"10.1016/j.vetmic.2024.110240","DOIUrl":"10.1016/j.vetmic.2024.110240","url":null,"abstract":"<div><p>Pseudorabies virus (PRV) and classical swine fever virus (CSFV) are both economically important pathogens threatening the pig industry in many countries. The triple-gene-deleted variant of PRV, herein referred to as rPRVTJ-delgE/gI/TK, has exhibited pronounced efficacy and safety profiles. This underscores its viability as a prospective vaccine vector. However, the generation of specific anti-E2 antibodies necessitates elevated immunization doses and extended durations when the extracellular domain of the E2 protein of CSFV is secreted via the recombinant rPRVTJ-delgE/gI/TK vector. To enhance the presentation of exogenous antigens by antigen-presenting cells (APCs), we engineered the E2 protein expressed on the surface of PRV particles in this study. The recombinant virus expressing the E2 protein with a heterogonous transmembrane domain was generated in the backbone of rPRVTJ-delgE/gI/TK and designated as rPRVTJ-UL44-E2. The <em>E2</em> gene was fused to the 3′ terminus of the <em>UL44</em> gene utilizing P2A, a self-cleaving peptide sequence. The electron microscopy showed that the E2 protein was anchored on the surface of the viral particles of rPRVTJ-delgE/gI/TK-E2. The insertion of the <em>E2</em> gene did not alter the native biological characteristics of the viral vector. Rabbits immunized with 10⁷ median tissue culture infective doses (TCID₅₀) of rPRVTJ-UL44-E2 exhibited a rapid seroconversion to anti-E2 specific antibodies within 7 days post-immunization (dpi). All the rabbits immunized with the rPRVTJ-UL44-E2 had generated antibodies specific to E2 prior to the administration of the booster immunization. However, the immunized rabbits were not protected from the CSFV C-strain challenge. Nevertheless, this strategy has notably achieved rapid induction of E2-specific non-neutralizing antibodies. These findings provide insights that the design of rPRVTJ-UL44-E2 requires optimization, thereby indicating a promising avenue for augmenting vaccine-induced immune responses.</p></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"298 ","pages":"Article 110240"},"PeriodicalIF":2.4,"publicationDate":"2024-09-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0378113524002621/pdfft?md5=60239b4a68b342c69f98ae9271a04995&pid=1-s2.0-S0378113524002621-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142162387","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}