Veterinary microbiology最新文献

{"title":"Bovine tracheal organoids for studying Mycoplasma bovis respiratory infections","authors":"Chintha K. Premachandre ,&nbsp;Pin Shie Quah ,&nbsp;Bang Manh Tran ,&nbsp;Elizabeth Vincan ,&nbsp;Georgia Deliyannis ,&nbsp;Chinn Yi Wong ,&nbsp;Andrés Diaz-Méndez ,&nbsp;David C. Jackson ,&nbsp;Patrick C. Reading ,&nbsp;Glenn F. Browning ,&nbsp;Paola K. Vaz ,&nbsp;Nadeeka K. Wawegama","doi":"10.1016/j.vetmic.2024.110340","DOIUrl":"10.1016/j.vetmic.2024.110340","url":null,"abstract":"<div><div><em>In vitro</em> three-dimensional organoid models simulate key aspects of the structure and function of <em>in vivo</em> organs and have been used to study physiology, host-pathogen interactions, pathogenesis and pharmacodynamics. Although most organoid studies have been developed using human or mouse tissues, recent advancements have enabled the establishment of intestinal and respiratory tract organoids from domestic animal samples. <em>Mycoplasma bovis</em> causes chronic respiratory tract infections in cattle with significant health and economic consequences. The pathogenesis and virulence factors of <em>M. bovis</em> have been studied in several <em>in vitro</em> infection models, but the use of organoids has not been examined previously. In this study, we assessed the feasibility of using a matrix-embedded bovine tracheal organoid system to study respiratory infections with <em>M. bovis</em>. Bovine tracheal organoids were inoculated with <em>M. bovis</em> strain MbovMil and incubated for 72 hours to investigate the ability of <em>M. bovis</em> to proliferate, attach and invade the organoids. <em>M. bovis</em> was able to infect the organoids, resulting in a mean 260-fold increase in the titre of viable <em>M. bovis</em> by 72 hours post-inoculation. Examination of the infected organoids using transmission electron microscopy revealed the presence of mycoplasmas within the organoid cells and membrane bound clusters of <em>M. bovis</em> inside the intercellular junctions. Our findings indicate that bovine tracheal organoids can be used as a model system for studying respiratory tract infections caused by <em>M. bovis</em>.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"300 ","pages":"Article 110340"},"PeriodicalIF":2.4,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142828677","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":"IFN-mediated lncRNA-ISL promotes SVV infection through G1P3","authors":"Chen Wang ,&nbsp;Yijun Yang ,&nbsp;Xiwang Yang ,&nbsp;Qiyue Yang ,&nbsp;Rui Liu ,&nbsp;Wenting Li ,&nbsp;Xiao Liu","doi":"10.1016/j.vetmic.2024.110318","DOIUrl":"10.1016/j.vetmic.2024.110318","url":null,"abstract":"<div><div>lncRNAs play important regulatory roles in almost every aspect of physiological processes. However, the mechanisms by which animal-encoded lncRNAs regulate the interaction of viral infection with host antiviral immunity are unknown. To explore the mechanisms of lncRNA regulation of SVV infection and interferon responses. We performed complete transcriptome sequencing analysis of porcine kidney 15 (PK-15) after infection with SVV-1 strain and IFN-α treatment, and identified and screened the sequencing data to obtain potential functional lncRNA-ISL. selected genes were knocked down using CRISPR/Cas9 guide RNAs (gRNAs), and the results of the sequencing were monitored by qRT-PCR and protein blotting in multiple cell lines for selected gene mRNAs and their proteins as well as SVV infection. The results showed that 68 lncRNAs were significantly altered by IFN-α and 176 lncRNAs were significantly altered after SVV infection. We found that lncRNA-ISL gRNA significantly inhibited SVV infection compared to negative gRNA control. The expression of the antiviral ISG G1P3 was significantly increased following lncRNA-ISL gRNA editing compared to negative gRNA control in SVV-infected PK-15 cells. We observed that lncRNA-ISL regulation of SVV was independent of JAK-STAT signaling and not associated with G1P3 DNA methylation. Finally, we confirmed that the regulatory effect of lncRNA-ISL on G1P3 occurs during the initial transcription.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"302 ","pages":"Article 110318"},"PeriodicalIF":2.4,"publicationDate":"2024-12-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143012670","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":"Genetic diversity of Brucella abortus strains from cattle and water buffalo in the Italian province of Caserta","authors":"Luigi Orrù ,&nbsp;Antonella Lamontanara ,&nbsp;Celestina Mascolo ,&nbsp;Giorgia Borriello ,&nbsp;Rubina Paradiso ,&nbsp;Anna Cerrone ,&nbsp;Paolo Coppa ,&nbsp;Manuela Tittarelli ,&nbsp;Carlo Ferrara ,&nbsp;Esterina De Carlo ,&nbsp;Giorgio Galiero ,&nbsp;Alessandra Martucciello","doi":"10.1016/j.vetmic.2024.110314","DOIUrl":"10.1016/j.vetmic.2024.110314","url":null,"abstract":"<div><div><em>Brucella abortus</em> is an important zoonotic pathogen that infects cattle and buffaloes. In Italy the application of eradication programs combined with vaccination has greatly contributed to reduce the incidence of brucellosis. However, despite the eradication programs brucellosis continue to persist with a high endemicity in some areas of Italy including the province of Caserta. In the present study the genomes of 44 <em>B. abortus</em> strains isolated from different outbreak cases that affected the province of Caserta were sequenced to characterize the genetic diversity of the <em>Brucella</em> strains circulating during the period from 2017 to 2022. The relatedness among these isolates was compared to 52 publicly available genomes of Italian B. abortus isolates. The results highlighted a low genetic diversity in the <em>B. abortus</em> population present in the Caserta area with the persistence of a low number of <em>Brucella</em> lineages and suggests a reduction in circulating lineages in recent years due to eradication programs.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"299 ","pages":"Article 110314"},"PeriodicalIF":2.4,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142745039","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":"Identification and characterization of biosynthetic loci of lipooligosaccharide and capsular polysaccharide in Avibacterium paragallinarum","authors":"Ling Chen ,&nbsp;Juan Sun ,&nbsp;Jialian Hu ,&nbsp;Ye Tian ,&nbsp;Pengfei Du ,&nbsp;Qianqian Guo ,&nbsp;Chenghuai Yang ,&nbsp;Qianyi Zhang ,&nbsp;Saixiang Feng ,&nbsp;Ming Liao","doi":"10.1016/j.vetmic.2024.110317","DOIUrl":"10.1016/j.vetmic.2024.110317","url":null,"abstract":"<div><div>Infectious coryza is an acute respiratory disease in chickens caused by <em>Avibacterium paragallinarum</em>. Lipooligosaccharides (LOSs) and capsular polysaccharides are important components of <em>Av</em>. <em>paragallinarum</em>. Herein, we identified that gene cluster L6 and two genes <em>waaF</em>, <em>waaQ</em> were associated with LOS synthesis, and two genes <em>acbD</em> and <em>ccbF1</em> were involved in capsular synthesis. Mutant and complementary strains of these genes were generated by natural transformation. Wild-type strains produced LOS that yielded an upper and lower band. In comparison, Δ<em>waaQ</em> and Δ<em>waaF</em> yielded a truncated lower band and lacked the upper band, while ΔL6 did not exhibit the upper band, and the lower band was identical to that of the wild-type strain. The survival rates of wild-type strain, Δ<em>waaF</em>, Δ<em>waaQ</em>, and ΔL6 in chicken serum were 4.89 % ± 0.27 %, 0.0013 % ± 0.0002 %, 0.43 % ± 0.05 %, and 3.1 % ± 0.35 %, respectively. Notably, the resistances of Δ<em>waaF</em>, Δ<em>waaQ</em>, and ΔL6 to chicken serum were significantly lower than that of parent strain. By contrast, the survival rate of the Δ<em>acbD</em> strain was 55.17 % ± 0.61 %, and its resistance to chicken serum was significantly higher than that of the wild-type strain (<em>p</em> &lt; 0.001). Deletion of the <em>waaF</em>, <em>waaQ</em>, L6, <em>acbD</em>, and <em>ccbF1</em> genes resulted in enhanced formation of biofilm without altering immunogenicity in chickens. The Δ<em>waaF</em>, Δ<em>waaQ</em>, and Δ<em>ccbF1</em> strains exhibited heightened susceptibility to fowlicidin-2. Furthermore, Δ<em>waaF</em>, Δ<em>acbD</em>, and Δ<em>ccbF1</em> strains shown a decrease in pathogenicity (<em>p</em> &lt; 0.05). These results are valuable for advancing research on the pathogenesis of <em>Av</em>. <em>paragallinarum</em>.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"299 ","pages":"Article 110317"},"PeriodicalIF":2.4,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142745038","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":"Essential role of the interaction between classical swine fever virus core protein and cellular MYO1B in viral components transport to exosomes and titer maintenance","authors":"Xi Bao ,&nbsp;Tenhan Zhuang ,&nbsp;Yue Xu ,&nbsp;Li Chen ,&nbsp;Lei Feng ,&nbsp;Huochun Yao","doi":"10.1016/j.vetmic.2024.110315","DOIUrl":"10.1016/j.vetmic.2024.110315","url":null,"abstract":"<div><div>Classical swine fever (CSF) is a severe disease caused by the highly contagious CSFV. Our previous study demonstrated that exosomes from CSFV-infected cells contained significant amounts of viral genome and Core (C) protein and were infectious. To further elucidate the mechanisms underlying the formation of these infectious exosomes, we investigated the intracellular transport of the C protein in this study. We first identified the synchronized transport of the C protein and viral genome to exosomes, distinguishing it from other structural proteins. This suggests that the C protein likely binds to the viral genome and is transported to exosomes as a nucleocapsid. Subsequently, Co-IP and co-localization experiments confirmed the interaction between the host Myosin 1B (MYO1B) protein and the C protein. Key interaction sites were identified by generating and analyzing various C protein point mutations and truncation variants. The results indicate that specific sites at the N-terminus of the C protein significantly impact its interaction with MYO1B. Ultimately, by modulating MYO1B expression, we found that MYO1B knockdown significantly reduced the C protein and viral genome content in exosomes, leading to a decrease in CSFV titers. These findings underscore the critical role of MYO1B in facilitating the transport of the C protein and viral genome into exosomes during CSFV infection. Overall, this study explores the mechanism of infectious exosome formation during CSFV infection, revealing the critical role of the host MYO1B in this process. This is the first study to identify the involvement of MYO1B in viral infection, not only offering important insights into host-virus interactions but also identifying a new target for antiviral drug development.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"299 ","pages":"Article 110315"},"PeriodicalIF":2.4,"publicationDate":"2024-11-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142722370","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":"PD-1 blockade synergizes with ascorbic acid to restore the activation and anti-viral immune functions of CD8+ T cells in a mouse model of BVDV infection","authors":"Yang Li ,&nbsp;Zhibo Zhao ,&nbsp;Linru He ,&nbsp;Yue Liang ,&nbsp;Meng Liu ,&nbsp;Meiqi Dong ,&nbsp;Zehao Li ,&nbsp;Bin Xu ,&nbsp;Zecai Zhang ,&nbsp;Yulong Zhou ,&nbsp;Yu Liu ,&nbsp;Zhanbo Zhu ,&nbsp;Jianjun Zhao","doi":"10.1016/j.vetmic.2024.110316","DOIUrl":"10.1016/j.vetmic.2024.110316","url":null,"abstract":"<div><div>Bovine viral diarrhea virus (BVDV) can cause typical peripheral lymphopenia and inhibit CD8⁺ T-cell activation and proliferation. Programmed death-1 (PD-1) blockade has been shown to increase CD8⁺ T-cell activation during cytopathic (CP) BVDV infection but not non-cytopathic (NCP) BVDV. Notably, ascorbic acid (AA) restores lymphocyte count and activation during SARS-CoV-2 and influenza virus infections and has a synergistic effect with PD-1 blockade to improve antitumor CD8⁺ T-cell activity. Nevertheless, it remains unclear whether AA exerts an immunomodulatory effect on the activation and proliferation of CD8⁺ T cells during BVDV infection, especially NCP BVDV infection, or whether PD-1 blockade and AA exert a synergistic effect in regulating CD8⁺ T cell antiviral activities. In this study, we found that BVDV infection significantly decreased AA levels in serum and CD8⁺ T cells in a BALB/c mouse model. Interestingly, AA supplementation dramatically downregulated PD-1 expression, restored the activation and proliferation of CD8⁺ T cells, inhibited viral replication, ameliorated BVDV-induced histological lesions, and upregulated the expression of CD25 and p-ERK. More importantly, we also found a synergistic effect of PD-1 blockade with AA in restoring the activation and proliferation of CD8⁺ T cells during CP BVDV infection. However, during NCP BVDV infection, a synergistic effect of PD-1 blockade and AA led to the inhibition of viral replication and the promotion of IFN-γ production. Our findings provided new insights into the immunopathological mechanisms of BVDV and the potential value of anti-viral strategies based on AA treatment alone or in combination with PD-1 blockade.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"300 ","pages":"Article 110316"},"PeriodicalIF":2.4,"publicationDate":"2024-11-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142743582","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":"Dihydrolipoamide acetyltransferase is a key factor mediating adhesion and invasion of host cells by Mycoplasma synoviae","authors":"Haiyun Ma,&nbsp;Yunhai Zhao,&nbsp;Xiaoxiao He,&nbsp;Qing Wang,&nbsp;Yuting Zhang,&nbsp;Xiaoyong Xing,&nbsp;Xiaochun Wu,&nbsp;Guomei Quan,&nbsp;Shijun Bao","doi":"10.1016/j.vetmic.2024.110297","DOIUrl":"10.1016/j.vetmic.2024.110297","url":null,"abstract":"<div><div><em>Mycoplasma synoviae</em> is a significant avian pathogen responsible for chronic respiratory diseases, arthritis, and infectious synovitis in chickens and turkeys. These infections result in substantial economic losses to the global poultry industry. Dihydrolipoamide acetyltransferase (E2) is a multifunctional protein that plays an indispensable role in energy metabolism and redox balance and is also a key virulence factor of various pathogens. In this study, we used the avian pathogen <em>M. synoviae</em> as a model to identify the role of the E2 protein in the colonization and invasion of host cells. First, we prepared the polyclonal antibody of recombinant E2 (rE2) protein and found that the rE2 antibody had a strong complement-activating ability. E2 was found to be distributed in the cytoplasm and cell membrane of <em>M. synoviae</em> by immunoelectron microscopy. E2 localized on the cell membrane is a key factor in the adhesion of <em>M. synoviae</em> and has good immunogenicity. Enzyme-linked immunosorbent assay showed that the binding of rE2 to membrane proteins of chicken embryo fibroblasts (DF-1) was dose-dependent, and antiserum effectively inhibited this binding ability. Furthermore, E2 interacted with various components of the host extracellular matrix (ECM) and promoted the conversion of plasminogen to plasmin through terephthalic acid (tPA). In addition, E2 can enhance the ability of <em>M. synoviae</em> to invade DF-1 cells, which was significantly reduced after treatment with anti-E2 serum. These results indicate that E2 is an adhesion- and invasion-related protein and may be involved in the pathogenesis of <em>M. synoviae</em>, which provides new ideas for studying the pathogenesis of <em>M. synoviae</em> and preparing subunit vaccines.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"299 ","pages":"Article 110297"},"PeriodicalIF":2.4,"publicationDate":"2024-11-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142677042","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":"Chlamydia psittaci infection induces IFN-I and IL-1β through the cGAS-STING-IRF3/NLRP3 pathway via mitochondrial oxidative stress in human macrophages","authors":"Hongyu Yang ,&nbsp;Peiyuan Sun ,&nbsp;Shi Zhou ,&nbsp;Yuanyuan Tang ,&nbsp;Sijia Li ,&nbsp;Weiwei Li ,&nbsp;Xiang Yu ,&nbsp;Hanying Liu ,&nbsp;Yimou Wu","doi":"10.1016/j.vetmic.2024.110292","DOIUrl":"10.1016/j.vetmic.2024.110292","url":null,"abstract":"<div><div><em>Chlamydia psittaci</em> (<em>C. psittaci</em>) is a multi-host pathogen that elicits robust innate immune responses in macrophages. <em>Chlamydiae</em> target host mitochondria to manipulate the cellular fate and metabolic functions. However, the effect of <em>C. psittaci</em> on the host mitochondria remains obscure. This study investigated how <em>C. psittaci</em>, post-infection in human macrophages, induces mitochondrial oxidative stress and damage to activate the cGAS-STING-IRF3/NLRP3 pathway for IFN-I and IL-1β production. Results demonstrate that <em>C. psittaci</em> increased mitochondrial ROS (mtROS) production. This induced the release of oxidized mitochondrial DNA (mtDNA) into the cytoplasm of macrophages. It also augmented IFN-I and IL-1β production dependent on the cGAS-STING pathway. Macrophages pre-treated with mtROS inhibitor mito-TEMPO displayed reduced oxidized mtDNA. This consequently lowered IFN-I and IL-1β production via the cGAS-STING pathway induced by <em>C. psittaci</em>. Additionally, we found that mtROS production may inhibit <em>C. psittaci</em> proliferation through the synergistic action of IFN-I and IL-1β. In conclusion, our study reveals that <em>C. psittaci</em> induces mtROS production leading to mtDNA release. This activates the cGAS-STING-IRF3/NLRP3 pathway to increase IFN-I and IL-1β production. This study elucidates a novel mechanism of bacterial pathogen activation in the cGAS-STING pathway. This reveals the molecular mechanisms underlying the immune response to <em>C. psittaci</em> infection and proposes potential targets for the treatment of <em>C. psittaci</em> related diseases.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"299 ","pages":"Article 110292"},"PeriodicalIF":2.4,"publicationDate":"2024-11-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142700617","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":"Type I-E CRISPR-Cas system regulates fimZY and T3SS1 genes expression in Salmonella enterica serovar Pullorum","authors":"Kai Zhang ,&nbsp;Pengyu Wang ,&nbsp;Shanshan Li ,&nbsp;Xiaolei Xie ,&nbsp;Zhenyu Wang ,&nbsp;Yang Li ,&nbsp;Xinan Jiao ,&nbsp;Qiuchun Li","doi":"10.1016/j.vetmic.2024.110301","DOIUrl":"10.1016/j.vetmic.2024.110301","url":null,"abstract":"<div><div>Clustered regularly interspaced short palindromic repeats and associated Cas proteins (CRISPR-Cas) provide prokaryotes with adaptive immunity against invasion by plasmids or phages. In <em>Salmonella,</em> the type I-E CRISPR-Cas system is typically considered silent in immunity against foreign genetic elements. To elucidate the role of the CRISPR-Cas system, we chose <em>Salmonella enterica</em> serovar Pullorum S06004 as a model organism due to its four spacers and well-defined biological characteristics observed in previous studies. Western blot analysis revealed expression of Cas3 in S06004 cultured <em>in vitro</em>, but plasmid transformation assays demonstrated that both wild-type (WT) and S06004 strains overexpressing LeuO (a positive regulator of CRISPR-Cas) showed no immunity against the target plasmid. RNA-Seq analysis detected significant downregulation of the <em>f</em>im<!--> <!--> cluster, encoding type I fimbriae, and T3SS1-related genes in the <em>cas</em> cluster mutant compared to the WT. This downregulation was further confirmed in mutants of CR1 and individual <em>cas</em> genes by qRT-PCR. Consequently, mutants of CR1 and <em>cas</em> clusters exhibited decreased invasion of chicken hepatocellular carcinoma cells. The consistent regulation of T3SS1 genes by the CRISPR-Cas system in <em>S.</em> Pullorum, <em>S</em>. Enteritidis, and <em>S</em>. Typhimurium indicates a common role for the type I-E CRISPR-Cas system in promoting bacterial virulence. However, the specific molecular mechanisms underlying this regulation require further investigation.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"299 ","pages":"Article 110301"},"PeriodicalIF":2.4,"publicationDate":"2024-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142677045","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":"Mesomycoplasma (Mycoplasma) ovipneumoniae dihydrolipoamide dehydrogenase is an immunogenic plasminogen binding protein and a putative adhesin","authors":"Jiazhen Ge ,&nbsp;Tongtong Tian ,&nbsp;Yijian Liu ,&nbsp;Xuerui Li ,&nbsp;Qianqian Li ,&nbsp;Guodong Song ,&nbsp;Pengcheng Gao ,&nbsp;Fuying Zheng ,&nbsp;Yuefeng Chu","doi":"10.1016/j.vetmic.2024.110302","DOIUrl":"10.1016/j.vetmic.2024.110302","url":null,"abstract":"<div><div>The interaction of <em>Mesomycoplasma (Mycoplasma) ovipneumoniae</em> (<em>M. ovipneumoniae</em>) with host cells is a pivotal step in the infection process, underlining the necessity to develop vaccines and therapeutic approaches targeting the pathogen's key invasion mechanisms. The bacterium's capacity for adherence, invasion, and subsequent evasion of the host immune response underpins its pathogenicity, rendering adherence genes feasible vaccine targets. This study focuses on pyruvate dehydrogenase complex component E3 (PdhD), a membrane-anchored surface protein implicated in these pathogenic processes. Bioinformatics analysis reveals the conservation of PdhD sequence within <em>M. ovipneumoniae</em>. Membrane protein extraction, immunoblotting and ELISA assay have confirmed the presence of PdhD on the <em>M. ovipneumoniae</em> surface and cytoplasm, suggesting its multifunctionality. Our research employed antibody inhibition assays to characterize the bacterial adhesion suppression by anti-PdhD antibodies, complemented by bactericidal complement assays, supporting its candidacy as a putative vaccine target. The ELISA binding assay substantiated that PdhD binded to plasminogen (Plg) in a dose-dependent manner. Notably, PdhD is also involved in biofilm formation. The inhibitory effect of anti-PdhD sera on biofilm formation is congruent with novel therapeutic strategies targeting related mycoplasmas. This study reports the characterization of the first virulence-associated protein PdhD of <em>M. ovipneumoniae</em> and suggests its potential as a vaccine target to combat <em>M. ovipneumoniae</em> infection.</div></div>","PeriodicalId":23551,"journal":{"name":"Veterinary microbiology","volume":"299 ","pages":"Article 110302"},"PeriodicalIF":2.4,"publicationDate":"2024-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142648689","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}