Agency: European Commission | Branch: FP7 | Program: CSA-CA | Phase: KBBE.2013.1.3-04 | Award Amount: 1.19M | Year: 2013
The continuous growth of the world population translates into a demand of animal protein that can only be achieved through technological advances in farming, intensification, and expansion of farmed land. These pressures, combined with the increasing international trade of animals and their products, will lead to the rapid spread of animal diseases across borders and the emergence of new pathogens. This can have a huge impact on trade, livelihoods and public health. China is no exception and is in fact the worlds largest livestock producer and consumer, with pig and poultry meat being the most consumed meats. Research has many of the answers to prevent and control animal diseases, either through the understanding of their spread (epidemiology) or through better diagnostics for disease detection and surveillance. Both the European Union (EU) and China are two major worldwide players in animal health research. With dozens of institutions working on livestock health, the cross-border coordination and networking of research becomes a top priority to avoid duplication, while maximizing efforts by bringing together new ideas, expertise, technologies and funds. LinkTADs brings together world-class research institutes and experts in cross-border cooperation with the aim to coordinate research between the EU and China, thus improving scientific excellence in animal health (epidemiology and laboratory). Main objectives: identify the priority areas, where joint actions are needed link the research activities carried out on by European and Chinese research programmes ensure a wide-range networking of scientific communities and stakeholders provide a long term vision and achieve coordinated planning on future common research contribute to the international policies of the EU improve the research capacity of organizations by supporting young researchers through exchange programmes and training share the results and methodologies within and outside the consortium.
Lu J.,University of Pennsylvania |
Han Z.,University of Pennsylvania |
Liu Y.,University of Pennsylvania |
Liu Y.,China Animal Disease Control Center |
And 6 more authors.
Journal of Virology | Year: 2014
There are currently no U.S. Food and Drug Administration (FDA)-approved vaccines or therapeutics to prevent or treat Argentine hemorrhagic fever (AHF). The causative agent of AHF is Junin virus (JUNV); a New World arenavirus classified as a National Institute of Allergy and Infectious Disease/Centers for Disease Control and Prevention category A priority pathogen. The PTAP late (L) domain motif within JUNV Z protein facilitates virion egress and transmission by recruiting host Tsg101 and other ESCRT complex proteins to promote scission of the virus particle from the plasma membrane. Here, we describe a novel compound (compound 0013) that blocks the JUNV Z-Tsg101 interaction and inhibits budding of virus-like particles (VLPs) driven by ectopic expression of the Z protein and live-attenuated JUNV Candid-1 strain in cell culture. Since inhibition of the PTAP-Tsg101 interaction inhibits JUNV egress, compound 0013 serves as a prototype therapeutic that could reduce virus dissemination and disease progression in infected individuals. Moreover, since PTAP L-domain-mediated Tsg101 recruitment is utilized by other RNA virus pathogens (e.g., Ebola virus and HIV-1), PTAP inhibitors such as compound 0013 have the potential to function as potent broad-spectrum, host-oriented antiviral drugs. © 2014, American Society for Microbiology.
Peng X.,China Agricultural University |
Dong H.,China Animal Disease Control Center |
Wu Q.,China Agricultural University
FEMS Microbiology Letters | Year: 2015
A total of 129 sRNA candidates were identified in Brucella abortus 2308 in our previous work, and one candidate with potential to regulate expression of hemH gene was further analyzed in this study. We found that the novel sRNA can inhibit the expression of hemH and called it BsrH (Brucella sRNA regulating HemH). The expression level of BsrH was tested in four different stress conditions. A significant upregulation was detected during the growth in acidic and Brucella minimal media, as well as in the presence of hydroxyl peroxide, while iron deficiency caused the opposite effect. As expected, BsrH strongly affected the survival ratio of the Brucella cells under iron-limitation conditions, though overexpression of BsrH did not affect Brucella virulence. Thus, we conclude that BsrH plays a regulatory role in bacterial heme biosynthesis and can be considered as the first Brucella sRNA involved in stress responses. © 2014 FEMS.
Wang G.,China Agricultural University |
Zhou X.,China Agricultural University |
Bai Y.,China Agricultural University |
Zhang Z.,China Animal Disease Control Center |
Zhao D.,China Agricultural University
Acta Biochimica et Biophysica Sinica | Year: 2010
Prion diseases are infectious and fatal neurodegenerative disorders. The cellular prion protein (PrPC) converting into misfolded isoform of prion protein (PrPSc) is responsible for prion disease infection. Immune system plays an important role in facilitating the spread of prion infections from the periphery to the central nervous system. Macrophages were considered associated with the transportation and replication of PrP Sc. So, understanding the PrPC trafficking in macrophages is important to explore the transport mechanism for PrPSc. Here, we isolated exosomes from the culture medium of Ana-1 macrophage cell line and investigated the PrPC trafficked by exosomes and the interaction of PrPC with Hsp70 in secreted exosomes by western blotting, immunoelectron microscopy, and co-immunoprecipitation. The results showed that the isolated vesicles from the culture medium of macrophages were characterized by exosomes and bore PrPC. And PrPC bound to Hsp70 both in intracellular environment and secreted exosomes. In contrast, PrPC had no interaction with marker proteins of exosomes, Tag101 and Flotillin-1. These results suggested that PrPC present in extracellular space might be externalized through secreted exosomes from macrophages, and Hsp70 may play roles in the process of PrPC released via secreted exosomes.
Yu X.,China Animal Disease Control Center |
Zhou Z.,China Animal Disease Control Center |
Hu D.,China Agricultural University |
Zhang Q.,China Agricultural University |
And 10 more authors.
Emerging Infectious Diseases | Year: 2014
In 2012, an unprecedented large-scale outbreak of disease in pigs in China caused great economic losses to the swine industry. Isolates from pseudorabies virus epidemics in swine herds were characterized. Evidence confirmed that the pathogenic pseudorabies virus was the etiologic agent of this epidemic.
Huang Y.,China Agricultural University |
Wang Y.,China Agricultural University |
Bai Y.,China Agricultural University |
Wang Z.G.,China Animal Disease Control Center |
And 2 more authors.
Molecular and Cellular Biochemistry | Year: 2010
The pathogenesis of tuberculosis causing Mycobacterium bovis is largely due to its successful entry and survival in macrophages. Previous research indicated that mycobacteria-specific PE-PGRS genes code for cell surface proteins which may have role in mediating interactions with macrophages. In this study, we expressed PE-PGRS 62 gene in a non-pathogenic fast growing Mycobacterium smegmatis strain and found that the recombinant Mycobacterium smegmatis decreased macrophages livability in a dosage-dependent manner and time-dependent manner, compared with parental strain containing the vector only. To explore whether PE-PGRS 62 modulates the gene expression profile of macrophages, we stimulated macrophages by the M. smegmatis strain expressing PE-PGRS 62 as well as the control strains, followed by real-time RT-PCR assay for the mRNA expression level of IL-1β, IL-6, and iNOS. The results showed that the expression of IL-1β, IL-6 in macrophages were down-regulated by stimulation with the M. smegmatis strain expressing PE-PGRS 62 compared to the control strains (P < 0.05). In contrast, there were no measurable differences in the expression of iNOS. Overall, we demonstrated that PE-PGRS 62 protein altered the immune environment of the host cells, which suggest that the pathogenic PE-PGRS 62 protein altering the immune mechanism maybe involved in the pathogenesis of mycobacterial disease. © 2010 Springer Science+Business Media B.V.
Cai L.,China Animal Disease Control Center |
Han X.,China Animal Disease Control Center |
Ni J.,China Animal Disease Control Center |
Yu X.,China Animal Disease Control Center |
And 4 more authors.
Virus Research | Year: 2011
Porcine circovirus diseases (PCVD) are globally emerging diseases that have huge economic impacts on swine industry. Porcine circovirus type 2 (PCV2) is considered to be the essential primary causative agent of PCVD. In the present study, recombination analyses of PCV2 identified two possible recombination events with high confidence using recombination detection program, phylogenetic analysis and base-by-base comparison. These recombination events occurred between strains 09CQ (HQ395024) and ZhuJi2003 (AY579893), giving rise to two recombinants 09GS (HQ395028) and HN0907 (GU938303). Phylogenetic analyses of the parental strains at full length level suggest that natural recombination happened between PCV2b strains. Interestingly, recombination of the two parental strains yielded two recombinants through different recombination patterns with crossover regions mainly located in ORF1 and ORF2, respectively. These results demonstrate that recombination between PCV2b strains can occur both in non-structural protein coding region and structural protein coding region. Our study not only indicates that PCV2b strains can undergo recombination through a variety of patterns, but also suggests that recombination contributes to the genetic diversity of PCV2. © 2011 Elsevier B.V.
Liu C.,Beijing University of Chemical Technology |
Wang H.,China Animal Disease Control Center |
Jiang Y.,China Animal Disease Control Center |
Du Z.,Beijing University of Chemical Technology
Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences | Year: 2011
A rapid, sensitive, and specific method for the determination of amoxicillin (AMO), amoxicilloic acid (AMA), amoxicillin diketopiperazine-2',5'-dione (DIKETO), penicillin G (PEN G), benzylpenicilloic acid (BPA-1), benzylpenilloic acid (BPA-2), and benzylpenillic acid (BPA-3) in bovine milk using ultra-high-performance liquid chromatography-tandem mass spectrometry (UHPLC-MS/MS) was developed and validated. The method used penicillin V (PEN V) as the internal standard and ethanol for the deproteinisation of bovine milk. Chromatographic separation of the components was performed on a Waters Acquity UPLC ® HSS T3 column (100mm×2.1mm, 1.8μm) using a mixture of 0.15% formic acid in water with 5mM ammonium acetate and acetonitrile as the mobile phase. Gradient elution was performed at a flow rate of 0.25mLmin -1. The mass spectrometer was operated in the positive electrospray ionisation MS/MS mode. The method was fully validated according to EU requirements, including linearity, precision, trueness, limit of quantification, limit of detection, and specificity. The results were within the ranges specified. The established method was successfully applied in the determination of AMO, PEN G, and their major metabolites in 40 commercial bovine milk samples. The results showed that 8 samples were contaminated with BPA-1 or BPA-2. The mean levels (occurrence) of BPA-1 and BPA-2 in positive samples were 287 (50%) and 320 (100%)ngmL -1, respectively. No sample was found to be contaminated with AMO, AMA, DIKETO, PEN G, and BPA-3. These findings could play an important role in food safety, because BPA-1 and BPA-2 metabolites pose possible health risks, although they are not included in the maximum residue limit legislation. © 2011 Elsevier B.V.
Liu Y.,China Animal Disease Control Center
Se pu = Chinese journal of chromatography / Zhongguo hua xue hui | Year: 2010
A method for the determination of robenidine residue in chicken tissues and eggs by high performance liquid chromatography (HPLC) was established. The samples were extracted with acetonitrile and purified by an HLB solid-phase extraction (SPE) cartridge. The extract was analyzed by HPLC with acetonitrile-0.05 mol/L NH4H2PO4 buffer (6:4, v/v, pH 6.5) as the mobile phase. The flow rate of the mobile phase was 1.0 mL/min and detection wavelength was 317 nm. There was a good linear correlation between the peak areas and the concentrations of robenidine in the range of 10-1000 microg/L. The limit of detection (S/N = 3) was 10 microg/L, and the limit of quantification (S/N = 10) was 15 microg/kg. The recoveries of robenidine were 73.1%-88.7% at the spiked levels of 15, 50 and 100 microg/kg. The results demonstrate that the method is easy, fast, sensitive, and suitable for the confirmation and quantification of robenidine residue in chicken tissues and eggs. The clean-up effect, sensitivity, accuracy and precision can all meet the analysis requirement.
Qi C.,CAS Institute of Mechanics |
Qi C.,University of Chinese Academy of Sciences |
Qi C.,CAS Institute of Biophysics |
Tian X.-S.,CAS Institute of Microbiology |
And 8 more authors.
Biosensors and Bioelectronics | Year: 2010
A novel method is reported for the detection of avian influenza virus subtype H5 using a biosensor based on high spatial resolution imaging ellipsometry (IE). Monoclonal antibodies specific to H5 hemagglutinin protein were immobilized on silicon wafers and used to capture virus particles. Resultant changes on the surface of the wafers were visualized directly in gray-scale on an imaging ellipsometry image. This preliminary study has shown that the assay is rapid and specific for the identification of avian influenza virus subtype H5. Compared with lateral-flow immunoassays, this biosensor not only has better sensitivity, but can also simultaneously perform multiplexed tests. These results suggest that this biosensor might be a valuable diagnostic tool for avian influenza virus detection. © 2009 Elsevier B.V. All rights reserved.