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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. Source

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. Source

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. Source

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. Source

Agency: Cordis | 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.

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