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Articles by Peng-Bo Ning
Total Records ( 3 ) for Peng-Bo Ning
  Kang-Kang Guo , Wei-Ming Zhang , Yan-Ming Zhang , Peng-Bo Ning , Jing-Yu Wang and Miao-Tao Zhang
  Classical Swine Fever (CSF) is a hemorrhagic disease of pigs caused by virulent strains of Classical Swine Fever Virus (CSFV). Vaccination is a useful tool for preventing and controlling CSF. In this study the protective antigens E0 and E2 genes of CSFV were cloned and inserted into a fowlpox virus vector to construct a recombinant plasmid. We transfected this plasmid into chicken embryo cells infected with the fowlpox virus FV282 to package and propagate the recombinant fowlpox virus FV282-E0-E2. Specific anti-CSFV antibodies were detected with enzyme-linked immunosorbent assay in FV282-E0-E2 immunized experimental mice and pigs. Moreover, virus challenge experiments were conducted in experimental pigs immunized with FV282-E0-E2. Immune protection was evaluated in experimental pigs infected with virulent CSFV by observing clinical manifestations and post-mortem examination. The results showed that recombinant fowlpox virus FV282-E0-E2 was obtained after ten cycles of blue plaque selection. The special anti-CSFV antibodies were detected in the experimental mice and pigs. The immunized pigs could resist the attack of the virulent CSFV strain. The recombinant fowlpox virus FV282-E0-E2 represents a potential candidate for the development of a genetic engineered vaccine for the future prevention of CSF.
  Jian-Ling Liu , Kang-Kang Guo , Zheng-Yuan Su , Xin-Gang Xu , He-Lin Li , Peng-Bo Ning , Hai-Xia Hong , Xiao-Yun Yang and Yan-Ming Zhang
  The viral envelope glycoprotein E2 is major target for eliciting protective antibodies against CSFV in infected animals. To express CSFV E2 protein on eukaryotic cells, the recombinant retroviral vector pBabe-puro-E2 was constructed by inserting full-length CSFV Shimen strain E2 region into pBabe-puro. Both of the recombinant retroviral vector and pVSVg plasmid were transfected eukaryotic 293GP cells using method of calcium phosphate coprecipitation in where thus the recombinant pseudovirus were packaged and propagated. The PK-15 cells were infected with recombinant pseudovirus. The recombinant PK-15 cells were screened by spytomycin resistance and the expression of E2 protein was detected by Flow Cytometer (FCM). The activity of recombinant E2 protein to induce immune responses was evaluated in Balb/c mice and unvaccinated pigs. The results showed that CSFV E2 protein was successfully expressed on PK-15 cells membrane. Anti-E2 antibody induced in experimental animals was detected by Enzyme Linked Immunosorbent Assay (ELISA). Moreover, the virus challenge indicated that the immunized pigs generated effective protection against virulent CSFV. These results indicated that a retroviral-based E2-vaccine is able to induce high level of specific antibodies and exhibits similar protective capability with that induced by the C-strain.
  Kang-Kang Guo , Qing-Hai Tang , Peng-Bo Ning , He-Lin Li , Wei Liu , Qi-Zhuang Lv , Wu-Long Liang , Zhi Lin , Cheng-Cheng Zhang and Yan-Ming Zhang
  The Nonstructural 2 (NS2) protein plays an important role in the infection process of Classical Swine Fever Virus (CSFV), it is an autoprotease cleaving the NS2-3 polyprotein for the NS3 protein release. The NS2 protein is an easily biodegradable protein in cells and the biogradation pathways are not still very clear at present. The Swine Umbilical Vein Endothelial Cell (SUVEC) constucted by the lab is a good cell line model for studying the pathogenic mechanism of CSFV. In this study, the degradation of CSFV NS2 were observed by detecting the NS2 protein expression in SUVEC and PK-15 cells. The recombinant plasmid pEGFP-NS2 with complete NS2 gene of CSFV was transfected into SUVEC and PK-15 cells, respectively. The NS2 RNA was determined by RT-PCR and expression of NS2 protein in cells were analyzed by fluorescence microscopy and western blot assay after transfected. The degradation of NS2 protein also were observed by fluorescence microscopy and Western-blot assay. The results shown that the NS2 protein is short-lived in cells, the biodegradation process could be inhibited by a proteasomal inhibitor (MG132), hinting the NS2 protein is degraded via proteasome pathway in cells and this degradation process was related to the phosphorylation of NS2 protein. This is a primary study on the degradation of CSFV NS2 protein. The future experiments will address the degradation mechanism of CSFV NS2 and find the phosphorylation amino acids of NS2 protein which maybe relate to protein degadation in cells.
 
 
 
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