Antigenic Characterization of the Glycosylated E2 Proteins of Classical Swine Fever Virus

被引:0
作者
Wang, Jin-Liang [1 ]
Sun, Quan-Wen [2 ]
Dong, Bing-Mei [3 ]
Wei, Feng [1 ]
Chen, Jin-long [3 ]
Dong, Yan-kai [3 ]
Wang, Ai-Hua [2 ]
Shen, Zhi-Qiang [1 ,3 ]
机构
[1] Shandong Binzhou Anim Sci & Vet Med Acad, Binzhou 256600, Peoples R China
[2] Hebei North Univ, Zhangjiakou 075000, Peoples R China
[3] Shandong Lvdu BioSci & Technol Co Ltd, Binzhou 256600, Peoples R China
关键词
D O I
暂无
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
E2 protein (E2) is one of the major structural proteins of the Classical Swine Fever Virus (CSFV). It is the major protective antigen of CSFV. The N-glycosylated E2 protein (Gly-E2) which had been glycosylated in vitro will enhance the immune response in theory. Therefore, in order to evaluate the immune efficacy of Gly-E2 of classical swine fever virus, the Gly-E20dendritic cells (DCs) and T cells were co-cultured and the BALB/c mice were inoculated with the Gly-E2 after that the E2 was glycosylated successfully. Sequentially, the IL-40IFN- and IgG levels in cell supernatant and in serum of BALB/c mice were measured by ELISA technology. The results showed that the glycosylation of E2 enhanced antigen presentation of dendritic cells significantly, and promoted the Th1 and Th2 immune response at the same time. Furthermore, the Th2 humoral immune response was more significant. The Gly-E2 excited the body to produce faster and more durable antibody protection and a better immune memory than that of CSFV and E2. Consequently, the results proved that the Gly-E2 possess a good preventive effect to classical swine fever. Therefore, the Gly-E2 will have a very deep development potential for the exploitation of new vaccines as a preferable antigen.
引用
收藏
页码:869 / 875
页数:7
相关论文
共 27 条
  • [1] Carbohydrate-mediated targeting of antigen to dendritic cells leads to enhanced presentation of antigen to T cells
    Adams, Eddie W.
    Ratner, Daniel M.
    Seeberger, Peter H.
    Hacohen, Nir
    [J]. CHEMBIOCHEM, 2008, 9 (02) : 294 - 303
  • [2] Determination of glycosylation sites and site-specific heterogeneity in glycoproteins
    An, Hyun Joo
    Froehlich, John W.
    Lebrilla, Carlito B.
    [J]. CURRENT OPINION IN CHEMICAL BIOLOGY, 2009, 13 (04) : 421 - 426
  • [3] Artemenko Natalia V, 2012, Methods Mol Biol, V899, P325, DOI 10.1007/978-1-61779-921-1_21
  • [4] Distinct pathways of antigen uptake and intracellular routing in CD4 and CD8 T cell activation
    Burgdorf, Sven
    Kautz, Andreas
    Boehnert, Volker
    Knolle, Percy A.
    Kurts, Christian
    [J]. SCIENCE, 2007, 316 (5824) : 612 - 616
  • [5] Dong BingMei, 2014, Chinese Journal of Veterinary Science, V34, P695
  • [6] Marker vaccine strategies and candidate CSFV marker vaccines
    Dong, Xiao-Nan
    Chen, Ying-Hua
    [J]. VACCINE, 2007, 25 (02) : 205 - 230
  • [7] The mannose receptor functions as a high capacity and broad specificity antigen receptor in human dendritic cells
    Engering, AJ
    Cella, M
    Fluitsma, D
    Brockhaus, M
    Hoefsmit, ECM
    Lanzavecchia, A
    Pieters, J
    [J]. EUROPEAN JOURNAL OF IMMUNOLOGY, 1997, 27 (09) : 2417 - 2425
  • [8] Dendritic cells: Functional aspects of glycosylation and lectins
    Erbacher, Annika
    Gieseke, Friederike
    Handgretinger, Rupert
    Mueller, Ingo
    [J]. HUMAN IMMUNOLOGY, 2009, 70 (05) : 308 - 312
  • [9] Alteration of the N-inked glycosylation condition in E1 glycoprotein of Classical Swine Fever Virus strain Brescia alters virulence in swine
    Fernandez-Sainz, I.
    Holinka, L. G.
    Gavrilov, B. K.
    Prarat, M. V.
    Gladue, D.
    Lu, Z.
    Jia, W.
    Risatti, G. R.
    Borca, M. V.
    [J]. VIROLOGY, 2009, 386 (01) : 210 - 216
  • [10] Mannose-binding lectin enhances Toll-like receptors 2 and 6 signaling from the phagosome
    Ip, W. K. Eddie
    Takahashi, Kazue
    Moore, Kathryn J.
    Stuart, Lynda M.
    Ezekowitz, R. Alan B.
    [J]. JOURNAL OF EXPERIMENTAL MEDICINE, 2008, 205 (01) : 169 - 181