Purification and immunogenicity of fusion VP1 protein of foot and mouth disease virus

Biochemistry ◽  
1984 ◽  
Vol 23 (26) ◽  
pp. 6474-6480 ◽  
Author(s):  
Steven J. Shire ◽  
Larry Bock ◽  
John Ogez ◽  
Stuart Builder ◽  
Dennis Kleid ◽  
...  
2017 ◽  
Vol 2017 ◽  
pp. 1-9 ◽  
Author(s):  
Xinsheng Liu ◽  
Jianliang Lv ◽  
Yuzhen Fang ◽  
Peng Zhou ◽  
Yanzhen Lu ◽  
...  

Improving vaccine immunogenicity by targeting antigens to dendritic cells has recently emerged as a new design strategy in vaccine development. In this study, the VP1 gene of foot-and-mouth disease virus (FMDV) serotype A was fused with the gene encoding human immunodeficiency virus (HIV) membrane glycoprotein gp120 or C2-V3 domain of hepatitis C virus (HCV) envelope glycoprotein E2, both of which are DC-SIGN-binding glycoproteins. After codon optimization, the VP1 protein and the two recombinant VP1-gp120 and VP1-E2 fusion proteins were expressed in Sf9 insect cells using the insect cell-baculovirus expression system. Western blotting showed that the VP1 protein and two recombinant VP1-gp120 and VP1-E2 fusion proteins were correctly expressed in the Sf9 insect cells and had good reactogenicity. Guinea pigs were then immunized with the purified proteins, and the resulting humoral and cellular immune responses were analyzed. The VP1-gp120 and VP1-E2 fusion proteins induced significantly higher specific anti-FMDV antibody levels than the VP1 protein and stronger cell-mediated immune responses. This study provides a new perspective for the development of novel FMDV subunit vaccines.


2009 ◽  
Vol 24 (6) ◽  
pp. 566-572
Author(s):  
Shuai Song ◽  
Tong Lin ◽  
Jun-jun Shao ◽  
Shan-dian Gao ◽  
Guo-zheng Cong ◽  
...  

2009 ◽  
Vol 24 (3) ◽  
pp. 215-220 ◽  
Author(s):  
Tong Lin ◽  
Jun-zheng Du ◽  
Jun-jun Shao ◽  
Guo-zheng Cong ◽  
Shuai Song ◽  
...  

2013 ◽  
Vol 175 (1) ◽  
pp. 87-90 ◽  
Author(s):  
A. Peralta ◽  
G.A. Maroniche ◽  
V. Alfonso ◽  
P. Molinari ◽  
O. Taboga

2017 ◽  
Vol 115 ◽  
pp. 374-381 ◽  
Author(s):  
Wenming Liu ◽  
Baolin Yang ◽  
Mingxia Wang ◽  
Haiwei Wang ◽  
Decheng Yang ◽  
...  

AMB Express ◽  
2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Mpho Victoria Mamabolo ◽  
Jacques Theron ◽  
Francois Maree ◽  
Michael Crampton

AbstractThe seven serotypes of foot-and-mouth disease virus (FMDV) differ on the surface exposed regions on the VP1, 2 and 3 proteins. Amongst the three, the VP1 protein has been produced the most for use in serotyping assays for some of the Euro-Asian serotypes. In this study the VP1 protein of the FMDV SAT2/ZIM/7/83 was expressed in Escherichia coli BL21 cells in Luria broth and EnPresso® B media in shake flasks. Production was further developed and the VP1 protein was produced at 2.15 g L−1 in fed-batch fermentations at 2 L scale. The protein formed insoluble inclusion bodies that were isolated, denatured and refolded. When tested in ELISA, the protein was found to be highly reactive with serum from a SAT2 vaccinated guinea pig, and not reactive to SAT1 and SAT3 antisera. These results open avenues to evaluate recombinantly expressed VP1 proteins for differentiation of the three Southern African Territories serotypes of FMDV that co-occur in Southern and East Africa. In addition, this could mitigate the need for employing virus as reagent, or having to raise reagent antibodies.


2012 ◽  
Vol 157 (10) ◽  
pp. 1967-1970 ◽  
Author(s):  
Biswajit Das ◽  
Aniket Sanyal ◽  
Saravanan Subramaniam ◽  
Jajati K. Mohapatra ◽  
Bramhadev Pattnaik

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