The surface display of porcine parvovirus VP2 protein in Lactobacillus casei.
- Author:
Yi-Gang XU
1
;
Li-Chun CUI
;
Guang-Peng MA
;
Li-Jie TANG
;
Jun-Wei GE
;
Chun-Li XIA
;
Xin-Yuan QIAO
;
Li-Li ZHAO
;
Yi-Jing LI
Author Information
1. Department of Veterinary Medicine, Northeast Agricultural University, Harbin 150030, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Antigens, Viral;
genetics;
metabolism;
Blotting, Western;
Capsid Proteins;
genetics;
metabolism;
Cell Membrane;
metabolism;
Electrophoresis, Polyacrylamide Gel;
Fluorescent Antibody Technique;
Lactobacillus casei;
genetics;
metabolism;
Parvovirus, Porcine;
genetics;
metabolism;
Plasmids;
genetics;
Recombinant Proteins;
metabolism;
Swine;
virology;
Transformation, Genetic;
Viral Proteins;
genetics;
metabolism
- From:
Chinese Journal of Biotechnology
2007;23(2):315-318
- CountryChina
- Language:Chinese
-
Abstract:
Lactobacillus casei 393 was selected as a bacterial carrier for the expression of Porcine Parvovirus (PPV) protective antigen VP2 protein. The gene encoding PPV VP2 protein was cloned into the Lactobacillus casei surface expression vector pPG, and then the constructed recombinant vector pPG-VP2 was electrotransformed into Lactobacillus casei 393 generating the recombinant system pPG-VP2/L. casei393 expressing PPV VP2 protein. The recombinant strain was induced by 2% Lactose in MRS and about 74kD protein was detected with SDS-PAGE. The result of Western-blot indicated that the expressed protein possessed the antigenic specificity which could be recognized by mouse anti-PPV serum. The indirect immunofluorescent test showed that the expressed protein was secreted on the cell surface Lactobacillus casei.
