期刊
JOURNAL OF BIOTECHNOLOGY
卷 168, 期 4, 页码 710-717出版社
ELSEVIER
DOI: 10.1016/j.jbiotec.2013.08.018
关键词
Twin-arginine translocation system; Signal peptide; Multivalent vaccine; Edwardsiella tarda; Aeromonas hydrophilaa
资金
- National High Technology Research and Development Program of China [2013AA093101]
- Ministry of Agriculture of China [CARS-50]
The twin-arginine translocation (Tat) system is a major pathway for transmembrane translocation of fully folded proteins. In this study, a multivalent vaccine to present foreign antigens on live attenuated vaccine Edwardsiella tarda WED using screened Tat signal peptide was constructed. Because the Tat system increases the yields of folded antigens in periplasmic space or extracellular milieu, it is expected to contribute to the production of conformational epitope-derived specific antibodies. E. tarda Tat signal peptides fused with the green fluorescent protein (GFP) was constructed under the control of an in vivo inducible dps promoter. The resulting plasmids were electroporated into WED and the subcellular localizations of GFP were analyzed with Western blotting. Eight signal peptides with optimized GFP translocation efficiency were further fused to a protective antigen glyceraldehyde-3-phosphate dehydrogenase (GapA) from a fish pathogen Aeromonas hydrophila. Signal peptides of DmsA, NapA, and SufI displayed high efficiency for GapA translocation. The relative percent survival (RPS) of turbot was measured with a co-infection of E. tarda and A. hydrophila, and the strain with DmsA signal peptide showed the maximal protection. This study demonstrated a new platform to construct multivalent vaccines using optimized Tat signal peptide in E. tarda. (C) 2013 Elsevier B.V. All rights reserved.
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