Abstract |
The gene encoding V antigen from Yersinia pestis was cloned into the plasmid expression vector pGEX-5X-2. When electroporated into Escherichia coli JM109, the recombinant expressed V antigen as a stable fusion protein with glutathione S-transferase. The glutathione S-transferase-V fusion protein was isolated from recombinant E. coli and cleaved with factor Xa to yield purified V antigen as a stable product. Recombinant V antigen was inoculated intraperitoneally into mice and shown to induce a protective immune response against a subcutaneous challenge with 3.74 x 10(6) CFU of virulent Y. pestis. Protection correlated with the induction of a high titer of serum antibodies and a T-cell response specific for recombinant V antigen. These results indicate that V antigen should be a major component of an improved vaccine for plague.
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Authors | S E Leary, E D Williamson, K F Griffin, P Russell, S M Eley, R W Titball |
Journal | Infection and immunity
(Infect Immun)
Vol. 63
Issue 8
Pg. 2854-8
(Aug 1995)
ISSN: 0019-9567 [Print] United States |
PMID | 7622205
(Publication Type: Journal Article)
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Chemical References |
- Antibodies, Bacterial
- Antigens, Bacterial
- DNA Primers
- LcrV protein, Yersinia
- Pore Forming Cytotoxic Proteins
- Recombinant Fusion Proteins
- Vaccines, Synthetic
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Topics |
- Animals
- Antibodies, Bacterial
(biosynthesis)
- Antigens, Bacterial
(immunology)
- Base Sequence
- DNA Primers
(chemistry)
- Female
- Genes, Bacterial
- Mice
- Mice, Inbred BALB C
- Molecular Sequence Data
- Plague
(prevention & control)
- Pore Forming Cytotoxic Proteins
- Recombinant Fusion Proteins
- Vaccines, Synthetic
- Yersinia pestis
(immunology)
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