This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mesnage, S.
Right arrow Articles by Fouet, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mesnage, S.
Right arrow Articles by Fouet, A.

 Previous Article  |  Next Article 

Infection and Immunity, September 1999, p. 4847-4850, Vol. 67, No. 9
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Cell Surface-Exposed Tetanus Toxin Fragment C Produced by Recombinant Bacillus anthracis Protects against Tetanus Toxin

Stéphane Mesnage,* Martine Weber-Levy, Michel Haustant, Michèle Mock, and Agnès Fouet

Toxines et Pathogénie Bactériennes, URA 1858, Centre National de la Recherche Scientifique, Institut Pasteur, Paris, France

Received 25 March 1999/Returned for modification 6 May 1999/Accepted 25 May 1999

Bacillus anthracis, the causal agent of anthrax, synthesizes two surface layer (S-layer) proteins, EA1 and Sap, which account for 5 to 10% of total protein and are expressed in vivo. A recombinant B. anthracis strain was constructed by integrating into the chromosome a translational fusion harboring the DNA fragments encoding the cell wall-targeting domain of the S-layer protein EA1 and tetanus toxin fragment C (ToxC). This construct was expressed under the control of the promoter of the S-layer component gene. The hybrid protein was stably expressed on the cell surface of the bacterium. Mice were immunized with bacilli of the corresponding strain, and the hybrid protein elicited a humoral response to ToxC. This immune response was sufficient to protect mice against tetanus toxin challenge. Thus, the strategy developed in this study may make it possible to generate multivalent live veterinary vaccines, using the S-layer protein genes as a cell surface display system.


* Corresponding author. Mailing address: Toxines et Pathogénie Bactériennes, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris cédex 15, France. Phone: 33 1 45 68 86 54. Fax: 33 1 45 68 89 54. E-mail: smesnage{at}pasteur.fr.


Infection and Immunity, September 1999, p. 4847-4850, Vol. 67, No. 9
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Okano, K., Zhang, Q., Kimura, S., Narita, J., Tanaka, T., Fukuda, H., Kondo, A. (2008). System Using Tandem Repeats of the cA Peptidoglycan-Binding Domain from Lactococcus lactis for Display of both N- and C-Terminal Fusions on Cell Surfaces of Lactic Acid Bacteria. Appl. Environ. Microbiol. 74: 1117-1123 [Abstract] [Full Text]  
  • Yang, T. H., Pan, J. G., Seo, Y. S., Rhee, J. S. (2004). Use of Pseudomonas putida EstA as an Anchoring Motif for Display of a Periplasmic Enzyme on the Surface of Escherichia coli. Appl. Environ. Microbiol. 70: 6968-6976 [Abstract] [Full Text]  
  • Schaffer, C., Messner, P. (2004). Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology. Glycobiology 14: 31R-42R [Abstract] [Full Text]  
  • Ilk, N., Vollenkle, C., Egelseer, E. M., Breitwieser, A., Sleytr, U. B., Sara, M. (2002). Molecular Characterization of the S-Layer Gene, sbpA, of Bacillus sphaericus CCM 2177 and Production of a Functional S-Layer Fusion Protein with the Ability To Recrystallize in a Defined Orientation while Presenting the Fused Allergen. Appl. Environ. Microbiol. 68: 3251-3260 [Abstract] [Full Text]  
  • Breitwieser, A., Egelseer, E. M., Moll, D., Ilk, N., Hotzy, C., Bohle, B., Ebner, C., Sleytr, U. B., Sara, M. (2002). A recombinant bacterial cell surface (S-layer)-major birch pollen allergen-fusion protein (rSbsC/Bet v1) maintains the ability to self-assemble into regularly structured monomolecular lattices and the functionality of the allergen. Protein Eng Des Sel 15: 243-249 [Abstract] [Full Text]  
  • Brossier, F., Weber-Levy, M., Mock, M., Sirard, J.-C. (2000). Protective Antigen-Mediated Antibody Response against a Heterologous Protein Produced In Vivo by Bacillus anthracis. Infect. Immun. 68: 5731-5734 [Abstract] [Full Text]