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 Chatel, J.-M.
Right arrow Articles by Corthier, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chatel, J.-M.
Right arrow Articles by Corthier, G.

 Previous Article  |  Next Article 

Clinical and Diagnostic Laboratory Immunology, May 2001, p. 545-551, Vol. 8, No. 3
1071-412X/01/$04.00+0   DOI: 10.1128/CDLI.8.3.545-551.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Induction of Mucosal Immune Response after Intranasal or Oral Inoculation of Mice with Lactococcus lactis Producing Bovine Beta-Lactoglobulin

Jean-Marc Chatel,1 Philippe Langella,2,* Karine Adel-Patient,1 Jacqueline Commissaire,2 Jean-Michel Wal,1 and Gérard Corthier3

Unité d'Immuno-Allergie Alimentaire INRA-CEA, Service de Pharmacologie et d'Immunologie, Bat 136 CEA Saclay, 91191 Gif sur Yvette,1 and Unité de Recherches Laitières et de Génétique Appliquée2 and Unité d'Ecologie et de Physiologie du Système Digestif,3 INRA, 78352 Jouy en Josas, France

Received 30 May 2000/Returned for modification 19 September 2000/Accepted 6 February 2001

The bovine beta-lactoglobulin (BLG) is a major cow's milk allergen. Here, we evaluated the immune response against BLG induced in mice, using the organism Lactococcus lactis, which has GRAS ("generally regarded as safe") status, as a delivery vehicle. The cDNA of the blg gene, encoding BLG, was expressed and engineered for either intra- or extracellular expression in L. lactis. Using a constitutive promoter, the yield of intracellular recombinant BLG (rBLG) was about 20 ng per ml of culture. To increase the quantity of rBLG, the nisin-inducible expression system was used to produce rBLG in the cytoplasmic and extracellular locations. Although the majority of rBLG remained in the cytoplasm, the highest yield (2 µg per ml of culture) was obtained with a secreting strain that encodes a fusion between a lactococcal signal peptide and rBLG. Whatever the expression system, the rBLG is produced mostly in a soluble, intracellular, and denatured form. The BLG-producing strains were then administered either orally or intranasally to mice, and the immune response to BLG was examined. Specific anti-BLG immunoglobulin A (IgA) antibodies were detected 3 weeks after the immunization protocol in the feces of mice immunized with the secreting lactococcal strain. Specific anti-BLG IgA detected in mice immunized with lactococci was higher than that obtained in mice immunized with the same quantity of pure BLG. No specific anti-BLG IgE, IgA, IgG1, or IgG2a was detected in sera of mice. These recombinant lactococcal strains constitute good vehicles to induce a mucosal immune response to a model allergen and to better understand the mechanism of allergy induced by BLG.


* Corresponding author. Mailing address: Unité de Recherches Laitières et de Génétique Appliquée, INRA, 78352 Jouy en Josas, France. Phone: 33(0)1 34 65 20 83. Fax: 33(0)1 34 65 20 65. E-mail: langella{at}biotec.jouy.inra.fr.


Clinical and Diagnostic Laboratory Immunology, May 2001, p. 545-551, Vol. 8, No. 3
1071-412X/01/$04.00+0   DOI: 10.1128/CDLI.8.3.545-551.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Llull, D., Poquet, I. (2004). New Expression System Tightly Controlled by Zinc Availability in Lactococcus lactis. Appl. Environ. Microbiol. 70: 5398-5406 [Abstract] [Full Text]  
  • Bermudez-Humaran, L. G., Cortes-Perez, N. G., Le Loir, Y., Alcocer-Gonzalez, J. M., Tamez-Guerra, R. S., de Oca-Luna, R. M., Langella, P. (2004). An inducible surface presentation system improves cellular immunity against human papillomavirus type 16 E7 antigen in mice after nasal administration with recombinant lactococci. J Med Microbiol 53: 427-433 [Abstract] [Full Text]  
  • Lindholm, A., Smeds, A., Palva, A. (2004). Receptor Binding Domain of Escherichia coli F18 Fimbrial Adhesin FedF Can Be both Efficiently Secreted and Surface Displayed in a Functional Form in Lactococcus lactis. Appl. Environ. Microbiol. 70: 2061-2071 [Abstract] [Full Text]  
  • Dieye, Y., Hoekman, A. J. W., Clier, F., Juillard, V., Boot, H. J., Piard, J.-C. (2003). Ability of Lactococcus lactis To Export Viral Capsid Antigens: a Crucial Step for Development of Live Vaccines. Appl. Environ. Microbiol. 69: 7281-7288 [Abstract] [Full Text]  
  • Chatel, J.-M., Nouaille, S., Adel-Patient, K., Le Loir, Y., Boe, H., Gruss, A., Wal, J.-M., Langella, P. (2003). Characterization of a Lactococcus lactis Strain That Secretes a Major Epitope of Bovine Beta-Lactoglobulin and Evaluation of Its Immunogenicity in Mice. Appl. Environ. Microbiol. 69: 6620-6627 [Abstract] [Full Text]  
  • Germond, J.-E., Delley, M., Gilbert, C., Atlan, D. (2003). Determination of the Domain of the Lactobacillus delbrueckii subsp. bulgaricus Cell Surface Proteinase PrtB Involved in Attachment to the Cell Wall after Heterologous Expression of the prtB Gene in Lactococcus lactis. Appl. Environ. Microbiol. 69: 3377-3384 [Abstract] [Full Text]  
  • Bernasconi, E., Germond, J.-E., Delley, M., Fritsche, R., Corthesy, B. (2002). Lactobacillus bulgaricus Proteinase Expressed in Lactococcus lactis Is a Powerful Carrier for Cell Wall-Associated and Secreted Bovine {beta}-Lactoglobulin Fusion Proteins. Appl. Environ. Microbiol. 68: 2917-2923 [Abstract] [Full Text]  
  • Miyoshi, A., Poquet, I., Azevedo, V., Commissaire, J., Bermudez-Humaran, L., Domakova, E., Le Loir, Y., Oliveira, S. C., Gruss, A., Langella, P. (2002). Controlled Production of Stable Heterologous Proteins in Lactococcus lactis. Appl. Environ. Microbiol. 68: 3141-3146 [Abstract] [Full Text]  
  • Ribeiro, L. A., Azevedo, V., Le Loir, Y., Oliveira, S. C., Dieye, Y., Piard, J.-C., Gruss, A., Langella, P. (2002). Production and Targeting of the Brucella abortus Antigen L7/L12 in Lactococcus lactis: a First Step towards Food-Grade Live Vaccines against Brucellosis. Appl. Environ. Microbiol. 68: 910-916 [Abstract] [Full Text]  
  • Bermudez-Humaran, L. G., Langella, P., Miyoshi, A., Gruss, A., Guerra, R. T., Montes de Oca-Luna, R., Le Loir, Y. (2002). Production of Human Papillomavirus Type 16 E7 Protein in Lactococcus lactis. Appl. Environ. Microbiol. 68: 917-922 [Abstract] [Full Text]  
  • Le Loir, Y., Nouaille, S., Commissaire, J., Bretigny, L., Gruss, A., Langella, P. (2001). Signal Peptide and Propeptide Optimization for Heterologous Protein Secretion in Lactococcus lactis. Appl. Environ. Microbiol. 67: 4119-4127 [Abstract] [Full Text]