Improvement of bovine beta-lactoglobulin production and secretion by Lactococcus lactis

Braz J Med Biol Res. 2005 Mar;38(3):353-9. doi: 10.1590/s0100-879x2005000300005. Epub 2005 Mar 8.

Abstract

The stabilizing effects of staphylococcal nuclease (Nuc) and of a synthetic propeptide (LEISSTCDA, hereafter called LEISS) on the production of a model food allergen, bovine beta-lactoglobulin (BLG), in Lactococcus lactis were investigated. The fusion of Nuc to BLG (Nuc-BLG) results in higher production and secretion of the hybrid protein. When LEISS was fused to BLG, the production of the resulting protein LEISS-BLG was only slightly improved compared to the one obtained with Nuc-BLG. However, the secretion of LEISS-BLG was dramatically enhanced (approximately 10- and 4-fold higher than BLG and Nuc-BLG, respectively). Finally, the fusion of LEISS to Nuc-BLG resulting in the protein LEISS-Nuc-BLG led to the highest production of the hybrid protein, estimated at approximately 8 microg/ml (approximately 2-fold higher than Nuc-BLG). In conclusion, the fusions described here led to the improvement of the production and secretion of BLG. These tools will be used to modulate the immune response against BLG via delivery of recombinant lactococci at the mucosal level, in a mouse model of cow's milk allergy.

MeSH terms

  • Animals
  • Cattle
  • Disease Models, Animal
  • Lactococcus lactis / immunology
  • Lactococcus lactis / metabolism*
  • Lactoglobulins / biosynthesis*
  • Lactoglobulins / immunology
  • Mice
  • Micrococcal Nuclease / immunology
  • Micrococcal Nuclease / metabolism*
  • Milk Hypersensitivity / immunology
  • Oligopeptides / immunology
  • Oligopeptides / metabolism*
  • Recombinant Fusion Proteins / immunology
  • Recombinant Fusion Proteins / metabolism

Substances

  • Lactoglobulins
  • Oligopeptides
  • Recombinant Fusion Proteins
  • Micrococcal Nuclease