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

被引:15
作者
Nouaille, S
Bermúdez-Humarán, LG
Adel-Patient, K
Commissaire, J
Gruss, A
Wal, GM
Azevedo, V
Langella, P
Chatel, JM
机构
[1] INRA, Ecol & Physiol Digest Tract Unit, Dairy Res & Appl Genet Unit, F-78352 Jouy En Josas, France
[2] CEA Saclay, INRA, DRM SPI, Food Immunoallergy Lab, F-91191 Gif Sur Yvette, France
[3] Univ Fed Minas Gerais, Inst Ciencias Biol, Belo Horizonte, MG, Brazil
关键词
Lactococcus lactis; protein secretion; LEISSTCDA; Staphylococcal nuclease; beta-lactoglobulin; allergen;
D O I
10.1590/S0100-879X2005000300005
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 B-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 (similar to 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 similar to 8 mu g/ml (similar to 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.
引用
收藏
页码:353 / 359
页数:7
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