Lactobacillus bulgaricus proteinase expressed in Lactococcus lactis is a powerful carrier for cell wall-associated and secreted bovine beta-lactoglobulin fusion proteins

Détails

ID Serval
serval:BIB_61795757DC10
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Lactobacillus bulgaricus proteinase expressed in Lactococcus lactis is a powerful carrier for cell wall-associated and secreted bovine beta-lactoglobulin fusion proteins
Périodique
Applied and Environmental Microbiology
Auteur⸱e⸱s
Bernasconi  E., Germond  J. E., Delley  M., Fritsche  R., Corthesy  B.
ISSN
0099-2240 (Print)
Statut éditorial
Publié
Date de publication
06/2002
Volume
68
Numéro
6
Pages
2917-23
Notes
Comparative Study
Journal Article --- Old month value: Jun
Résumé
Lactic acid bacteria have a good potential as agents for the delivery of heterologous proteins to the gastrointestinal mucosa and thus for the reequilibration of inappropriate immune responses to food antigens. Bovine beta-lactoglobulin (BLG) is considered a major allergen in cow's milk allergy. We have designed recombinant Lactococcus lactis expressing either full-length BLG or BLG-derived octapeptide T6 (IDALNENK) as fusions with Lactobacillus bulgaricus extracellular proteinase (PrtB). In addition to constructs encoding full-length PrtB for the targeting of heterologous proteins to the cell surface, we generated vectors aiming at the release into the medium of truncated PrtB derivatives lacking 100 (PrtB partial differential, PrtB partial differential-BLG, and PrtB partial differential-T6) or 807 (PrtBdelta) C-terminal amino acids. Expression of recombinant products was confirmed using either anti-PrtB, anti-BLG, or anti-peptide T6 antiserum. All forms of the full-length and truncated recombinant products were efficiently translocated, irrespective of the presence of eucaryotic BLG sequences in the fusion proteins. L. lactis expressing PrtB partial differential-BLG yielded up to 170 microg per 10(9) CFU in the culture supernatant and 9 microg per 10(9) CFU at the bacterial cell surface within 14 h. Therefore, protein fusions relying on the use of PrtB gene products are adequate for concomitant cell surface display and secretion by recombinant L. lactis and thus may ensure maximal bioavailability of the eucaryotic antigen in the gut-associated lymphoid tissue.
Mots-clé
*Bacterial Proteins Biological Transport Carrier Proteins/metabolism Cell Wall/*metabolism Endopeptidases/biosynthesis/genetics/*metabolism Lactobacillus/*enzymology Lactococcus lactis/*genetics/metabolism Lactoglobulins/genetics/*secretion Recombinant Fusion Proteins/metabolism/secretion
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/01/2008 15:53
Dernière modification de la notice
20/08/2019 15:18
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