Surface proteins of Lactococcus lactis: Bacterial resources for muco-adhesion in the gastrointestinal tract

Martín M, Gutiérrez J, Criado R, Herranz C, Cintas LM, Hernández PE (2007) Chimeras of mature pediocin PA-1 fused to the signal peptide of enterocin P permits the cloning,

Using Usp45 as a control for homolo- gous protein secretion, we looked for a pos- sible perturbation of the lactococcal secre- tion machinery due to the high level of Nuc secretion

In the case of Afp1, secretion enhancement by fusion with the LEISS propeptide leads to the release of some of the secreted LEISS-Afp1 form in the supernatant, whereas no protein

Here, we review several works evaluating the influence of the localization on the production yields of several heterologous proteins produced in L. The questions of size

lactis strains, 20 from goat milk whey and one strain from cow milk were used to evaluate their antibacterial activity against four pathogenic germs responsible for mastitis:

lactis bacterial cells immobilized onto AFM tip and cantilever; (B, E) histograms of adhesion forces and (C, F) typical force-distance curves obtained when probing interactions

In contrast, data available for pili of non-pathogenic Gram-positive bacteria, such as Lactic Acid Bacteria (LAB), are scarce and restricted to Lactobacillus rhamnosus GG

A hydrophobie de surface équivalente (comme montré par la méthode MATS - Annexe 1 ) et donc avec une probabilité d’interaction avec le PS similaire sur la seule base de