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, Material and methods Bacterial strains and culture conditions ST strain LMD-9

. Makarova, Three isogenic mutants, prtS¯ (Lecomte et al. 2014), srtA¯, and mucBP¯ (this study), derived from LMD-9 were also used. Lactobacillus rhamnosus GG (LGG) (ATCC® 53103?, GenBank accession: CP000419), originally isolated from yogurt, was used in this study, 2006.

. Finland, ST strains were conserved at ?20 °C in reconstituted skim milk (10 %, w/v) and routinely grown at 42 °C without shaking in M17 medium supplemented with 2 % (w/v) of lactose (LM17; Terzaghi and Sandine, LGG strain was routinely cultivated in de Man Rogosa and Sharpe, 1975.

). and L. , All cultures were grown for 12 h (stationary phase) before to be used in bile salts survival and adhesion experiments. Construction of mucBP mutant A mutation in the gene STER_0576 (new locus tag STER_RS02840, NCBI-GI: 500000151) encoding MucBP protein was performed by replacing this gene by an erythromycin resistance gene. The LMD-9 mucBP¯ mutant was constructed according to the method described previously by, Sigma Aldrich®) medium at 37 °C without shaking and conserved in this medium with 20 % (w/v) of glycerol (Sigma) at ?20 °C, 2013.

, Amplification of each fragment was performed in 20 ?L PCR reaction mixture using 0.4 U Phusion high fidelity DNA polymerase (Finnzymes, Thermo Scientific, Finland), 80 ng mL ?1 of plasmid or 222 ng mL ?1 of LMD-9 DNA template, 0.2 ?M of each dNTPs, 0.5 ?M of each primer, and 4 ?L of ×5 Phusion HF buffer. Cycling conditions were 1 min at 98 °C, 30 cycles of three steps (20 s at 98 °C, 30 s at 52 °C, and 30 s at 72 °C), and a final extension at 72 °C for 10 min. When required, the PCR-amplified fragments were purified with the High Pure PCR purification Kit, Genomic DNA of LMD-9 strain, extracted according to Green and Sambrook (2012), was used as a template to amplify the UP-mucBP and mucBP-Down fragments which are located upstream and downstream the mucBP gene, respectively. The primers used are presented in Table 1. All primers were purchased from Eurogentec, 2013.

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M. Junjua, N. Kechaou, F. Chain, A. A. Awussi, Y. Roussel et al., Dary-Mourot A. A large scale in vitro screening of Streptococcus thermophilus strains revealed strains with a high anti-inflammatory potential. LWT-Food Science and Technology

M. Kebouchi, W. Galia, M. Genay, C. Soligot, X. Lecomte et al., Implication of sortase-dependant proteins of Streptococcus thermophilus in adhesion to human intestinal epithelial cell lines and bile salts tolerance, Applied Microbiology and Biotechnology

A. A. Awussi, C. Humeau, B. Maigret, X. Lecomte, M. Genay et al., Dary-Mourot A. Deficiency of the sortase SrtA and releasing of the cell-wall proteinase PrtS in extracellular medium of Streptococcus thermophilus 4F44, Article soumis au journal Applied Microbiology and Biotechnology

N. Jameh, W. Galia, A. A. Awussi, M. Genay, E. Roux et al., Characterization of a new peptide transport system in Streptococcus thermophilus, Article accepté dans le journal Food Reseach International
URL : https://hal.archives-ouvertes.fr/hal-01533905

A. A. Awussi, Z. Hafeez, L. Miclo, C. Perrin, and A. Dary-mourot, Proteolytic system of Streptococcus thermophilus, its evolution and emerging potential to produce bioactive peptides. Article revue en cours de rédaction pour soumission dans le journal Food Research International

A. Awussi, A. Caractérisation de l'ancrage de la protéase PrtS à la paroi de
URL : https://hal.archives-ouvertes.fr/hal-01329215

, Streptococcus thermophilus / Hydrolyse des caséines par PrtS. 12 ème édition du Séminaire de l'école doctorale RP2E, 15 Janvier 2015 -Vandoeuvre-lès-Nancy

A. A. Awussi, E. Roux, O. K. Chang, G. Humbert, A. Dary-mourot et al., Déficience de la sortase A, responsable de la libération de la protéase, p.16

, Janvier 2014 -Vandoeuvre-lès-Nancy

A. A. Awussi, E. Roux, O. K. Chang, G. Humbert, A. Dary-mourot et al., Déficience de la sortase A, responsable de la libération de la protéase, pp.16-18

C. Perrin, A. A. Awussi, C. Preuss, E. Roux, and . Miclo-l, Dary-Mourot A. La protéase PrtS de Streptococcus thermophilus : un outil biotechnologique pour l'obtention de peptides bioactifs

, ème Colloque du Clubs des Bactéries Lactiques, 2015.

. Résumé, Une étude de la variabilité des systèmes de transport Ami et OTS des trente souches de S. thermophilus a été réalisée. Enfin, l'interruption du cluster ots dans la souche LMD-9 a permis de conclure que le système de transport OTS intervient dans le transport de ditri peptides mais non dans le transport de nickel. D'autre part, l'hydrolyse des caséines par la protéase PrtS de S. thermophilus a été étudiée. Cette protéase habituellement ancrée à la paroi de la bactérie est retrouvée chez la souche 4F44 également sous forme libre. Les rôles des acteurs pouvant expliquer la libération partielle de PrtS de la souche 4F44 (PrtS4F44) ont été étudiés. Ainsi, la séquence protéique de PrtS4F44, différente de celle de PrtS de la souche LMD-9 (PrtSLMD-9), n'est pas la cause de la libération partielle de PrtS4F44. De plus, les quatre maturases identifiées dans le chromosome de S. thermophilus ont été comparées et leurs rôles ont été recherchés. Ainsi, les maturases n'interviennent pas dans le non-ancrage partiel de PrtS4F44 et PrtS pourrait s'automaturer chez S. thermophilus. La sortase A, acteur de l'ancrage de PrtS à la paroi de la bactérie, présente chez la souche 4F44 (srtA4F44) un allèle différent de celui de la souche LMD-9, Streptococcus thermophilus est une bactérie d'une importance économique majeure en raison de son utilisation dans la production de nombreux produits laitiers. Nous nous intéressons à la production de peptides bioactifs dans des laits fermentés par cette bactérie

, Mots clés : S. thermophilus, MLST, système de transport d'oligopeptides, Protéase PrtS, Sortase A