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Volumn 113, Issue , 2015, Pages 447-461

Surface proteins of Propionibacterium freudenreichii are involved in its anti-inflammatory properties

Author keywords

Cell wall; Fluorescent labeling; Probiotic; Proteome; Shaving; Surfaceome

Indexed keywords

MEMBRANE PROTEIN; PREBIOTIC AGENT; PROBIOTIC AGENT; ANTIINFLAMMATORY AGENT; BACTERIAL PROTEIN; IMMUNOLOGIC FACTOR;

EID: 84915818563     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2014.07.018     Document Type: Article
Times cited : (87)

References (77)
  • 2
    • 0033033684 scopus 로고    scopus 로고
    • Effect of propionibacteria supplementation on fecal bifidobacteria and segmental colonic transit time in healthy human subjects
    • Bouglé D., Roland N., Lebeurrier F., Arhan P. Effect of propionibacteria supplementation on fecal bifidobacteria and segmental colonic transit time in healthy human subjects. Scand J Gastroenterol Feb 1999, 34(2):144-148.
    • (1999) Scand J Gastroenterol , vol.34 , Issue.2 , pp. 144-148
    • Bouglé, D.1    Roland, N.2    Lebeurrier, F.3    Arhan, P.4
  • 3
    • 0001320952 scopus 로고    scopus 로고
    • Propionibacterium freudenreichii stimulates the growth of Bifidobacterium bifidum in vitro and increases fecal bifidobacteria in healthy human volunteers
    • Roland N., Bougle D., Lebeurrier F., Arhan P., Maubois J.L. Propionibacterium freudenreichii stimulates the growth of Bifidobacterium bifidum in vitro and increases fecal bifidobacteria in healthy human volunteers. Int Dairy J 1998, 8(6):587-588.
    • (1998) Int Dairy J , vol.8 , Issue.6 , pp. 587-588
    • Roland, N.1    Bougle, D.2    Lebeurrier, F.3    Arhan, P.4    Maubois, J.L.5
  • 4
    • 33748445092 scopus 로고    scopus 로고
    • Effect of ingested culture of Propionibacterium freudenreichii ET-3 on fecal microflora and stool frequency in healthy females
    • Hojo K., Yoda N., Tsuchita H., Ohtsu T., Seki K., Taketomo N., et al. Effect of ingested culture of Propionibacterium freudenreichii ET-3 on fecal microflora and stool frequency in healthy females. Biosci Microflora 2002, 21(2):115-120.
    • (2002) Biosci Microflora , vol.21 , Issue.2 , pp. 115-120
    • Hojo, K.1    Yoda, N.2    Tsuchita, H.3    Ohtsu, T.4    Seki, K.5    Taketomo, N.6
  • 5
    • 33748452632 scopus 로고    scopus 로고
    • A novel bifidogenic growth stimulator produced by Propionibacterium freudenreichii
    • Kaneko T. A novel bifidogenic growth stimulator produced by Propionibacterium freudenreichii. Biosci Microflora 1999, 18(2):73-80.
    • (1999) Biosci Microflora , vol.18 , Issue.2 , pp. 73-80
    • Kaneko, T.1
  • 6
    • 79958249012 scopus 로고    scopus 로고
    • Effects of fermented milk whey containing novel bifidogenic growth stimulator produced by Propionibacterium on fecal bacteria, putrefactive metabolite, defecation frequency and fecal properties in senile volunteers needed serious nursing-care taking enteral nutrition by tube feeding
    • Seki K., Nakao H., Umino H., Isshiki H., Yoda N., Tachihara R., et al. Effects of fermented milk whey containing novel bifidogenic growth stimulator produced by Propionibacterium on fecal bacteria, putrefactive metabolite, defecation frequency and fecal properties in senile volunteers needed serious nursing-care taking enteral nutrition by tube feeding. J Intest Microbiol 2004, 18(2):107-115.
    • (2004) J Intest Microbiol , vol.18 , Issue.2 , pp. 107-115
    • Seki, K.1    Nakao, H.2    Umino, H.3    Isshiki, H.4    Yoda, N.5    Tachihara, R.6
  • 7
    • 0035995860 scopus 로고    scopus 로고
    • Effect of probiotics on constipation, fecal azoreductase activity and fecal mucin content in the elderly
    • Ouwehand A.C., Lagstrom H., Suomalainen T., Salminen S. Effect of probiotics on constipation, fecal azoreductase activity and fecal mucin content in the elderly. Ann Nutr Metab 2002, 46(3-4):159-162.
    • (2002) Ann Nutr Metab , vol.46 , Issue.3-4 , pp. 159-162
    • Ouwehand, A.C.1    Lagstrom, H.2    Suomalainen, T.3    Salminen, S.4
  • 8
    • 80054823312 scopus 로고    scopus 로고
    • Treatment of ulcerative colitis with milk whey culture with Propionibacterium freudenreichii
    • Mitsuyama K., Masuda J., Yamasaki H., Kuwaki K., Kitazaki S., Koga H., et al. Treatment of ulcerative colitis with milk whey culture with Propionibacterium freudenreichii. J Intest Microbiol 2007, 21(2):143-147.
    • (2007) J Intest Microbiol , vol.21 , Issue.2 , pp. 143-147
    • Mitsuyama, K.1    Masuda, J.2    Yamasaki, H.3    Kuwaki, K.4    Kitazaki, S.5    Koga, H.6
  • 9
    • 85047698232 scopus 로고    scopus 로고
    • Propionibacteria induce apoptosis of colorectal carcinoma cells via short-chain fatty acids acting on mitochondria
    • Jan G., Belzacq A.S., Haouzi D., Rouault A., Metivier D., Kroemer G., et al. Propionibacteria induce apoptosis of colorectal carcinoma cells via short-chain fatty acids acting on mitochondria. Cell Death Differ Feb 2002, 9(2):179-188.
    • (2002) Cell Death Differ , vol.9 , Issue.2 , pp. 179-188
    • Jan, G.1    Belzacq, A.S.2    Haouzi, D.3    Rouault, A.4    Metivier, D.5    Kroemer, G.6
  • 10
    • 33847265296 scopus 로고    scopus 로고
    • Acidic extracellular pH shifts colorectal cancer cell death from apoptosis to necrosis upon exposure to propionate and acetate, major end-products of the human probiotic propionibacteria
    • Lan A., Lagadic-Gossmann D., Lemaire C., Brenner C., Jan G. Acidic extracellular pH shifts colorectal cancer cell death from apoptosis to necrosis upon exposure to propionate and acetate, major end-products of the human probiotic propionibacteria. Apoptosis Dec 29 2007, 12:573-591.
    • (2007) Apoptosis , vol.12 , pp. 573-591
    • Lan, A.1    Lagadic-Gossmann, D.2    Lemaire, C.3    Brenner, C.4    Jan, G.5
  • 11
    • 84858768983 scopus 로고    scopus 로고
    • Milk fermented by Propionibacterium freudenreichii induces apoptosis of HGT-1 human gastric cancer cells
    • Cousin F.J., Jouan-Lanhouet S., Dimanche-Boitrel M.T., Corcos L., Jan G. Milk fermented by Propionibacterium freudenreichii induces apoptosis of HGT-1 human gastric cancer cells. PLoS ONE 2012, 7(3):e31892.
    • (2012) PLoS ONE , vol.7 , Issue.3 , pp. e31892
    • Cousin, F.J.1    Jouan-Lanhouet, S.2    Dimanche-Boitrel, M.T.3    Corcos, L.4    Jan, G.5
  • 12
    • 84880321496 scopus 로고    scopus 로고
    • Tracking the microbiome functionality: focus on Propionibacterium species
    • Foligné B., Breton J., Mater D., Jan G. Tracking the microbiome functionality: focus on Propionibacterium species. Gut Feb 6 2013, 62(8):1227-1228.
    • (2013) Gut , vol.62 , Issue.8 , pp. 1227-1228
    • Foligné, B.1    Breton, J.2    Mater, D.3    Jan, G.4
  • 13
    • 78650340356 scopus 로고    scopus 로고
    • Promising immunomodulatory effects of selected strains of dairy propionibacteria as evidenced in vitro and in vivo
    • Foligné B., Deutsch S.M., Breton J., Cousin F.J., Dewulf J., Samson M., et al. Promising immunomodulatory effects of selected strains of dairy propionibacteria as evidenced in vitro and in vivo. Appl Environ Microbiol Dec 2010, 76(24):8259-8264.
    • (2010) Appl Environ Microbiol , vol.76 , Issue.24 , pp. 8259-8264
    • Foligné, B.1    Deutsch, S.M.2    Breton, J.3    Cousin, F.J.4    Dewulf, J.5    Samson, M.6
  • 14
    • 84857811489 scopus 로고    scopus 로고
    • Contribution of surface beta-glucan polysaccharide to physicochemical and immunomodulatory properties of Propionibacterium freudenreichii
    • Deutsch S.M., Parayre S., Bouchoux A., Guyomarc'h F., Dewulf J., Dols-Lafargue M., et al. Contribution of surface beta-glucan polysaccharide to physicochemical and immunomodulatory properties of Propionibacterium freudenreichii. Appl Environ Microbiol Mar 2012, 78(6):1765-1775.
    • (2012) Appl Environ Microbiol , vol.78 , Issue.6 , pp. 1765-1775
    • Deutsch, S.M.1    Parayre, S.2    Bouchoux, A.3    Guyomarc'h, F.4    Dewulf, J.5    Dols-Lafargue, M.6
  • 15
    • 1542373514 scopus 로고    scopus 로고
    • Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii
    • Leverrier P., Vissers J.P., Rouault A., Boyaval P., Jan G. Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii. Arch Microbiol Mar 2004, 181(3):215-230.
    • (2004) Arch Microbiol , vol.181 , Issue.3 , pp. 215-230
    • Leverrier, P.1    Vissers, J.P.2    Rouault, A.3    Boyaval, P.4    Jan, G.5
  • 16
    • 33846522362 scopus 로고    scopus 로고
    • Transcarboxylase mRNA: a marker which evidences P. freudenreichii survival and metabolic activity during its transit in the human gut
    • Hervé C., Fondrevez M., Cheron A., Barloy-Hubler F., Jan G. Transcarboxylase mRNA: a marker which evidences P. freudenreichii survival and metabolic activity during its transit in the human gut. Int J Food Microbiol Feb 15 2007, 113(3):303-314.
    • (2007) Int J Food Microbiol , vol.113 , Issue.3 , pp. 303-314
    • Hervé, C.1    Fondrevez, M.2    Cheron, A.3    Barloy-Hubler, F.4    Jan, G.5
  • 17
    • 77955388627 scopus 로고    scopus 로고
    • The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy actinobacterium with food and probiotic applications
    • Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S., et al. The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy actinobacterium with food and probiotic applications. PLoS ONE 2010, 5(7):e11748.
    • (2010) PLoS ONE , vol.5 , Issue.7 , pp. e11748
    • Falentin, H.1    Deutsch, S.M.2    Jan, G.3    Loux, V.4    Thierry, A.5    Parayre, S.6
  • 19
    • 4444244050 scopus 로고    scopus 로고
    • In vitro adhesion of propionibacteria to human intestinal mucus
    • Thiel A., Eikmanns B., Salminen S., Ouwehand A.C. In vitro adhesion of propionibacteria to human intestinal mucus. Ital J Food Sci 2004, 16(2):245-253.
    • (2004) Ital J Food Sci , vol.16 , Issue.2 , pp. 245-253
    • Thiel, A.1    Eikmanns, B.2    Salminen, S.3    Ouwehand, A.C.4
  • 20
    • 0032983458 scopus 로고    scopus 로고
    • Human ileostomy glycoproteins as a model for small intestinal mucus to investigate adhesion of probiotics
    • Tuomola E.M., Ouwehand A.C., Salminen S.J. Human ileostomy glycoproteins as a model for small intestinal mucus to investigate adhesion of probiotics. Lett Appl Microbiol Mar 1999, 28(3):159-163.
    • (1999) Lett Appl Microbiol , vol.28 , Issue.3 , pp. 159-163
    • Tuomola, E.M.1    Ouwehand, A.C.2    Salminen, S.J.3
  • 21
    • 0242668278 scopus 로고    scopus 로고
    • An in vitro model for investigating intestinal adhesion of potential dairy propionibacteria probiotic strains using cell line C2BBe1
    • Huang Y., Adams M.C. An in vitro model for investigating intestinal adhesion of potential dairy propionibacteria probiotic strains using cell line C2BBe1. Lett Appl Microbiol 2003, 36(4):213-216.
    • (2003) Lett Appl Microbiol , vol.36 , Issue.4 , pp. 213-216
    • Huang, Y.1    Adams, M.C.2
  • 22
    • 33745806239 scopus 로고    scopus 로고
    • Interaction of bifidobacteria with Caco-2 cells-adhesion and impact on expression profiles
    • Riedel C.U., Foata F., Goldstein D.R., Blum S., Eikmanns B.J. Interaction of bifidobacteria with Caco-2 cells-adhesion and impact on expression profiles. Int J Food Microbiol Jul 1 2006, 110(1):62-68.
    • (2006) Int J Food Microbiol , vol.110 , Issue.1 , pp. 62-68
    • Riedel, C.U.1    Foata, F.2    Goldstein, D.R.3    Blum, S.4    Eikmanns, B.J.5
  • 23
    • 77951574475 scopus 로고    scopus 로고
    • Selection of bifidobacteria based on adhesion and anti-inflammatory capacity in vitro for amelioration of murine colitis
    • Preising J., Philippe D., Gleinser M., Wei H., Blum S., Eikmanns B.J., et al. Selection of bifidobacteria based on adhesion and anti-inflammatory capacity in vitro for amelioration of murine colitis. Appl Environ Microbiol 2010, 76(9):3048-3051.
    • (2010) Appl Environ Microbiol , vol.76 , Issue.9 , pp. 3048-3051
    • Preising, J.1    Philippe, D.2    Gleinser, M.3    Wei, H.4    Blum, S.5    Eikmanns, B.J.6
  • 24
    • 76949107790 scopus 로고    scopus 로고
    • Host interactions of probiotic bacterial surface molecules: comparison with commensals and pathogens
    • Lebeer S., Vanderleyden J., De Keersmaecker S.C. Host interactions of probiotic bacterial surface molecules: comparison with commensals and pathogens. Nat Rev Microbiol Mar 2010, 8(3):171-184.
    • (2010) Nat Rev Microbiol , vol.8 , Issue.3 , pp. 171-184
    • Lebeer, S.1    Vanderleyden, J.2    De Keersmaecker, S.C.3
  • 25
  • 26
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen J.D., Nielsen H., von Heijne G., Brunak S. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol Jul 16 2004, 340(4):783-795.
    • (2004) J Mol Biol , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 27
    • 84858222518 scopus 로고    scopus 로고
    • Protein secretion and surface display in Gram-positive bacteria
    • Schneewind O., Missiakas D.M. Protein secretion and surface display in Gram-positive bacteria. Philos Trans R Soc Lond B Biol Sci Apr 19 2012, 367(1592):1123-1139.
    • (2012) Philos Trans R Soc Lond B Biol Sci , vol.367 , Issue.1592 , pp. 1123-1139
    • Schneewind, O.1    Missiakas, D.M.2
  • 28
    • 59449088232 scopus 로고    scopus 로고
    • Prediction of surface exposed proteins in Streptococcus pyogenes, with a potential application to other Gram-positive bacteria
    • Barinov A., Loux V., Hammani A., Nicolas P., Langella P., Ehrlich D., et al. Prediction of surface exposed proteins in Streptococcus pyogenes, with a potential application to other Gram-positive bacteria. Proteomics Jan 2009, 9(1):61-73.
    • (2009) Proteomics , vol.9 , Issue.1 , pp. 61-73
    • Barinov, A.1    Loux, V.2    Hammani, A.3    Nicolas, P.4    Langella, P.5    Ehrlich, D.6
  • 29
    • 80054010871 scopus 로고    scopus 로고
    • Characterization of adhesive molecule with affinity to Caco-2 cells in Lactobacillus acidophilus by proteome analysis
    • Ashida N., Yanagihara S., Shinoda T., Yamamoto N. Characterization of adhesive molecule with affinity to Caco-2 cells in Lactobacillus acidophilus by proteome analysis. J Biosci Bioeng Oct 2011, 112(4):333-337.
    • (2011) J Biosci Bioeng , vol.112 , Issue.4 , pp. 333-337
    • Ashida, N.1    Yanagihara, S.2    Shinoda, T.3    Yamamoto, N.4
  • 30
    • 58049194098 scopus 로고    scopus 로고
    • S layer protein A of Lactobacillus acidophilus NCFM regulates immature dendritic cell and T cell functions
    • Konstantinov S.R., Smidt H., de Vos W.M., Bruijns S.C., Singh S.K., Valence F., et al. S layer protein A of Lactobacillus acidophilus NCFM regulates immature dendritic cell and T cell functions. Proc Natl Acad Sci U S A Dec 9 2008, 105(49):19474-19479.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.49 , pp. 19474-19479
    • Konstantinov, S.R.1    Smidt, H.2    de Vos, W.M.3    Bruijns, S.C.4    Singh, S.K.5    Valence, F.6
  • 31
    • 0034283014 scopus 로고    scopus 로고
    • Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation
    • Mesnage S., Fontaine T., Mignot T., Delepierre M., Mock M., Fouet A. Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation. EMBO J Sep 1 2000, 19(17):4473-4484.
    • (2000) EMBO J , vol.19 , Issue.17 , pp. 4473-4484
    • Mesnage, S.1    Fontaine, T.2    Mignot, T.3    Delepierre, M.4    Mock, M.5    Fouet, A.6
  • 32
    • 79960383869 scopus 로고    scopus 로고
    • Structure of surface layer homology (SLH) domains from Bacillus anthracis surface array protein
    • Kern J., Wilton R., Zhang R., Binkowski T.A., Joachimiak A., Schneewind O. Structure of surface layer homology (SLH) domains from Bacillus anthracis surface array protein. J Biol Chem Jul 22 2011, 286(29):26042-26049.
    • (2011) J Biol Chem , vol.286 , Issue.29 , pp. 26042-26049
    • Kern, J.1    Wilton, R.2    Zhang, R.3    Binkowski, T.A.4    Joachimiak, A.5    Schneewind, O.6
  • 33
    • 32344453260 scopus 로고    scopus 로고
    • Characterization and identification of vaccine candidate proteins through analysis of the group A Streptococcus surface proteome
    • Rodriguez-Ortega M.J., Norais N., Bensi G., Liberatori S., Capo S., Mora M., et al. Characterization and identification of vaccine candidate proteins through analysis of the group A Streptococcus surface proteome. Nat Biotechnol Feb 2006, 24(2):191-197.
    • (2006) Nat Biotechnol , vol.24 , Issue.2 , pp. 191-197
    • Rodriguez-Ortega, M.J.1    Norais, N.2    Bensi, G.3    Liberatori, S.4    Capo, S.5    Mora, M.6
  • 34
    • 84862330001 scopus 로고    scopus 로고
    • Multi high-throughput approach for highly selective identification of vaccine candidates: the Group A Streptococcus case
    • Bensi G., Mora M., Tuscano G., Biagini M., Chiarot E., Bombaci M., et al. Multi high-throughput approach for highly selective identification of vaccine candidates: the Group A Streptococcus case. Mol Cell Proteomics Jun 2012, 11(6):M111.
    • (2012) Mol Cell Proteomics , vol.11 , Issue.6 , pp. M111
    • Bensi, G.1    Mora, M.2    Tuscano, G.3    Biagini, M.4    Chiarot, E.5    Bombaci, M.6
  • 35
    • 84869204697 scopus 로고    scopus 로고
    • Proteomic and transcriptomic profiling of Staphylococcus aureus surface LPXTG-proteins: correlation with agr genotypes and adherence phenotypes
    • Ythier M., Resch G., Waridel P., Panchaud A., Gfeller A., Majcherczyk P., et al. Proteomic and transcriptomic profiling of Staphylococcus aureus surface LPXTG-proteins: correlation with agr genotypes and adherence phenotypes. Mol Cell Proteomics Nov 2012, 11(11):1123-1139.
    • (2012) Mol Cell Proteomics , vol.11 , Issue.11 , pp. 1123-1139
    • Ythier, M.1    Resch, G.2    Waridel, P.3    Panchaud, A.4    Gfeller, A.5    Majcherczyk, P.6
  • 37
    • 84884747785 scopus 로고    scopus 로고
    • The cold-shock RNA binding protein CspR is also exposed to the surface of Enterococcus faecalis
    • Michaux C., Romero Saavedra L.F., Reffuveille F., Bernay B., Goux D., Hartke A., et al. The cold-shock RNA binding protein CspR is also exposed to the surface of Enterococcus faecalis. Microbiology Aug 16 2013, 159:2153-2161.
    • (2013) Microbiology , vol.159 , pp. 2153-2161
    • Michaux, C.1    Romero Saavedra, L.F.2    Reffuveille, F.3    Bernay, B.4    Goux, D.5    Hartke, A.6
  • 38
    • 79953189726 scopus 로고    scopus 로고
    • Identification of candidate carrier proteins for surface display on Lactococcus lactis by theoretical and experimental analyses of the surface proteome
    • Berlec A., Zadravec P., Jevnikar Z., Strukelj B. Identification of candidate carrier proteins for surface display on Lactococcus lactis by theoretical and experimental analyses of the surface proteome. Appl Environ Microbiol Feb 2011, 77(4):1292-1300.
    • (2011) Appl Environ Microbiol , vol.77 , Issue.4 , pp. 1292-1300
    • Berlec, A.1    Zadravec, P.2    Jevnikar, Z.3    Strukelj, B.4
  • 39
    • 32144456800 scopus 로고    scopus 로고
    • DIGE compatible labeling of surface proteins on vital cells in vitro and in vivo
    • Mayrhofer C., Krieger S., Allmaier G., Kerjaschki D. DIGE compatible labeling of surface proteins on vital cells in vitro and in vivo. Proteomics Jan 2006, 6(2):579-585.
    • (2006) Proteomics , vol.6 , Issue.2 , pp. 579-585
    • Mayrhofer, C.1    Krieger, S.2    Allmaier, G.3    Kerjaschki, D.4
  • 41
    • 33746920166 scopus 로고    scopus 로고
    • Lipolysis during ripening of Emmental cheese considering organization of fat and preferential localization of bacteria
    • Lopez C., Maillard M.B., Briard-Bion V., Camier B., Hannon J.A. Lipolysis during ripening of Emmental cheese considering organization of fat and preferential localization of bacteria. J Agric Food Chem Aug 9 2006, 54(16):5855-5867.
    • (2006) J Agric Food Chem , vol.54 , Issue.16 , pp. 5855-5867
    • Lopez, C.1    Maillard, M.B.2    Briard-Bion, V.3    Camier, B.4    Hannon, J.A.5
  • 42
    • 84861759933 scopus 로고    scopus 로고
    • Interactions between probiotic dairy propionibacteria and the intestinal epithelium
    • Cousin F.J., Deutsch S.M., Perez Chaia A., Foligné B., Jan G. Interactions between probiotic dairy propionibacteria and the intestinal epithelium. Curr Immunol Rev 2012, 8(3):216-226.
    • (2012) Curr Immunol Rev , vol.8 , Issue.3 , pp. 216-226
    • Cousin, F.J.1    Deutsch, S.M.2    Perez Chaia, A.3    Foligné, B.4    Jan, G.5
  • 43
    • 0035994483 scopus 로고    scopus 로고
    • In vitro adhesion of propionic acid bacteria to human intestinal mucus
    • Ouwehand A.C., Suomalainen T., Tolkko S., Salminen S. In vitro adhesion of propionic acid bacteria to human intestinal mucus. Lait 2002, 82(1):123-130.
    • (2002) Lait , vol.82 , Issue.1 , pp. 123-130
    • Ouwehand, A.C.1    Suomalainen, T.2    Tolkko, S.3    Salminen, S.4
  • 44
    • 0032377501 scopus 로고    scopus 로고
    • Effect of NaCl content on lactate fermentation by Propionibacterium freudenreichii in small scale Swiss-type cheeses
    • Richoux R., Faivre E., Kerjean J.R. Effect of NaCl content on lactate fermentation by Propionibacterium freudenreichii in small scale Swiss-type cheeses. Lait 1998, 78(3):319-331.
    • (1998) Lait , vol.78 , Issue.3 , pp. 319-331
    • Richoux, R.1    Faivre, E.2    Kerjean, J.R.3
  • 45
    • 2942707361 scopus 로고    scopus 로고
    • Isovaleric acid is mainly produced by Propionibacterium freudenreichii in Swiss cheese
    • Thierry A., Richoux R., Kerjean J.R. Isovaleric acid is mainly produced by Propionibacterium freudenreichii in Swiss cheese. Int Dairy J 2004, 14(9):801-807.
    • (2004) Int Dairy J , vol.14 , Issue.9 , pp. 801-807
    • Thierry, A.1    Richoux, R.2    Kerjean, J.R.3
  • 46
    • 33746809569 scopus 로고    scopus 로고
    • AGMIAL: implementing an annotation strategy for prokaryote genomes as a distributed system
    • Bryson K., Loux V., Bossy R., Nicolas P., Chaillou S., van de Guchte M., et al. AGMIAL: implementing an annotation strategy for prokaryote genomes as a distributed system. Nucleic Acids Res 2006, 34(12):3533-3545.
    • (2006) Nucleic Acids Res , vol.34 , Issue.12 , pp. 3533-3545
    • Bryson, K.1    Loux, V.2    Bossy, R.3    Nicolas, P.4    Chaillou, S.5    van de Guchte, M.6
  • 47
    • 84865127914 scopus 로고    scopus 로고
    • Assessment of the probiotic potential of a dairy product fermented by Propionibacterium freudenreichii in piglets
    • Cousin F.J., Foligne B., Deutsch S.M., Massart S., Parayre S., Le Loir Y., et al. Assessment of the probiotic potential of a dairy product fermented by Propionibacterium freudenreichii in piglets. J Agric Food Chem Aug 15 2012, 60(32):7917-7927.
    • (2012) J Agric Food Chem , vol.60 , Issue.32 , pp. 7917-7927
    • Cousin, F.J.1    Foligne, B.2    Deutsch, S.M.3    Massart, S.4    Parayre, S.5    Le Loir, Y.6
  • 48
    • 0014353905 scopus 로고
    • An evaluation of the taxonomy of Propionibacterium
    • Malik A.C., Reinbold G.W., Vedamuthu E.R. An evaluation of the taxonomy of Propionibacterium. Can J Microbiol 1968, 14:1185-1191.
    • (1968) Can J Microbiol , vol.14 , pp. 1185-1191
    • Malik, A.C.1    Reinbold, G.W.2    Vedamuthu, E.R.3
  • 49
    • 84915791825 scopus 로고    scopus 로고
    • Permanent draft genome of the probiotic strain Propionibacterium freudenreichii CIRM-BIA 129 (ITG P20)
    • (Submitted for publication)
    • Falentin H., Deutsch S.M., Loux V., Hammani A., Buratti J., Parayre S., et al. Permanent draft genome of the probiotic strain Propionibacterium freudenreichii CIRM-BIA 129 (ITG P20). Stand Genomic Sci 2014, (Submitted for publication).
    • (2014) Stand Genomic Sci
    • Falentin, H.1    Deutsch, S.M.2    Loux, V.3    Hammani, A.4    Buratti, J.5    Parayre, S.6
  • 51
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature Aug 15 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 52
    • 0031725571 scopus 로고    scopus 로고
    • Autolysis of Lactobacillus helveticus and Propionibacterium freudenreichii in Swiss cheeses: first evidence by using species-specific lysis markers
    • Valence F., Richoux R., Thierry D., Palva A., Lortal S. Autolysis of Lactobacillus helveticus and Propionibacterium freudenreichii in Swiss cheeses: first evidence by using species-specific lysis markers. J Dairy Res 1998, 65(4):609-620.
    • (1998) J Dairy Res , vol.65 , Issue.4 , pp. 609-620
    • Valence, F.1    Richoux, R.2    Thierry, D.3    Palva, A.4    Lortal, S.5
  • 53
    • 67650770057 scopus 로고    scopus 로고
    • A toolbox for validation of mass spectrometry peptides identification and generation of database: IRMa
    • Dupierris V., Masselon C., Court M., Kieffer-Jaquinod S., Bruley C. A toolbox for validation of mass spectrometry peptides identification and generation of database: IRMa. Bioinformatics Aug 1 2009, 25(15):1980-1981.
    • (2009) Bioinformatics , vol.25 , Issue.15 , pp. 1980-1981
    • Dupierris, V.1    Masselon, C.2    Court, M.3    Kieffer-Jaquinod, S.4    Bruley, C.5
  • 54
    • 80055120646 scopus 로고    scopus 로고
    • Selective labeling of cell-surface proteins using CyDye DIGE Fluor minimal dyes
    • Hagner-McWhirter A., Winkvist M., Bourin S., Marouga R. Selective labeling of cell-surface proteins using CyDye DIGE Fluor minimal dyes. J Vis Exp 2008, 21.
    • (2008) J Vis Exp , vol.21
    • Hagner-McWhirter, A.1    Winkvist, M.2    Bourin, S.3    Marouga, R.4
  • 55
    • 33645902169 scopus 로고    scopus 로고
    • Changes in protein synthesis during thermal adaptation of Propionibacterium freudenreichii subsp. shermanii
    • Anastasiou R., Leverrier P., Krestas I., Rouault A., Kalantzopoulos G., Boyaval P., et al. Changes in protein synthesis during thermal adaptation of Propionibacterium freudenreichii subsp. shermanii. Int J Food Microbiol Feb 10 2006, 108(3):301-314.
    • (2006) Int J Food Microbiol , vol.108 , Issue.3 , pp. 301-314
    • Anastasiou, R.1    Leverrier, P.2    Krestas, I.3    Rouault, A.4    Kalantzopoulos, G.5    Boyaval, P.6
  • 56
    • 0001092477 scopus 로고    scopus 로고
    • Nanoelectrospray tandem mass spectrometry and sequence similarity searching for identification of proteins from organisms with unknown genomes
    • Shevchenko A., Sunyaev S., Liska A., Bork P., Shevchenko A. Nanoelectrospray tandem mass spectrometry and sequence similarity searching for identification of proteins from organisms with unknown genomes. Methods Mol Biol 2003, 211:221-234.
    • (2003) Methods Mol Biol , vol.211 , pp. 221-234
    • Shevchenko, A.1    Sunyaev, S.2    Liska, A.3    Bork, P.4    Shevchenko, A.5
  • 57
    • 33846940786 scopus 로고    scopus 로고
    • Correlation between in vitro and in vivo immunomodulatory properties of lactic acid bacteria
    • Foligné B., Nutten S., Grangette C., Dennin V., Goudercourt D., Poiret S., et al. Correlation between in vitro and in vivo immunomodulatory properties of lactic acid bacteria. World J Gastroenterol Jan 14 2007, 13(2):236-243.
    • (2007) World J Gastroenterol , vol.13 , Issue.2 , pp. 236-243
    • Foligné, B.1    Nutten, S.2    Grangette, C.3    Dennin, V.4    Goudercourt, D.5    Poiret, S.6
  • 58
    • 84862183876 scopus 로고    scopus 로고
    • Improved adhesive properties of recombinant bifidobacteria expressing the Bifidobacterium bifidum-specific lipoprotein BopA
    • Gleinser M., Grimm V., Zhurina D., Yuan J., Riedel C.U. Improved adhesive properties of recombinant bifidobacteria expressing the Bifidobacterium bifidum-specific lipoprotein BopA. Microb Cell Fact 2012, 11:80.
    • (2012) Microb Cell Fact , vol.11 , pp. 80
    • Gleinser, M.1    Grimm, V.2    Zhurina, D.3    Yuan, J.4    Riedel, C.U.5
  • 59
    • 57349109968 scopus 로고    scopus 로고
    • Genes and molecules of lactobacilli supporting probiotic action
    • Lebeer S., Vanderleyden J., De Keersmaecker S.C. Genes and molecules of lactobacilli supporting probiotic action. Microbiol Mol Biol Rev Dec 2008, 72(4):728-764.
    • (2008) Microbiol Mol Biol Rev , vol.72 , Issue.4 , pp. 728-764
    • Lebeer, S.1    Vanderleyden, J.2    De Keersmaecker, S.C.3
  • 60
    • 84892874899 scopus 로고    scopus 로고
    • Surfomics: shaving live organisms for a fast proteomic identification of surface proteins
    • Olaya-Abril A., Jimenez-Munguia I., Gomez-Gascon L., Rodriguez-Ortega M.J. Surfomics: shaving live organisms for a fast proteomic identification of surface proteins. J Proteome Apr 26 2014, 97:164-176.
    • (2014) J Proteome , vol.97 , pp. 164-176
    • Olaya-Abril, A.1    Jimenez-Munguia, I.2    Gomez-Gascon, L.3    Rodriguez-Ortega, M.J.4
  • 61
    • 84886652105 scopus 로고    scopus 로고
    • Identification of extracellular surface-layer associated proteins in Lactobacillus acidophilus NCFM
    • Johnson B., Selle K., O'Flaherty S., Goh Y.J., Klaenhammer T. Identification of extracellular surface-layer associated proteins in Lactobacillus acidophilus NCFM. Microbiology Nov 2013, 159(Pt 11):2269-2282.
    • (2013) Microbiology , vol.159 , pp. 2269-2282
    • Johnson, B.1    Selle, K.2    O'Flaherty, S.3    Goh, Y.J.4    Klaenhammer, T.5
  • 62
    • 84893780545 scopus 로고    scopus 로고
    • Impact of actin on adhesion and translocation of Enterococcus faecalis
    • Peng Z., Krey V., Wei H., Tan Q., Vogelmann R., Ehrmann M.A., et al. Impact of actin on adhesion and translocation of Enterococcus faecalis. Arch Microbiol Dec 21 2013, 196:109-117.
    • (2013) Arch Microbiol , vol.196 , pp. 109-117
    • Peng, Z.1    Krey, V.2    Wei, H.3    Tan, Q.4    Vogelmann, R.5    Ehrmann, M.A.6
  • 63
    • 84861653144 scopus 로고    scopus 로고
    • Lactobacillaceae and cell adhesion: genomic and functional screening
    • Turpin W., Humblot C., Noordine M.L., Thomas M., Guyot J.P. Lactobacillaceae and cell adhesion: genomic and functional screening. PLoS ONE 2012, 7(5):e38034.
    • (2012) PLoS ONE , vol.7 , Issue.5 , pp. e38034
    • Turpin, W.1    Humblot, C.2    Noordine, M.L.3    Thomas, M.4    Guyot, J.P.5
  • 64
    • 84880580463 scopus 로고    scopus 로고
    • The expression of adhesin EF-Tu in response to mucin and its role in Lactobacillus adhesion and competitive inhibition of enteropathogens to mucin
    • Dhanani A.S., Bagchi T. The expression of adhesin EF-Tu in response to mucin and its role in Lactobacillus adhesion and competitive inhibition of enteropathogens to mucin. J Appl Microbiol Aug 2013, 115(2):546-554.
    • (2013) J Appl Microbiol , vol.115 , Issue.2 , pp. 546-554
    • Dhanani, A.S.1    Bagchi, T.2
  • 65
    • 38649114046 scopus 로고    scopus 로고
    • Analysis of host-inducing proteome changes in Bifidobacterium longum NCC2705 grown in vivo
    • Yuan J., Wang B., Sun Z., Bo X., Yuan X., He X., et al. Analysis of host-inducing proteome changes in Bifidobacterium longum NCC2705 grown in vivo. J Proteome Res Jan 2008, 7(1):375-385.
    • (2008) J Proteome Res , vol.7 , Issue.1 , pp. 375-385
    • Yuan, J.1    Wang, B.2    Sun, Z.3    Bo, X.4    Yuan, X.5    He, X.6
  • 66
    • 34648825063 scopus 로고    scopus 로고
    • Lactococcus lactis gene yjgB encodes a gamma-d-glutaminyl-l-lysyl-endopeptidase which hydrolyzes peptidoglycan
    • Redko Y., Courtin P., Mezange C., Huard C., Chapot-Chartier M.P. Lactococcus lactis gene yjgB encodes a gamma-d-glutaminyl-l-lysyl-endopeptidase which hydrolyzes peptidoglycan. Appl Environ Microbiol Sep 2007, 73(18):5825-5831.
    • (2007) Appl Environ Microbiol , vol.73 , Issue.18 , pp. 5825-5831
    • Redko, Y.1    Courtin, P.2    Mezange, C.3    Huard, C.4    Chapot-Chartier, M.P.5
  • 67
    • 84875023105 scopus 로고    scopus 로고
    • Phenotypic characterization of the foldase homologue PrsA in Streptococcus mutans
    • Guo L., Wu T., Hu W., He X., Sharma S., Webster P., et al. Phenotypic characterization of the foldase homologue PrsA in Streptococcus mutans. Mol Oral Microbiol Apr 2013, 28(2):154-165.
    • (2013) Mol Oral Microbiol , vol.28 , Issue.2 , pp. 154-165
    • Guo, L.1    Wu, T.2    Hu, W.3    He, X.4    Sharma, S.5    Webster, P.6
  • 68
    • 80052329723 scopus 로고    scopus 로고
    • Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease
    • Henderson B., Martin A. Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease. Infect Immun Sep 2011, 79(9):3476-3491.
    • (2011) Infect Immun , vol.79 , Issue.9 , pp. 3476-3491
    • Henderson, B.1    Martin, A.2
  • 70
    • 80053578297 scopus 로고    scopus 로고
    • Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis
    • Yang C.K., Ewis H.E., Zhang X., Lu C.D., Hu H.J., Pan Y., et al. Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis. J Bacteriol Oct 2011, 193(20):5607-5615.
    • (2011) J Bacteriol , vol.193 , Issue.20 , pp. 5607-5615
    • Yang, C.K.1    Ewis, H.E.2    Zhang, X.3    Lu, C.D.4    Hu, H.J.5    Pan, Y.6
  • 71
    • 84877854477 scopus 로고    scopus 로고
    • Staphylococcus aureus extracellular vesicles carry biologically active beta-lactamase
    • Lee J., Lee E.Y., Kim S.H., Kim D.K., Park K.S., Kim K.P., et al. Staphylococcus aureus extracellular vesicles carry biologically active beta-lactamase. Antimicrob Agents Chemother Jun 2013, 57(6):2589-2595.
    • (2013) Antimicrob Agents Chemother , vol.57 , Issue.6 , pp. 2589-2595
    • Lee, J.1    Lee, E.Y.2    Kim, S.H.3    Kim, D.K.4    Park, K.S.5    Kim, K.P.6
  • 72
    • 84899486231 scopus 로고    scopus 로고
    • An internal hydrophobic helical domain of Bacillus subtilis enolase is essential but not sufficient as a non-cleavable signal for its secretion
    • Yang C.K., Zhang X.Z., Lu C.D., Tai P.C. An internal hydrophobic helical domain of Bacillus subtilis enolase is essential but not sufficient as a non-cleavable signal for its secretion. Biochem Biophys Res Commun Mar 15 2014, 446:901-905.
    • (2014) Biochem Biophys Res Commun , vol.446 , pp. 901-905
    • Yang, C.K.1    Zhang, X.Z.2    Lu, C.D.3    Tai, P.C.4
  • 73
    • 83655163906 scopus 로고    scopus 로고
    • The genome sequence of the lactic acid bacterium, Carnobacterium maltaromaticum ATCC 35586 encodes potential virulence factors
    • Leisner J.J., Hansen M.A., Larsen M.H., Hansen L., Ingmer H., Sorensen S.J. The genome sequence of the lactic acid bacterium, Carnobacterium maltaromaticum ATCC 35586 encodes potential virulence factors. Int J Food Microbiol Jan 16 2012, 152(3):107-115.
    • (2012) Int J Food Microbiol , vol.152 , Issue.3 , pp. 107-115
    • Leisner, J.J.1    Hansen, M.A.2    Larsen, M.H.3    Hansen, L.4    Ingmer, H.5    Sorensen, S.J.6
  • 74
    • 49449116100 scopus 로고    scopus 로고
    • Implication of an outer surface lipoprotein in adhesion of Bifidobacterium bifidum to Caco-2 cells
    • Guglielmetti S., Tamagnini I., Mora D., Minuzzo M., Scarafoni A., Arioli S., et al. Implication of an outer surface lipoprotein in adhesion of Bifidobacterium bifidum to Caco-2 cells. Appl Environ Microbiol Aug 2008, 74(15):4695-4702.
    • (2008) Appl Environ Microbiol , vol.74 , Issue.15 , pp. 4695-4702
    • Guglielmetti, S.1    Tamagnini, I.2    Mora, D.3    Minuzzo, M.4    Scarafoni, A.5    Arioli, S.6
  • 75
    • 46449125693 scopus 로고    scopus 로고
    • The surface-exposed carboxyl region of Mycoplasma pneumoniae elongation factor Tu interacts with fibronectin
    • Balasubramanian S., Kannan T.R., Baseman J.B. The surface-exposed carboxyl region of Mycoplasma pneumoniae elongation factor Tu interacts with fibronectin. Infect Immun Jul 2008, 76(7):3116-3123.
    • (2008) Infect Immun , vol.76 , Issue.7 , pp. 3116-3123
    • Balasubramanian, S.1    Kannan, T.R.2    Baseman, J.B.3
  • 76
    • 80052466465 scopus 로고    scopus 로고
    • Lactobacillus plantarum surface layer adhesive protein protects intestinal epithelial cells against tight junction injury induced by enteropathogenic Escherichia coli
    • Liu Z., Shen T., Zhang P., Ma Y., Qin H. Lactobacillus plantarum surface layer adhesive protein protects intestinal epithelial cells against tight junction injury induced by enteropathogenic Escherichia coli. Mol Biol Rep Jun 2011, 38(5):3471-3480.
    • (2011) Mol Biol Rep , vol.38 , Issue.5 , pp. 3471-3480
    • Liu, Z.1    Shen, T.2    Zhang, P.3    Ma, Y.4    Qin, H.5
  • 77
    • 84874733256 scopus 로고    scopus 로고
    • S-layer protein mediates the stimulatory effect of Lactobacillus helveticus MIMLh5 on innate immunity
    • Taverniti V., Stuknyte M., Minuzzo M., Arioli S., De Noni I., Scabiosi C., et al. S-layer protein mediates the stimulatory effect of Lactobacillus helveticus MIMLh5 on innate immunity. Appl Environ Microbiol Feb 2013, 79(4):1221-1231.
    • (2013) Appl Environ Microbiol , vol.79 , Issue.4 , pp. 1221-1231
    • Taverniti, V.1    Stuknyte, M.2    Minuzzo, M.3    Arioli, S.4    De Noni, I.5    Scabiosi, C.6


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