메뉴 건너뛰기




Volumn 74, Issue 1, 2006, Pages 425-434

GroEL of Lactobacillus johnsonii La1 (NCC 533) is cell surface associated: Potential role in interactions with the host and the gastric pathogen Helicobacter pylori

Author keywords

[No Author keywords available]

Indexed keywords

CD14 ANTIGEN; CELL SURFACE PROTEIN; CHAPERONIN; HEAT SHOCK PROTEIN 60; INTERLEUKIN 8; MUCIN; PROBIOTIC AGENT; RECOMBINANT PROTEIN;

EID: 29644437923     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.74.1.425-434.2006     Document Type: Article
Times cited : (244)

References (57)
  • 4
    • 0026663088 scopus 로고
    • Adhesion of human Lactobacillus acidophilus strain LB to human enterocyte-like Caco-2 cells
    • Chauviere, G., M. H. Coconnier, S. Kerneis, J. Fourniat, and A. L. Servin. 1992. Adhesion of human Lactobacillus acidophilus strain LB to human enterocyte-like Caco-2 cells. J. Gen. Microbiol. 138:1689-1696.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1689-1696
    • Chauviere, G.1    Coconnier, M.H.2    Kerneis, S.3    Fourniat, J.4    Servin, A.L.5
  • 5
    • 0026747726 scopus 로고
    • Protein-mediated adhesion of Lactobacillus acidophilus BG2FO4 on human enterocyte and mucus-secreting cell lines in culture
    • Coconnier, M.-H., T. R. Klaenhammer, S. Kernéis, M.-F. Bernet, and A. L. Servin. 1992. Protein-mediated adhesion of Lactobacillus acidophilus BG2FO4 on human enterocyte and mucus-secreting cell lines in culture. Appl. Environ. Microbiol. 58:2034-2039.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2034-2039
    • Coconnier, M.-H.1    Klaenhammer, T.R.2    Kernéis, S.3    Bernet, M.-F.4    Servin, A.L.5
  • 6
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402-414.
    • (1993) Microbiol. Rev. , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 7
    • 0033972192 scopus 로고    scopus 로고
    • Effects of probiotic bacteria on diarrhea, lipid metabolism, and carcinogenesis: A review of papers published between 1988 and 1998
    • de Roos, N. M., and M. B. Katan. 2000. Effects of probiotic bacteria on diarrhea, lipid metabolism, and carcinogenesis: a review of papers published between 1988 and 1998. Am. J. Clin. Nutr. 71:405-411.
    • (2000) Am. J. Clin. Nutr. , vol.71 , pp. 405-411
    • Roos, N.M.1    Katan, M.B.2
  • 9
    • 0026642506 scopus 로고
    • A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus
    • Ensgraber, M., and M. Loos. 1992. A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus. Infect. Immun. 60:3072-3078.
    • (1992) Infect. Immun. , vol.60 , pp. 3072-3078
    • Ensgraber, M.1    Loos, M.2
  • 10
    • 0031888740 scopus 로고    scopus 로고
    • GroEL heat shock protein of Haemophilus ducreyi: Association with cell surface and capacity to bind to eukaryotic cells
    • Frisk, A., C. A. Ison, and T. Lagergård. 1998. GroEL heat shock protein of Haemophilus ducreyi: association with cell surface and capacity to bind to eukaryotic cells. Infect. Immun. 66:1252-1257.
    • (1998) Infect. Immun. , vol.66 , pp. 1252-1257
    • Frisk, A.1    Ison, C.A.2    Lagergård, T.3
  • 12
    • 0020600404 scopus 로고
    • Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing
    • Gasson, M. J. 1983. Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing. J. Bacteriol. 154:1-9.
    • (1983) J. Bacteriol. , vol.154 , pp. 1-9
    • Gasson, M.J.1
  • 13
    • 0021759116 scopus 로고
    • 2-terminal of lipoprotein are sufficient for its modification, processing, and localization in the outer membrane of Escherichia coli
    • 2-terminal of lipoprotein are sufficient for its modification, processing, and localization in the outer membrane of Escherichia coli. J. Biol. Chem. 259:463-467.
    • (1984) J. Biol. Chem. , vol.259 , pp. 463-467
    • Ghrayeh, J.1    Inouye, M.2
  • 14
    • 0021887832 scopus 로고
    • Immunochemical characterization of a protein associated with Mycobacterium leprae cell wall
    • Gillis, T. P., R. A. Miller, D. B. Young, S. R. Khanolkar, and T. M. Buchanan. 1985. Immunochemical characterization of a protein associated with Mycobacterium leprae cell wall. Infect. Immun. 49:371-377.
    • (1985) Infect. Immun. , vol.49 , pp. 371-377
    • Gillis, T.P.1    Miller, R.A.2    Young, D.B.3    Khanolkar, S.R.4    Buchanan, T.M.5
  • 15
    • 0345791527 scopus 로고    scopus 로고
    • Helicobacter pylori heat shock protein 60 mediates interleukin-6 production by macrophages via a toll-like receptor (TLR)-2-, TLR-4-, and myeloid differentiation factor 88-independent mechanism
    • Gobert, A. P., J. C. Bambou, C. Werts, V. Balloy, M. Chignard, A. P. Moran, and R. L. Ferrero. 2004. Helicobacter pylori heat shock protein 60 mediates interleukin-6 production by macrophages via a toll-like receptor (TLR)-2-, TLR-4-, and myeloid differentiation factor 88-independent mechanism. J. Biol. Chem. 279:245-250.
    • (2004) J. Biol. Chem. , vol.279 , pp. 245-250
    • Gobert, A.P.1    Bambou, J.C.2    Werts, C.3    Balloy, V.4    Chignard, M.5    Moran, A.P.6    Ferrero, R.L.7
  • 16
    • 1842431723 scopus 로고    scopus 로고
    • Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins
    • Granato, D., G. E. Bergonzelli, R. D. Pridmore, L. Marvin, M. Rouvet, and I. E. Corthésy-Theulaz. 2004. Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins. Infect. Immun. 72:2160-2169.
    • (2004) Infect. Immun. , vol.72 , pp. 2160-2169
    • Granato, D.1    Bergonzelli, G.E.2    Pridmore, R.D.3    Marvin, L.4    Rouvet, M.5    Corthésy-Theulaz, I.E.6
  • 17
    • 0033019689 scopus 로고    scopus 로고
    • Cell surface-associated lipoteichoic acid acts as an adhesion factor for attachment of Lactobacillus johnsonii La1 to human enterocyte-like Caco-2 cells
    • Granato, D., F. Perotti, I. Masserey, M. Rouvet, M. Golliard, A. Servin, and D. Brassart. 1999. Cell surface-associated lipoteichoic acid acts as an adhesion factor for attachment of Lactobacillus johnsonii La1 to human enterocyte-like Caco-2 cells. Appl. Environ. Microbiol. 65:1071-1077.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1071-1077
    • Granato, D.1    Perotti, F.2    Masserey, I.3    Rouvet, M.4    Golliard, M.5    Servin, A.6    Brassart, D.7
  • 18
    • 0027947440 scopus 로고
    • Factors involved in adherence of lactobacilli to human Caco-2 cells
    • Greene, J. D., and T. R. Klaenhammer. 1994. Factors involved in adherence of lactobacilli to human Caco-2 cells. Appl. Environ. Microbiol. 60:4487-4494.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4487-4494
    • Greene, J.D.1    Klaenhammer, T.R.2
  • 19
    • 0028960169 scopus 로고
    • Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells
    • Gupta, R. S. 1995. Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells. Mol. Microbiol. 15:1-11.
    • (1995) Mol. Microbiol. , vol.15 , pp. 1-11
    • Gupta, R.S.1
  • 20
    • 0027203858 scopus 로고
    • TnMax-a versatile mini-transposon for the analysis of cloned genes and shuttle mutagenesis
    • Haas, R., A. F. Kahrs, D. Facius, H. Allmeier, R. Schmitt, and T. F. Meyer. 1993. TnMax-a versatile mini-transposon for the analysis of cloned genes and shuttle mutagenesis. Gene 130:23-31.
    • (1993) Gene , vol.130 , pp. 23-31
    • Haas, R.1    Kahrs, A.F.2    Facius, D.3    Allmeier, H.4    Schmitt, R.5    Meyer, T.F.6
  • 21
    • 0037413845 scopus 로고    scopus 로고
    • Different heat shock protein 60 species share pro-inflammatory activity but not binding sites on macrophages
    • Habich, C., K. Kempe, R. van der Zee, V. Burkart, and H. Kolb. 2003. Different heat shock protein 60 species share pro-inflammatory activity but not binding sites on macrophages. FEBS Lett. 533:105-109.
    • (2003) FEBS Lett. , vol.533 , pp. 105-109
    • Habich, C.1    Kempe, K.2    Van Der Zee, R.3    Burkart, V.4    Kolb, H.5
  • 22
    • 0002647979 scopus 로고    scopus 로고
    • Non-pathogenic bacteria elicit a differential cytokine response by intestinal epithelial cell/leucocyte co-cultures
    • Haller, D., C. Bode, W. P. Hammes, A. M. Pfeifer, E. J. Schiffrin, and S. Blum. 2000. Non-pathogenic bacteria elicit a differential cytokine response by intestinal epithelial cell/leucocyte co-cultures. Gut 47:79-87.
    • (2000) Gut , vol.47 , pp. 79-87
    • Haller, D.1    Bode, C.2    Hammes, W.P.3    Pfeifer, A.M.4    Schiffrin, E.J.5    Blum, S.6
  • 23
    • 0021249121 scopus 로고
    • Simple method for development of sensitive and specific antiinsulin antisera for laboratory use
    • Havrankova, J., and J. L. Petit. 1984. Simple method for development of sensitive and specific antiinsulin antisera for laboratory use. J. Immunoassay 5:131-144.
    • (1984) J. Immunoassay , vol.5 , pp. 131-144
    • Havrankova, J.1    Petit, J.L.2
  • 25
    • 0032909564 scopus 로고    scopus 로고
    • Surface-associated heat shock proteins of Legionella pneumophila and Helicobacter pylori: Roles in pathogenesis and immunity
    • Hoffman, P. S., and R. A. Garduno. 1999. Surface-associated heat shock proteins of Legionella pneumophila and Helicobacter pylori: roles in pathogenesis and immunity. Infect. Dis. Obstet. Gynecol. 7:58-63.
    • (1999) Infect. Dis. Obstet. Gynecol. , vol.7 , pp. 58-63
    • Hoffman, P.S.1    Garduno, R.A.2
  • 26
    • 0033946528 scopus 로고    scopus 로고
    • Adherence of Lactobacillus to intestinal 407 cells in culture correlates with fibronectin binding
    • Kapczynski, D. R., R. J. Meinersmann, and M. D. Lee. 2000. Adherence of Lactobacillus to intestinal 407 cells in culture correlates with fibronectin binding. Curr. Microbiol. 41:136-141.
    • (2000) Curr. Microbiol. , vol.41 , pp. 136-141
    • Kapczynski, D.R.1    Meinersmann, R.J.2    Lee, M.D.3
  • 28
    • 0033019732 scopus 로고    scopus 로고
    • Subcellular fractionation of group B Streptococcus
    • Kling, D. E., L. C. Madoff, and J. L. Michel. 1999. Subcellular fractionation of group B Streptococcus. BioTechniques 27:24-26, 28.
    • (1999) BioTechniques , vol.27 , pp. 24-26
    • Kling, D.E.1    Madoff, L.C.2    Michel, J.L.3
  • 29
    • 0033557202 scopus 로고    scopus 로고
    • Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages
    • Kol, A., T. Bourcier, A. H. Lichtman, and P. Libby. 1999. Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages. J. Clin. Investig. 103:571-577.
    • (1999) J. Clin. Investig. , vol.103 , pp. 571-577
    • Kol, A.1    Bourcier, T.2    Lichtman, A.H.3    Libby, P.4
  • 30
    • 0033975855 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells
    • Kol, A., A. H. Lichtman, R. W. Finberg, P. Libby, and E. A. Kurt-Jones. 2000. Cutting edge: heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells. J. Immunol. 164:13-17.
    • (2000) J. Immunol. , vol.164 , pp. 13-17
    • Kol, A.1    Lichtman, A.H.2    Finberg, R.W.3    Libby, P.4    Kurt-Jones, E.A.5
  • 32
    • 0025144305 scopus 로고
    • Growth adaptation to methotrexate of HT-29 human colon carcinoma cells is associated with their ability to differentiate into columnar absorptive and mucus-secreting cells
    • Lesuffleur, T., A. Barbat, E. Dussaulx, and A. Zweibaum. 1990. Growth adaptation to methotrexate of HT-29 human colon carcinoma cells is associated with their ability to differentiate into columnar absorptive and mucus-secreting cells. Cancer Res. 50:6334-6343.
    • (1990) Cancer Res. , vol.50 , pp. 6334-6343
    • Lesuffleur, T.1    Barbat, A.2    Dussaulx, E.3    Zweibaum, A.4
  • 33
    • 0036668063 scopus 로고    scopus 로고
    • Characterization of lactosylated proteins of infant formula powders using two-dimensional gel electrophoresis and nanoelectrospray mass spectrometry
    • Marvin, L. F., V. Parisod, L. B. Fay, and P. A. Guy. 2002. Characterization of lactosylated proteins of infant formula powders using two-dimensional gel electrophoresis and nanoelectrospray mass spectrometry. Electrophoresis 23:2505-2512.
    • (2002) Electrophoresis , vol.23 , pp. 2505-2512
    • Marvin, L.F.1    Parisod, V.2    Fay, L.B.3    Guy, P.A.4
  • 34
    • 0033250680 scopus 로고    scopus 로고
    • New binding assay and preparative trial of cell-surface lectin from Lactobacillus acidophilus group lactic acid bacteria
    • Matsumura, A., T. Saito, M. Arakuni, H. Kitazawa, Y. Kawai, and T. Itoh. 1999. New binding assay and preparative trial of cell-surface lectin from Lactobacillus acidophilus group lactic acid bacteria. J. Dairy Sci. 82:2525-2529.
    • (1999) J. Dairy Sci. , vol.82 , pp. 2525-2529
    • Matsumura, A.1    Saito, T.2    Arakuni, M.3    Kitazawa, H.4    Kawai, Y.5    Itoh, T.6
  • 36
    • 0345201644 scopus 로고    scopus 로고
    • Study of adhesion of Lactobacillus casei CRL 431 to ileal intestinal cells of mice
    • Morata de Ambrosini, V., S. N. Gonzalez, and G. Oliver. 1999. Study of adhesion of Lactobacillus casei CRL 431 to ileal intestinal cells of mice. J. Food Prot. 62:1430-1434.
    • (1999) J. Food Prot. , vol.62 , pp. 1430-1434
    • Morata De Ambrosini, V.1    Gonzalez, S.N.2    Oliver, G.3
  • 37
    • 0030978219 scopus 로고    scopus 로고
    • Rapid and sensitive detection of hiochi bacteria by amplification of hiochi bacterial common antigen gene by PCR method and characterization of the antigen
    • Nakamura, J., D. Ito, K. Nagai, Y. Umehara, M. Hamachi, and C. Kumagai. 1997. Rapid and sensitive detection of hiochi bacteria by amplification of hiochi bacterial common antigen gene by PCR method and characterization of the antigen. J. Ferment. Bioeng. 83:161-167.
    • (1997) J. Ferment. Bioeng. , vol.83 , pp. 161-167
    • Nakamura, J.1    Ito, D.2    Nagai, K.3    Umehara, Y.4    Hamachi, M.5    Kumagai, C.6
  • 39
    • 0030021824 scopus 로고    scopus 로고
    • Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis
    • Phadnis, S. H., M. H. Parlow, M. Levy, D. Ilver, C. M. Caulkins, J. B. Connors, and B. E. Dunn. 1996. Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis. Infect. Immun. 64:905-912.
    • (1996) Infect. Immun. , vol.64 , pp. 905-912
    • Phadnis, S.H.1    Parlow, M.H.2    Levy, M.3    Ilver, D.4    Caulkins, C.M.5    Connors, J.B.6    Dunn, B.E.7
  • 40
    • 0035108475 scopus 로고    scopus 로고
    • Association of Lactobacillus spp. with Peyer's patches in mice
    • Plant, L., and P. Conway. 2001. Association of Lactobacillus spp. with Peyer's patches in mice. Clin. Diagn. Lab. Immunol. 8:320-324.
    • (2001) Clin. Diagn. Lab. Immunol. , vol.8 , pp. 320-324
    • Plant, L.1    Conway, P.2
  • 41
    • 0028113172 scopus 로고
    • Bacterial heat shock proteins directly induce cytokine mRNA and interleukin-1 secretion in macrophage cultures
    • Retzlaff, C., Y. Yamamoto, P. S. Hoffman, H. Friedman, and T. W. Klein. 1994. Bacterial heat shock proteins directly induce cytokine mRNA and interleukin-1 secretion in macrophage cultures. Infect. Immun. 62:5689-5693.
    • (1994) Infect. Immun. , vol.62 , pp. 5689-5693
    • Retzlaff, C.1    Yamamoto, Y.2    Hoffman, P.S.3    Friedman, H.4    Klein, T.W.5
  • 42
    • 0036253495 scopus 로고    scopus 로고
    • Purification and characterization of a surface protein from Lactobacillus fermentum 104R that binds to porcine small intestinal mucus and gastric mucin
    • Rojas, M., F. Ascencio, and P. L. Conway. 2002. Purification and characterization of a surface protein from Lactobacillus fermentum 104R that binds to porcine small intestinal mucus and gastric mucin. Appl. Environ. Microbiol. 68:2330-2336.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2330-2336
    • Rojas, M.1    Ascencio, F.2    Conway, P.L.3
  • 43
    • 0029808626 scopus 로고    scopus 로고
    • Colonization by lactobacilli of piglet small intestinal mucus
    • Rojas, M., and P. L. Conway. 1996. Colonization by lactobacilli of piglet small intestinal mucus. J. Appl. Bacteriol. 81:474-480.
    • (1996) J. Appl. Bacteriol. , vol.81 , pp. 474-480
    • Rojas, M.1    Conway, P.L.2
  • 44
    • 0033972717 scopus 로고    scopus 로고
    • The role of probiotic cultures in the control of gastrointestinal health
    • Rolfe, R. D. 2000. The role of probiotic cultures in the control of gastrointestinal health. J. Nutr. 130:396S-402S.
    • (2000) J. Nutr. , vol.130
    • Rolfe, R.D.1
  • 45
    • 0036181685 scopus 로고    scopus 로고
    • A high-molecular-mass cell-surface protein from Lactobacillus reuteri 1063 adheres to mucus components
    • Roos, S., and H. Jonsson. 2002. A high-molecular-mass cell-surface protein from Lactobacillus reuteri 1063 adheres to mucus components. Microbiology 148:433-442.
    • (2002) Microbiology , vol.148 , pp. 433-442
    • Roos, S.1    Jonsson, H.2
  • 46
    • 7344240408 scopus 로고    scopus 로고
    • Homogeneous Escherichia coli chaperonin 60 induces IL-1 beta and IL-6 gene expression in human monocytes by a mechanism independent of protein conformation
    • Tabona, P., K. Reddi, S. Khan, S. P. Nair, S. J. Crean, S. Meghji, M. Wilson, M. Preuss, A. D. Miller, S. Poole, S. Carne, and B. Henderson. 1998. Homogeneous Escherichia coli chaperonin 60 induces IL-1 beta and IL-6 gene expression in human monocytes by a mechanism independent of protein conformation. J. Immunol. 161:1414-1421.
    • (1998) J. Immunol. , vol.161 , pp. 1414-1421
    • Tabona, P.1    Reddi, K.2    Khan, S.3    Nair, S.P.4    Crean, S.J.5    Meghji, S.6    Wilson, M.7    Preuss, M.8    Miller, A.D.9    Poole, S.10    Carne, S.11    Henderson, B.12
  • 47
    • 1942545081 scopus 로고    scopus 로고
    • Cytokine function of heat shock proteins
    • Tsan, M. F., and B. Gao. 2004. Cytokine function of heat shock proteins. Am. J. Physiol. Cell Physiol. 286:C739-C744.
    • (2004) Am. J. Physiol. Cell Physiol. , vol.286
    • Tsan, M.F.1    Gao, B.2
  • 48
    • 0032983458 scopus 로고    scopus 로고
    • Human ileostomy glycoproteins as a model for small intestinal mucus to investigate adhesion of probiotics
    • Tuomola, E. M., A. C. Ouwehand, and S. J. Salminen. 1999. Human ileostomy glycoproteins as a model for small intestinal mucus to investigate adhesion of probiotics. Lett. Appl. Microbiol. 28:159-163.
    • (1999) Lett. Appl. Microbiol. , vol.28 , pp. 159-163
    • Tuomola, E.M.1    Ouwehand, A.C.2    Salminen, S.J.3
  • 49
    • 0032836635 scopus 로고    scopus 로고
    • The effect of probiotic bacteria on the adhesion of pathogens to human intestinal mucus
    • Tuomola, E. M., A. C. Ouwehand, and S. J. Salminen. 1999. The effect of probiotic bacteria on the adhesion of pathogens to human intestinal mucus. FEMS Immunol. Med. Microbiol. 26:137-142.
    • (1999) FEMS Immunol. Med. Microbiol. , vol.26 , pp. 137-142
    • Tuomola, E.M.1    Ouwehand, A.C.2    Salminen, S.J.3
  • 50
    • 0034666532 scopus 로고    scopus 로고
    • Chemical, physical and enzymatic pre-treatments of probiotic lactobacilli alter their adhesion to human intestinal mucus glycoproteins
    • Tuomola, E. M., A. C. Ouwehand, and S. J. Salminen. 2000. Chemical, physical and enzymatic pre-treatments of probiotic lactobacilli alter their adhesion to human intestinal mucus glycoproteins. Int. J. Food Microbiol. 60:75-81.
    • (2000) Int. J. Food Microbiol. , vol.60 , pp. 75-81
    • Tuomola, E.M.1    Ouwehand, A.C.2    Salminen, S.J.3
  • 51
    • 0032485784 scopus 로고    scopus 로고
    • Adhesion of some probiotic and dairy Lactobacillus strains to Caco-2 cell cultures
    • Tuomola, E. M., and S. J. Salminen. 1998. Adhesion of some probiotic and dairy Lactobacillus strains to Caco-2 cell cultures. Int. J. Food Microbiol. 41:45-51.
    • (1998) Int. J. Food Microbiol. , vol.41 , pp. 45-51
    • Tuomola, E.M.1    Salminen, S.J.2
  • 52
    • 0031911053 scopus 로고    scopus 로고
    • Evidence for specific secretion rather than autolysis in the release of some Helicobacter pylori proteins
    • Vanet, A., and A. Labigne. 1998. Evidence for specific secretion rather than autolysis in the release of some Helicobacter pylori proteins. Infect. Immun. 66:1023-1027.
    • (1998) Infect. Immun. , vol.66 , pp. 1023-1027
    • Vanet, A.1    Labigne, A.2
  • 53
    • 0036128867 scopus 로고    scopus 로고
    • Lipoteichoic acids from Lactobacillus johnsonii strain La1 and Lactobacillus acidophilus strain La10 antagonize the responsiveness of human intestinal epithelial HT29 cells to lipopolysaccharide and gram-negative bacteria
    • Vidal, K., A. Donnet-Hughes, and D. Granato. 2002. Lipoteichoic acids from Lactobacillus johnsonii strain La1 and Lactobacillus acidophilus strain La10 antagonize the responsiveness of human intestinal epithelial HT29 cells to lipopolysaccharide and gram-negative bacteria. Infect. Immun. 70:2057-2064.
    • (2002) Infect. Immun. , vol.70 , pp. 2057-2064
    • Vidal, K.1    Donnet-Hughes, A.2    Granato, D.3
  • 54
    • 0035491061 scopus 로고    scopus 로고
    • Soluble CD14 in human breast milk and its role in innate immune responses
    • Vidal, K., M. O. Labeta, E. J. Schiffrin, and A. Donnet-Hughes. 2001. Soluble CD14 in human breast milk and its role in innate immune responses. Acta Odontol. Scand. 59:330-334.
    • (2001) Acta Odontol. Scand. , vol.59 , pp. 330-334
    • Vidal, K.1    Labeta, M.O.2    Schiffrin, E.J.3    Donnet-Hughes, A.4
  • 56
    • 0032724070 scopus 로고    scopus 로고
    • Induction of secretion of interleukin-8 from human gastric epithelial cells by heat-shock protein 60 homologue of Helicobacter pylori
    • Yamaguchi, H., T. Osaki, N. Kurihara, M. Kitajima, M. Kai, M. Takahashi, H. Taguchi, and S. Kamiya. 1999. Induction of secretion of interleukin-8 from human gastric epithelial cells by heat-shock protein 60 homologue of Helicobacter pylori. J. Med. Microbiol. 48:927-933.
    • (1999) J. Med. Microbiol. , vol.48 , pp. 927-933
    • Yamaguchi, H.1    Osaki, T.2    Kurihara, N.3    Kitajima, M.4    Kai, M.5    Takahashi, M.6    Taguchi, H.7    Kamiya, S.8
  • 57
    • 0030882160 scopus 로고    scopus 로고
    • Heat-shock protein 60 homologue of Helicobacter pylori is associated with adhesion of H. pylori to human gastric epithelial cells
    • Yamaguchi, H., T. Osaki, N. Kurihara, H. Taguchi, T. Hanawa, T. Yamamoto, and S. Kamiya. 1997. Heat-shock protein 60 homologue of Helicobacter pylori is associated with adhesion of H. pylori to human gastric epithelial cells. J. Med. Microbiol. 46:825-831.
    • (1997) J. Med. Microbiol. , vol.46 , pp. 825-831
    • Yamaguchi, H.1    Osaki, T.2    Kurihara, N.3    Taguchi, H.4    Hanawa, T.5    Yamamoto, T.6    Kamiya, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.