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Volumn 155, Issue 8, 2009, Pages 2707-2713

Interaction of triosephosphate isomerase from the cell surface of Staphylococcus aureus and α-(1←3)-mannooligosaccharides derived from glucuronoxylomannan of Cryptococcus neoformans

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA (1-3) MANNOOLIGOSACCHARIDE; GLUCURONOXYLOMANNAN; MANNOSE OLIGOSACCHARIDE; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG;

EID: 69949148010     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.028068-0     Document Type: Article
Times cited : (36)

References (37)
  • 1
    • 35948951215 scopus 로고    scopus 로고
    • Enolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traits
    • Antikainen, J., Kuparinen, V., Lahteenmaki, K. & Korhonen, T. K. (2007). Enolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traits. FEMS Immunol Med Microbiol 51, 526-534.
    • (2007) FEMS Immunol Med Microbiol , vol.51 , pp. 526-534
    • Antikainen, J.1    Kuparinen, V.2    Lahteenmaki, K.3    Korhonen, T.K.4
  • 2
    • 0034931519 scopus 로고    scopus 로고
    • α-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann, S., Rohde, M., Chhatwal, G. S. & Hammerschmidt, S. (2001). α-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol 40, 1273-1287.
    • (2001) Mol Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 3
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein
    • Bergmann, S., Rohde, M. & Hammerschmidt, S. (2004). Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein. Infect Immun 72, 2416-2419.
    • (2004) Infect Immun , vol.72 , pp. 2416-2419
    • Bergmann, S.1    Rohde, M.2    Hammerschmidt, S.3
  • 4
    • 0032825315 scopus 로고    scopus 로고
    • SWEET - WWW-based rapid 3D construction of oligo- and polysaccharides
    • Bohne, A., Lang, E. & von der Lieth, C. W. (1999). SWEET - WWW-based rapid 3D construction of oligo- and polysaccharides. Bioinformatics 15, 767-768.
    • (1999) Bioinformatics , vol.15 , pp. 767-768
    • Bohne, A.1    Lang, E.2    von der Lieth, C.W.3
  • 6
    • 33748413638 scopus 로고    scopus 로고
    • Mannose-binding lectin in innate immunity: Past, present and future
    • Dommett, R. M., Klein, N. & Turner, M. W. (2006). Mannose-binding lectin in innate immunity: past, present and future. Tissue Antigens 68, 193-209.
    • (2006) Tissue Antigens , vol.68 , pp. 193-209
    • Dommett, R.M.1    Klein, N.2    Turner, M.W.3
  • 7
    • 34249332380 scopus 로고    scopus 로고
    • Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: Interaction of the extracellular enzyme with human plasminogen and fibrinogen
    • Egea, L., Aguilera, L., Gimenez, R., Sorolla, M. A., Aguilar, J., Badia, J. & Baldoma, L. (2007). Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: interaction of the extracellular enzyme with human plasminogen and fibrinogen. Int J Biochem Cell Biol 39, 1190-1203.
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 1190-1203
    • Egea, L.1    Aguilera, L.2    Gimenez, R.3    Sorolla, M.A.4    Aguilar, J.5    Badia, J.6    Baldoma, L.7
  • 8
    • 15244357417 scopus 로고    scopus 로고
    • The Staphylococcus aureus "superbug
    • Foster, T. J. (2004). The Staphylococcus aureus "superbug". J Clin Invest 114, 1693-1696.
    • (2004) J Clin Invest , vol.114 , pp. 1693-1696
    • Foster, T.J.1
  • 10
    • 0030789362 scopus 로고    scopus 로고
    • The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen
    • Gil-Navarro, I., Gil, M. L., Casanova, M., O'Connor, J. E., Martinez, J. P. & Gozalbo, D. (1997). The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen. J Bacteriol 179, 4992-4999.
    • (1997) J Bacteriol , vol.179 , pp. 4992-4999
    • Gil-Navarro, I.1    Gil, M.L.2    Casanova, M.3    O'Connor, J.E.4    Martinez, J.P.5    Gozalbo, D.6
  • 11
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. & Peitsch, M. C. (1997). SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 12
    • 0034787277 scopus 로고    scopus 로고
    • Structural studies of a cell wall polysaccharide of Trichosporon asahii containing antigen II
    • Ichikawa, T., Nishikawa, A., Ikeda, R. & Shinoda, T. (2001). Structural studies of a cell wall polysaccharide of Trichosporon asahii containing antigen II. Eur J Biochem 268, 5098-5106.
    • (2001) Eur J Biochem , vol.268 , pp. 5098-5106
    • Ichikawa, T.1    Nishikawa, A.2    Ikeda, R.3    Shinoda, T.4
  • 13
    • 0842330749 scopus 로고    scopus 로고
    • Structural studies of the capsular polysaccharide of a non-neoformans Cryptococcus species identified as C. laurentii, which was reclassified as Cryptococcus flavescens, from a patient with AIDS
    • Ikeda, R. & Maeda, T. (2004). Structural studies of the capsular polysaccharide of a non-neoformans Cryptococcus species identified as C. laurentii, which was reclassified as Cryptococcus flavescens, from a patient with AIDS. Carbohydr Res 339, 503-509.
    • (2004) Carbohydr Res , vol.339 , pp. 503-509
    • Ikeda, R.1    Maeda, T.2
  • 14
    • 56949107774 scopus 로고    scopus 로고
    • 2 stress-induced apoptosis-like events in Cryptococcus neoformans
    • 2 stress-induced apoptosis-like events in Cryptococcus neoformans. Res Microbiol 159, 628-634.
    • (2008) Res Microbiol , vol.159 , pp. 628-634
    • Ikeda, R.1    Sawamura, K.2
  • 15
    • 34347385440 scopus 로고    scopus 로고
    • Contribution of the mannan backbone of cryptococcal glucuronoxylomannan and a glycolytic enzyme of Staphylococcus aureus to contact-mediated killing of Cryptococcus neoformans
    • Ikeda, R., Saito, F., Matsuo, M., Kurokawa, K., Sekimizu, K., Yamaguchi, M. & Kawamoto, S. (2007). Contribution of the mannan backbone of cryptococcal glucuronoxylomannan and a glycolytic enzyme of Staphylococcus aureus to contact-mediated killing of Cryptococcus neoformans. J Bacteriol 189, 4815-4826.
    • (2007) J Bacteriol , vol.189 , pp. 4815-4826
    • Ikeda, R.1    Saito, F.2    Matsuo, M.3    Kurokawa, K.4    Sekimizu, K.5    Yamaguchi, M.6    Kawamoto, S.7
  • 16
    • 19744374524 scopus 로고    scopus 로고
    • Bacterial cell-to-cell signaling in the gastrointestinal tract
    • Kaper, J. B. & Sperandio, V. (2005). Bacterial cell-to-cell signaling in the gastrointestinal tract. Infect Immun 73, 3197-3209.
    • (2005) Infect Immun , vol.73 , pp. 3197-3209
    • Kaper, J.B.1    Sperandio, V.2
  • 17
    • 0030746910 scopus 로고    scopus 로고
    • Nasal carriage of Staphylococcus aureus: Epidemiology, underlying mechanisms, and associated risks
    • Kluytmans, J., van Belkum, A. & Verbrugh, H. (1997). Nasal carriage of Staphylococcus aureus: epidemiology, underlying mechanisms, and associated risks. Clin Microbiol Rev 10, 505-520.
    • (1997) Clin Microbiol Rev , vol.10 , pp. 505-520
    • Kluytmans, J.1    van Belkum, A.2    Verbrugh, H.3
  • 18
  • 19
    • 0035252008 scopus 로고    scopus 로고
    • Antibacterial action of chitosan and carboxymethylated chitosan
    • Liu, X. F., Guan, Y. L., Yang, D. Z., Li, Z. & Yao, K. D. (2000). Antibacterial action of chitosan and carboxymethylated chitosan. J Appl Polym Sci 79, 1324-1335.
    • (2000) J Appl Polym Sci , vol.79 , pp. 1324-1335
    • Liu, X.F.1    Guan, Y.L.2    Yang, D.Z.3    Li, Z.4    Yao, K.D.5
  • 20
    • 1542346915 scopus 로고    scopus 로고
    • Interaction of the crystalline bacterial cell surface layer protein SbsB and the secondary cell wall polymer of Geobacillus stearothermophilus PV72 assessed by real-time surface plasmon resonance biosensor technology
    • Mader, C., Huber, C., Moll, D., Sleytr, U. B. & Sara, M. (2004). Interaction of the crystalline bacterial cell surface layer protein SbsB and the secondary cell wall polymer of Geobacillus stearothermophilus PV72 assessed by real-time surface plasmon resonance biosensor technology. J Bacteriol 186, 1758-1768.
    • (2004) J Bacteriol , vol.186 , pp. 1758-1768
    • Mader, C.1    Huber, C.2    Moll, D.3    Sleytr, U.B.4    Sara, M.5
  • 21
    • 0032975361 scopus 로고    scopus 로고
    • The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase
    • Modun, B. & Williams, P. (1999). The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase. Infect Immun 67, 1086-1092.
    • (1999) Infect Immun , vol.67 , pp. 1086-1092
    • Modun, B.1    Williams, P.2
  • 22
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K. & Olson, A. J. (1998). Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem 19, 1639-1662.
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 23
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi, V. & Fischetti, V. A. (1992). A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J Exp Med 176, 415-426.
    • (1992) J Exp Med , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 24
    • 0032486286 scopus 로고    scopus 로고
    • Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi, V. & Fischetti, V. A. (1998). Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J Biol Chem 273, 14503-14515.
    • (1998) J Biol Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 25
    • 41549111120 scopus 로고    scopus 로고
    • Role of Staphylococcus aureus catalase in niche competition against Streptococcus pneumoniae
    • Park, B., Nizet, V. & Liu, G. Y. (2008). Role of Staphylococcus aureus catalase in niche competition against Streptococcus pneumoniae. J Bacteriol 190, 2275-2278.
    • (2008) J Bacteriol , vol.190 , pp. 2275-2278
    • Park, B.1    Nizet, V.2    Liu, G.Y.3
  • 27
    • 0015115188 scopus 로고
    • Studies on human triosephosphate isomerase. I. Isolation and properties of the enzyme from erythrocytes
    • Rozacky, E. E., Sawyer, T. H., Barton, R. A. & Gracy, R. W. (1971). Studies on human triosephosphate isomerase. I. Isolation and properties of the enzyme from erythrocytes. Arch Biochem Biophys 146, 312-320.
    • (1971) Arch Biochem Biophys , vol.146 , pp. 312-320
    • Rozacky, E.E.1    Sawyer, T.H.2    Barton, R.A.3    Gracy, R.W.4
  • 28
    • 51149093453 scopus 로고    scopus 로고
    • Diffusible signals and interspecies communication in bacteria
    • Ryan, R. P. & Dow, J. M. (2008). Diffusible signals and interspecies communication in bacteria. Microbiology 154, 1845-1858.
    • (2008) Microbiology , vol.154 , pp. 1845-1858
    • Ryan, R.P.1    Dow, J.M.2
  • 29
    • 30644476416 scopus 로고    scopus 로고
    • Killing of Cryptococcus neoformans by Staphylococcus aureus: The role of cryptococcal capsular polysaccharide in the fungal-bacteria interaction
    • Saito, F. & Ikeda, R. (2005). Killing of Cryptococcus neoformans by Staphylococcus aureus: the role of cryptococcal capsular polysaccharide in the fungal-bacteria interaction. Med Mycol 43, 603-612.
    • (2005) Med Mycol , vol.43 , pp. 603-612
    • Saito, F.1    Ikeda, R.2
  • 30
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N. & Peitsch, M. C. (2003). SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31, 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 31
    • 33646103431 scopus 로고    scopus 로고
    • Carbohydrates as future anti-adhesion drugs for infectious diseases
    • Sharon, N. (2006). Carbohydrates as future anti-adhesion drugs for infectious diseases. Biochim Biophys Acta 1760, 527-537.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 527-537
    • Sharon, N.1
  • 32
    • 0141907308 scopus 로고    scopus 로고
    • Mapping of regions within the vaccinia virus complement control protein involved in dose-dependent binding to key complement components and heparin using surface plasmon resonance
    • Smith, S. A., Sreenivasan, R., Krishnasamy, G., Judge, K. W., Murthy, K. H., Arjunwadkar, S. J., Pugh, D. R. & Kotwal, G. J. (2003). Mapping of regions within the vaccinia virus complement control protein involved in dose-dependent binding to key complement components and heparin using surface plasmon resonance. Biochim Biophys Acta 1650, 30-39.
    • (2003) Biochim Biophys Acta , vol.1650 , pp. 30-39
    • Smith, S.A.1    Sreenivasan, R.2    Krishnasamy, G.3    Judge, K.W.4    Murthy, K.H.5    Arjunwadkar, S.J.6    Pugh, D.R.7    Kotwal, G.J.8
  • 33
    • 33744901493 scopus 로고    scopus 로고
    • Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils
    • Terao, Y., Yamaguchi, M., Hamada, S. & Kawabata, S. (2006). Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils. J Biol Chem 281, 14215-14223.
    • (2006) J Biol Chem , vol.281 , pp. 14215-14223
    • Terao, Y.1    Yamaguchi, M.2    Hamada, S.3    Kawabata, S.4
  • 35
    • 46049097555 scopus 로고    scopus 로고
    • Cell-cell communication in bacteria: United we stand
    • von Bodman, S. B., Willey, J. M. & Diggle, S. P. (2008). Cell-cell communication in bacteria: united we stand. J Bacteriol 190, 4377-4391.
    • (2008) J Bacteriol , vol.190 , pp. 4377-4391
    • von Bodman, S.B.1    Willey, J.M.2    Diggle, S.P.3
  • 36
    • 0035804274 scopus 로고    scopus 로고
    • Nasal carriage as a source of Staphylococcus aureus bacteremia. Study Group
    • von Eiff, C., Becker, K., Machka, K., Stammer, H. & Peters, G. (2001). Nasal carriage as a source of Staphylococcus aureus bacteremia. Study Group. N Engl J Med 344, 11-16.
    • (2001) N Engl J Med , vol.344 , pp. 11-16
    • von Eiff, C.1    Becker, K.2    Machka, K.3    Stammer, H.4    Peters, G.5


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