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Volumn 21, Issue 9, 2011, Pages 1217-1227

Binding of Clostridium difficile toxins to human milk oligosaccharides

Author keywords

Clostridium difficile; cytotoxicity; docking; human milk oligosaccharide; ligand binding; mass spectrometry; toxin

Indexed keywords

AMINE; CLOSTRIDIUM DIFFICILE TOXIN A; CLOSTRIDIUM DIFFICILE TOXIN B; DISACCHARIDE; LACTOSAMINE; LACTOSE; OLIGOSACCHARIDE; UNCLASSIFIED DRUG;

EID: 80051523939     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwr055     Document Type: Article
Times cited : (40)

References (39)
  • 1
    • 0022652475 scopus 로고
    • Inhibition of attachment of Streptococcus pneumoniae and Haemophilus influenzae by human milk and receptor oligosaccharides
    • Andersson B, Porras O, Hanson B, Lagergard T, Svanborgeden C. 1986. Inhibition of attachment of Streptococcus pneumoniae and Haemophilus influenzae by human milk and receptor oligosaccharides. J Infect Dis. 153:232-237. (Pubitemid 16156054)
    • (1986) Journal of Infectious Diseases , vol.153 , Issue.2 , pp. 232-237
    • Andersson, B.1    Porras, O.2    Hanson, L.A.3
  • 2
    • 77958004353 scopus 로고    scopus 로고
    • Medical microbiology: A toxin contest
    • Ballard JD. 2010. Medical microbiology: A toxin contest. Nature. 467 (7316):665-666.
    • (2010) Nature , vol.467 , Issue.7316 , pp. 665-666
    • Ballard, J.D.1
  • 3
    • 39749142406 scopus 로고    scopus 로고
    • Historical perspectives on studies of Clostridium difficile and C. difficile infection
    • DOI 10.1086/521865
    • Bartlett JG. 2008. Historical perspectives on studies of Clostridium difficile and Clostridium difficile infection. Clin Infect Dis. 46:S4-S11. (Pubitemid 351323660)
    • (2008) Clinical Infectious Diseases , vol.46 , Issue.SUPPL. 1
    • Bartlett, J.G.1
  • 4
    • 23744489602 scopus 로고    scopus 로고
    • On the generalized valence bond description of the anomeric and exo-anomeric effects: An ab initio conformational study of 2- methoxytetrahydropyran
    • DOI 10.1016/j.carres.2005.07.001, PII S0008621505003216
    • Bitzer RS, Barbosa AGH, da Silva CO, Nascimento MAC. 2005. On the generalized valence bond description of the anomeric and exo-anomeric effects: An ab initio conformational study of 2-methoxytetrahydropyran. Carbohydr Res. 340:2171-2184. (Pubitemid 41139992)
    • (2005) Carbohydrate Research , vol.340 , Issue.13 , pp. 2171-2184
    • Bitzer, R.S.1    Barbosa, A.G.H.2    Da Silva, C.O.3    Nascimento, M.A.C.4
  • 5
    • 0026072432 scopus 로고
    • Inhibition of localized adhesion of enteropathogenic Escherichia coli to Hep-2 cells by immunoglobulin and oligosaccharide fractions of human colostrum and breast-milk
    • Cravioto A, Tello A, Villafan H, Ruiz J, Delvedovo S, Neeser JR. 1991. Inhibition of localized adhesion of enteropathogenic Escherichia coli to Hep-2 cells by immunoglobulin and oligosaccharide fractions of human colostrum and breast-milk. J Infect Dis. 163:1247-1255.
    • (1991) J Infect Dis , vol.163 , pp. 1247-1255
    • Cravioto, A.1    Tello, A.2    Villafan, H.3    Ruiz, J.4    Delvedovo, S.5    Neeser, J.R.6
  • 6
    • 33846253977 scopus 로고    scopus 로고
    • TcdC genotypes associated with severe TcdC truncation in an epidemic clone and other strains of Clostridium difficile
    • DOI 10.1128/JCM.01599-06
    • Curry SR, Marsh JW, Muto CA, O'Leary MM, Pasculle AW, Harrison LH. 2007. TcdC genotypes associated of Clostridium difficile with severe TcdC truncation in an epidemic clone and other strains of Clostridium difficile. J Clin Microbiol. 45:215-221. (Pubitemid 46106429)
    • (2007) Journal of Clinical Microbiology , vol.45 , Issue.1 , pp. 215-221
    • Curry, S.R.1    Marsh, J.W.2    Muto, C.A.3    O'Leary, M.M.4    Pasculle, A.W.5    Harrison, L.H.6
  • 7
    • 0031762948 scopus 로고    scopus 로고
    • Binding of Clostridium difficile toxin A to human milk secretory component
    • Dallas SD, Rolfe RD. 1998. Binding of Clostridium difficile toxin A to human milk secretory component. J Med Microbiol. 47:879-888. (Pubitemid 28484379)
    • (1998) Journal of Medical Microbiology , vol.47 , Issue.10 , pp. 879-888
    • Dallas, S.D.1    Rolfe, R.D.2
  • 8
    • 58149115498 scopus 로고    scopus 로고
    • Functional properties of the carboxy-terminal host cell-binding domains of the two toxins, TcdA and TcdB, expressed by Clostridium difficile
    • Dingle T, Wee S, Mulvey GL, Greco A, Kitova EN, Sun JX, Lin SJ, Klassen JS, Palcic MM, Ng KKS, et al. 2008. Functional properties of the carboxy-terminal host cell-binding domains of the two toxins, TcdA and TcdB, expressed by Clostridium difficile. Glycobiology. 18:698-706.
    • (2008) Glycobiology , vol.18 , pp. 698-706
    • Dingle, T.1    Wee, S.2    Mulvey, G.L.3    Greco, A.4    Kitova, E.N.5    Sun, J.X.6    Lin, S.J.7    Klassen, J.S.8    Palcic, M.M.9    Ng, K.K.S.10
  • 10
    • 0347383758 scopus 로고    scopus 로고
    • MODELLER: Generation and Refinement of Homology-Based Protein Structure Models
    • DOI 10.1016/S0076-6879(03)74020-8
    • Fiser A, Sali A. 2003. Modeller: Generation and refinement of homology-based protein structure models. Methods Enzymol. 374:461-491. (Pubitemid 37531821)
    • (2003) Methods in Enzymology , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 11
    • 78649807947 scopus 로고    scopus 로고
    • Healthcare epidemiology: Management of Clostridium difficile infection: Thinking inside and outside the box
    • Gerding DN, Johnson S. 2010. Healthcare epidemiology: Management of Clostridium difficile infection: Thinking inside and outside the box. Clin Infect Dis. 51(11):1306-1313.
    • (2010) Clin Infect Dis , vol.51 , Issue.11 , pp. 1306-1313
    • Gerding, D.N.1    Johnson, S.2
  • 13
    • 0028358924 scopus 로고
    • Oligosaccharide sequences attached to an inert support (SYNSORB) as potential therapy for antibiotic-associated diarrhea and pseudomembranous colitis
    • Heerze LD, Kelm MA, Talbot JA, Armstrong GD. 1994. Oligosaccharide sequences attached to an inert support (Synsorb) as potential therapy for antibiotic-associated diarrhea and Pseudomembranous colitis. J Infect Dis. 169:1291-1296. (Pubitemid 24164593)
    • (1994) Journal of Infectious Diseases , vol.169 , Issue.6 , pp. 1291-1296
    • Heerze, L.D.1    Kelm, M.A.2    Talbot, J.A.3    Armstrong, G.D.4
  • 15
    • 0025050372 scopus 로고
    • A molecular mechanical force field for the conformational analysis of oligosaccharides: Comparison of theoretical and crystal structures of Manα1-3Manβ1-4GlcNAc
    • Homans SW. 1990. A molecular mechanical force-field for the conformational analysis of oligosaccharides: Comparison of theoretical and crystal structures of Man oc1-3Man (31-4 GlcNAc. Biochemistry. 29(39):9110-9118. (Pubitemid 20320874)
    • (1990) Biochemistry , vol.29 , Issue.39 , pp. 9110-9118
    • Homans, S.W.1
  • 16
    • 33947716119 scopus 로고    scopus 로고
    • A semiempirical free energy force field with charge-based desolvation
    • Huey R, Morris GM, Olson AJ, Goodsell DS. 2006. A semiempirical free energy force field with charge-based desolvation. J Comput Chem. 28:1145-1152.
    • (2006) J Comput Chem , vol.28 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 18
    • 0031958706 scopus 로고    scopus 로고
    • Clostridium difficile infection
    • DOI 10.1146/annurev.med.49.1.375
    • Kelly CP, LaMont JT. 1998. Clostridium difficile infection. Annu Rev Med. 49:375-390. (Pubitemid 28197461)
    • (1998) Annual Review of Medicine , vol.49 , pp. 375-390
    • Kelly, C.P.1    LaMont, J.T.2
  • 19
    • 0022525082 scopus 로고
    • Cell surface binding site for Clostridium difficile enterotoxin: Evidence for a glycoconjugate containing the sequence Ga1α1-3Galβ1-4GlcNAc
    • Krivan HC, Clark GF, Smith DF, Wilkins TD. 1986. Cell-surface binding-site for Clostridium difficile enterotoxin-evidence for a glycoconjugate containing the sequence Gal-alpha-1-3Gal-beta-1-4GlcNAc. Infect Immun. 53:573-581. (Pubitemid 16053178)
    • (1986) Infection and Immunity , vol.53 , Issue.3 , pp. 573-581
    • Krivan, H.C.1    Clark, G.F.2    Smith, D.F.3    Wilkins, T.D.4
  • 22
    • 0036790050 scopus 로고    scopus 로고
    • The sialylated fraction of milk oligosaccharides is partially responsible for binding to enterotoxigenic and uropathogenic Escherichia coli human strains
    • Martin-Sosa S, Martin MJ, Hueso P. 2002. The sialylated fraction of milk oligosaccharides is partially responsible for binding to enterotoxigenic and uropathogenic Escherichia coli human strains. J Nutr. 132:3067-3072.
    • (2002) J Nutr , vol.132 , pp. 3067-3072
    • Martin-Sosa, S.1    Martin, M.J.2    Hueso, P.3
  • 23
    • 65449118333 scopus 로고    scopus 로고
    • Neonatal protection by an innate immune system of human milk consisting of oligosaccharides and glycans
    • Newburg DS. 2009. Neonatal protection by an innate immune system of human milk consisting of oligosaccharides and glycans. JAnim Sci. 87:26-34.
    • (2009) JAnim Sci , vol.87 , pp. 26-34
    • Newburg, D.S.1
  • 24
    • 23944482922 scopus 로고    scopus 로고
    • Human milk glycans protect infants against enteric pathogens
    • DOI 10.1146/annurev.nutr.25.050304.092553
    • Newburg DS, Ruiz-Palacios GM, Morrow AL. 2005. Human milk glycans protect infants against enteric pathogens. Annu Rev Nutr. 25:37-58. (Pubitemid 41208993)
    • (2005) Annual Review of Nutrition , vol.25 , pp. 37-58
    • Newburg, D.S.1    Ruiz-Palacios, G.M.2    Morrow, A.L.3
  • 26
    • 70349117661 scopus 로고    scopus 로고
    • Glycan arrays: Recent advances and future challenges
    • Oyelaran O, Gildersleeve JC. 2009. Glycan arrays: Recent advances and future challenges. Curr Opin Chem Biol. 13(4):406-413.
    • (2009) Curr Opin Chem Biol , vol.13 , Issue.4 , pp. 406-413
    • Oyelaran, O.1    Gildersleeve, J.C.2
  • 27
    • 77955782233 scopus 로고    scopus 로고
    • Structural organization of the functional domains of Clostridium difficile toxins A and B
    • Pruitt RN, Chambers MG, Ng KK, Ohi MD, Lacy DB. 2010. Structural organization of the functional domains of Clostridium difficile toxins A and B. Proc Natl Acad Sci USA. 107(30):13467-13472.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.30 , pp. 13467-13472
    • Pruitt, R.N.1    Chambers2    Mg3    Ng, K.K.4    Ohi, M.D.5    Lacy, D.B.6
  • 28
    • 0028859828 scopus 로고
    • Immunoglobulin and nonimmunoglobulin components of human milk inhibit Clostridium difficile toxin A-receptor binding
    • Rolfe RD, Song W. 1995. Immunoglobulin and nonimmunoglobulin components of human milk inhibit Clostridium difficile toxin A-receptor binding. J Med Microbiol. 42:10-19.
    • (1995) J Med Microbiol , vol.42 , pp. 10-19
    • Rolfe, R.D.1    Song, W.2
  • 29
    • 0013238319 scopus 로고    scopus 로고
    • Campylobacter jejuni binds intestinal H(O) antigen (Fucα1, 2Galβ1, 4GlcNAc), and fucosyloligosaccharides of human milk inhibit its binding and infection
    • DOI 10.1074/jbc.M207744200
    • Ruiz-Palacios GM, Cervantes LE, Ramos P, Chavez-Munguia B, Newburg DS. 2003. Campylobacter jejuni binds intestinal H(O) antigen (Fuc alpha 1, 2Gal beta 1, 4GlcNAc), and fucosyloligosaccharides of human milk inhibit its binding and infection. J Biol Chem. 278:14112-14120. (Pubitemid 36799958)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14112-14120
    • Ruiz-Palacios, G.M.1    Cervantes, L.E.2    Ramos, P.3    Chavez-Munguia, B.4    Newburg, D.S.5
  • 30
    • 67649391053 scopus 로고    scopus 로고
    • Clostridium difficile infection: New developments in epidemiology and pathogenesis
    • Rupnik M, Wilcox MH, Gerding DN. 2009. Clostridium difficile infection: New developments in epidemiology and pathogenesis. Nat Rev Microbiol. 7(7):526-536.
    • (2009) Nat Rev Microbiol , vol.7 , Issue.7 , pp. 526-536
    • Rupnik, M.1    Wilcox, M.H.2    Gerding, D.N.3
  • 32
    • 33646589615 scopus 로고    scopus 로고
    • Method for distinguishing specific from nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry
    • DOI 10.1021/ac0522005
    • Sun JX, Kitova EN, Wang WJ, Klassen JS. 2006. Method for distinguishing specific from nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry. Anal Chem. 78:3010-3018. (Pubitemid 43726119)
    • (2006) Analytical Chemistry , vol.78 , Issue.9 , pp. 3010-3018
    • Sun, J.1    Kitova, E.N.2    Wang, W.3    Klassen, J.S.4
  • 33
    • 76149120388 scopus 로고    scopus 로고
    • Software news and update. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott O, Olson AJ. 2010. Software news and update. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem. 31: 455-461.
    • (2010) J Comput Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 34
    • 0026078094 scopus 로고
    • Toxin-A of Clostridium difficile binds to the human carbohydrate antigens-I, antigens-X, and antigens-Y
    • Tucker KD, Wilkins TD. 1991. Toxin-A of Clostridium difficile binds to the human carbohydrate antigens-I, antigens-X, and antigens-Y. Infect Immun. 59:73-78.
    • (1991) Infect Immun , vol.59 , pp. 73-78
    • Tucker, K.D.1    Wilkins, T.D.2
  • 35
    • 0030271882 scopus 로고    scopus 로고
    • Large clostridial cytotoxins - A family of glycosyltransferases modifying small GTP-binding proteins
    • DOI 10.1016/0966-842X(96)10061-5
    • Voneichelstreiber C, Boquet P, Sauerborn M, Thelestam M. 1996. Large clos-tridial cytotoxins-A family of glycosyltransferases modifying small GTP-binding proteins. TIM. 4:375-382. (Pubitemid 26325127)
    • (1996) Trends in Microbiology , vol.4 , Issue.10 , pp. 375-382
    • Von Eichel-Streiber, C.1    Boquet, P.2    Sauerborn, M.3    Thelestam, M.4
  • 36
    • 0026702564 scopus 로고
    • Evidence for a modular structure of the homologous repetitive c-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus mutans glu-cosyltransferases
    • Voneichelstreiber C, Sauerborn M, Kuramitsu HK. 1992. Evidence for a modular structure of the homologous repetitive c-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus mutans glu-cosyltransferases. J Bacteriol. 174:6707-6710.
    • (1992) J Bacteriol , vol.174 , pp. 6707-6710
    • Voneichelstreiber, C.1    Sauerborn, M.2    Kuramitsu, H.K.3
  • 37
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins: Mechanism of action and role in disease
    • DOI 10.1128/CMR.18.2.247-263.2005
    • Voth DE, Ballard JD. 2005. Clostridium difficile toxins: Mechanism of action and role in disease. Clin Microbiol Rev. 18:247-263. (Pubitemid 40548293)
    • (2005) Clinical Microbiology Reviews , vol.18 , Issue.2 , pp. 247-263
    • Voth, D.E.1    Ballard, J.D.2
  • 38
    • 0141958921 scopus 로고    scopus 로고
    • Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray fourier transform ion cyclotron resonance mass spectrometry
    • DOI 10.1021/ac034300l
    • Wang WJ, Kitova EN, Klassen JS. 2003. Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoe-lectrospray Fourier transform ion cyclotron resonance mass spectrometry. Anal Chem. 75:4945-4955. (Pubitemid 37238544)
    • (2003) Analytical Chemistry , vol.75 , Issue.19 , pp. 4945-4955
    • Wang, W.1    Kitova, E.N.2    Klassen, J.S.3
  • 39
    • 33745142549 scopus 로고    scopus 로고
    • In vitro fermentation of breast milk oligosaccharides by Bifidobacterium infantis and Lactobacillus gasseri
    • DOI 10.1128/AEM.02515-05
    • Ward RE, Ninonuevo M, Mills DA, Lebrilla CB, German JB. 2006. In vitro fermentation of breast milk oligosaccharides by Bifidobacterium infantis and Lactobacillus gasseri. Appl Environ Microbiol. 72: 4497-4499. (Pubitemid 43894931)
    • (2006) Applied and Environmental Microbiology , vol.72 , Issue.6 , pp. 4497-4499
    • Ward, R.E.1    Ninonuevo, M.2    Mills, D.A.3    Lebrilla, C.B.4    German, J.B.5


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