메뉴 건너뛰기




Volumn 289, Issue 26, 2014, Pages 18008-18021

Mechanism of action and epitopes of Clostridium difficile toxin B-neutralizing antibody bezlotoxumab revealed by X-ray crystallography

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; BINDING SITES; CARBOHYDRATES; CELL MEMBRANES; EPITOPES; TOXIC MATERIALS; X RAY CRYSTALLOGRAPHY;

EID: 84903537030     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.560748     Document Type: Article
Times cited : (114)

References (44)
  • 1
    • 67649391053 scopus 로고    scopus 로고
    • Clostridium difficile infection: New developments in epidemiology and pathogenesis
    • Rupnik, M., Wilcox, M. H., and Gerding, D. N. (2009) Clostridium difficile infection: new developments in epidemiology and pathogenesis. Nat. Rev. Microbiol. 7, 526-536
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 526-536
    • Rupnik, M.1    Wilcox, M.H.2    Gerding, D.N.3
  • 3
    • 84855510455 scopus 로고    scopus 로고
    • The role of toxin A and toxin B in the virulence of Clostridium difficile
    • Carter, G. P., Rood, J. I., and Lyras, D. (2012) The role of toxin A and toxin B in the virulence of Clostridium difficile. Trends Microbiol. 20, 21-29
    • (2012) Trends Microbiol. , vol.20 , pp. 21-29
    • Carter, G.P.1    Rood, J.I.2    Lyras, D.3
  • 4
    • 84857790535 scopus 로고    scopus 로고
    • Clostridium difficile toxins: Mediators of inflammation
    • Shen, A. (2012) Clostridium difficile toxins: mediators of inflammation. J. Innate Immun. 4, 149-158
    • (2012) J. Innate Immun. , vol.4 , pp. 149-158
    • Shen, A.1
  • 5
    • 84878486491 scopus 로고    scopus 로고
    • Toward a structural understanding of Clostridium difficile toxins A and B
    • Pruitt, R. N., and Lacy, D. B. (2012) Toward a structural understanding of Clostridium difficile toxins A and B. Front. Cell Infect. Microbiol. 2, 28
    • (2012) Front. Cell Infect. Microbiol. , vol.2 , pp. 28
    • Pruitt, R.N.1    Lacy, D.B.2
  • 7
    • 77955782233 scopus 로고    scopus 로고
    • Structural organization of the functional domains of Clostridium difficile toxins A and B
    • Pruitt, R. N., Chambers, M. G., Ng, K. K., Ohi, M. D., and Lacy, D. B. (2010) Structural organization of the functional domains of Clostridium difficile toxins A and B. Proc. Natl. Acad. Sci. U. S. A. 107, 13467-13472
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 13467-13472
    • Pruitt, R.N.1    Chambers, M.G.2    Ng, K.K.3    Ohi, M.D.4    Lacy, D.B.5
  • 8
    • 0034114105 scopus 로고    scopus 로고
    • PH-induced conformational changes in Clostridium difficile toxin B
    • Qa'Dan, M., Spyres, L. M., and Ballard, J. D. (2000) pH-induced conformational changes in Clostridium difficile toxin B. Infect. Immun. 68, 2470-2474
    • (2000) Infect. Immun. , vol.68 , pp. 2470-2474
    • Qa'Dan, M.1    Spyres, L.M.2    Ballard, J.D.3
  • 9
    • 0242414631 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium difficile toxin B. Translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells
    • Pfeifer, G., Schirmer, J., Leemhuis, J., Busch, C., Meyer, D. K., Aktories, K., and Barth, H. (2003) Cellular uptake of Clostridium difficile toxin B. Translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells. J. Biol. Chem. 278, 44535-44541
    • (2003) J. Biol. Chem. , vol.278 , pp. 44535-44541
    • Pfeifer, G.1    Schirmer, J.2    Leemhuis, J.3    Busch, C.4    Meyer, D.K.5    Aktories, K.6    Barth, H.7
  • 10
    • 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, G. L., Greco, A., Kitova, E. N., Sun, J., Lin, S., Klassen, J. S., Palcic, M. M., Ng, K. K., and Armstrong, G. D. (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.6    Lin, S.7    Klassen, J.S.8    Palcic, M.M.9    Ng, K.K.10    Armstrong, G.D.11
  • 13
    • 0022525082 scopus 로고
    • Cell surface binding site for Clostridium difficile enterotoxin: Evidence for a glycoconjugate containing the sequence Gal β1-3Gal α1-4GlcNAc
    • Krivan, H. C., Clark, G. F., Smith, D. F., and Wilkins, T. D. (1986) Cell surface binding site for Clostridium difficile enterotoxin: evidence for a glycoconjugate containing the sequence Gal β1-3Gal α1-4GlcNAc. Infect. Immun. 53, 573-581
    • (1986) Infect. Immun. , vol.53 , pp. 573-581
    • Krivan, H.C.1    Clark, G.F.2    Smith, D.F.3    Wilkins, T.D.4
  • 15
    • 0025893128 scopus 로고
    • Characterization of rabbit ileal receptors for Clostridium difficile toxin A. Evidence for a receptor-coupled G protein
    • Pothoulakis, C., LaMont, J. T., Eglow, R., Gao, N., Rubins, J. B., Theoharides, T. C., and Dickey, B. F. (1991) Characterization of rabbit ileal receptors for Clostridium difficile toxin A. Evidence for a receptor-coupled G protein. J. Clin. Invest. 88, 119-125
    • (1991) J. Clin. Invest. , vol.88 , pp. 119-125
    • Pothoulakis, C.1    LaMont, J.T.2    Eglow, R.3    Gao, N.4    Rubins, J.B.5    Theoharides, T.C.6    Dickey, B.F.7
  • 16
    • 0026078094 scopus 로고
    • Toxin A of Clostridium difficile binds to the human carbohydrate antigens I, X, and Y
    • Tucker, K. D., and Wilkins, T. D. (1991) Toxin A of Clostridium difficile binds to the human carbohydrate antigens I, X, and Y. Infect. Immun. 59, 73-78
    • (1991) Infect. Immun. , vol.59 , pp. 73-78
    • Tucker, K.D.1    Wilkins, T.D.2
  • 18
    • 0037449918 scopus 로고    scopus 로고
    • The complete receptor-binding domain of Clostridium difficile toxin A is required for endocytosis
    • Frisch, C., Gerhard, R., Aktories, K., Hofmann, F., and Just, I. (2003) The complete receptor-binding domain of Clostridium difficile toxin A is required for endocytosis. Biochem. Biophys. Res. Commun. 300, 706-711
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 706-711
    • Frisch, C.1    Gerhard, R.2    Aktories, K.3    Hofmann, F.4    Just, I.5
  • 19
    • 0026702564 scopus 로고
    • Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus mutans glucosyltransferases
    • von Eichel-Streiber, C., Sauerborn, M., and Kuramitsu, H. K. (1992) Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus mutans glucosyltransferases. J. Bacteriol. 174, 6707-6710
    • (1992) J. Bacteriol. , vol.174 , pp. 6707-6710
    • Von Eichel-Streiber, C.1    Sauerborn, M.2    Kuramitsu, H.K.3
  • 20
    • 79952803707 scopus 로고    scopus 로고
    • The repetitive oligopeptide sequences modulate cytopathic potency but are not crucial for cellular uptake of Clostridium difficile toxin A
    • Olling, A., Goy, S., Hoffmann, F., Tatge, H., Just, I., and Gerhard, R. (2011) The repetitive oligopeptide sequences modulate cytopathic potency but are not crucial for cellular uptake of Clostridium difficile toxin A. PLoS One 6, e17623
    • (2011) PLoS One , vol.6
    • Olling, A.1    Goy, S.2    Hoffmann, F.3    Tatge, H.4    Just, I.5    Gerhard, R.6
  • 22
    • 0025667927 scopus 로고
    • Clostridium difficile toxinA carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransferases
    • von Eichel-Streiber, C., and Sauerborn, M. (1990) Clostridium difficile toxinA carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransferases. Gene 96, 107-113
    • (1990) Gene , vol.96 , pp. 107-113
    • Von Eichel-Streiber, C.1    Sauerborn, M.2
  • 23
    • 29444439842 scopus 로고    scopus 로고
    • Crystal structure of receptor-binding C-terminal repeats from Clostridium difficile toxin A
    • Ho, J. G., Greco, A., Rupnik, M., and Ng, K. K. (2005) Crystal structure of receptor-binding C-terminal repeats from Clostridium difficile toxin A. Proc. Natl. Acad. Sci. U. S. A. 102, 18373-18378
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18373-18378
    • Ho, J.G.1    Greco, A.2    Rupnik, M.3    Ng, K.K.4
  • 25
    • 84893137156 scopus 로고    scopus 로고
    • Structural basis for antibody recognition in the receptor-binding domains of toxins A and B from Clostridium difficile
    • Murase, T., Eugenio, L., Schorr, M., Hussack, G., Tanha, J., Kitova, E. N., Klassen, J. S., and Ng, K. K. (2014) Structural basis for antibody recognition in the receptor-binding domains of toxins A and B from Clostridium difficile. J. Biol. Chem. 289, 2331-2343
    • (2014) J. Biol. Chem. , vol.289 , pp. 2331-2343
    • Murase, T.1    Eugenio, L.2    Schorr, M.3    Hussack, G.4    Tanha, J.5    Kitova, E.N.6    Klassen, J.S.7    Ng, K.K.8
  • 27
    • 84891353755 scopus 로고    scopus 로고
    • Theimportance of toxin A, toxinB and CDT in virulence of an epidemic Clostridium difficile strain
    • Kuehne, S. A., Collery, M. M., Kelly, M. L., Cartman, S. T., Cockayne, A., and Minton, N. P. (2014) Theimportance of toxin A, toxinB and CDT in virulence of an epidemic Clostridium difficile strain. J. Infect. Dis. 209, 83-86
    • (2014) J. Infect. Dis. , vol.209 , pp. 83-86
    • Kuehne, S.A.1    Collery, M.M.2    Kelly, M.L.3    Cartman, S.T.4    Cockayne, A.5    Minton, N.P.6
  • 30
    • 0031948840 scopus 로고    scopus 로고
    • Antibodies to recombinant Clostridium difficile toxins A and B are an effective treatment and prevent relapse of C. Difficile-associated disease in a hamster model of infection
    • Kink, J. A., and Williams, J. A. (1998) Antibodies to recombinant Clostridium difficile toxins A and B are an effective treatment and prevent relapse of C. difficile-associated disease in a hamster model of infection. Infect. Immun. 66, 2018-2025
    • (1998) Infect. Immun. , vol.66 , pp. 2018-2025
    • Kink, J.A.1    Williams, J.A.2
  • 31
    • 84871775506 scopus 로고    scopus 로고
    • Antibody against TcdB, but not TcdA, prevents development of gastrointestinal and systemic Clostridium difficile disease
    • Steele, J., Mukherjee, J., Parry, N., and Tzipori, S. (2013) Antibody against TcdB, but not TcdA, prevents development of gastrointestinal and systemic Clostridium difficile disease. J. Infect. Dis. 207, 323-330
    • (2013) J. Infect. Dis. , vol.207 , pp. 323-330
    • Steele, J.1    Mukherjee, J.2    Parry, N.3    Tzipori, S.4
  • 32
    • 0028818809 scopus 로고
    • Evaluation of formalin-inactivated Clostridium difficile vaccines administered by parenteral and mucosal routes of immunization in hamsters
    • Torres, J. F., Lyerly, D. M., Hill, J. E., and Monath, T. P. (1995) Evaluation of formalin-inactivated Clostridium difficile vaccines administered by parenteral and mucosal routes of immunization in hamsters. Infect. Immun. 63, 4619-4627
    • (1995) Infect. Immun. , vol.63 , pp. 4619-4627
    • Torres, J.F.1    Lyerly, D.M.2    Hill, J.E.3    Monath, T.P.4
  • 34
    • 80052727104 scopus 로고    scopus 로고
    • Fully activated MEK1 exhibits compromised affinity for binding of allosteric inhibitors U0126 and PD0325901
    • Sheth, P. R., Liu, Y., Hesson, T., Zhao, J., Vilenchik, L., Liu, Y. H., Mayhood, T. W., and Le, H. V. (2011) Fully activated MEK1 exhibits compromised affinity for binding of allosteric inhibitors U0126 and PD0325901. Biochemistry 50, 7964-7976
    • (2011) Biochemistry , vol.50 , pp. 7964-7976
    • Sheth, P.R.1    Liu, Y.2    Hesson, T.3    Zhao, J.4    Vilenchik, L.5    Liu, Y.H.6    Mayhood, T.W.7    Le, H.V.8
  • 35
    • 62549108693 scopus 로고    scopus 로고
    • Epitope mapping by amide hydrogen/deuterium exchange coupled with immobilization of antibody, on-line proteolysis, liquid chromatography and mass spectrometry
    • Coales, S. J., Tuske, S. J., Tomasso, J. C., and Hamuro, Y. (2009) Epitope mapping by amide hydrogen/deuterium exchange coupled with immobilization of antibody, on-line proteolysis, liquid chromatography and mass spectrometry. Rapid Commun. Mass Spectrom. 23, 639-647
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 639-647
    • Coales, S.J.1    Tuske, S.J.2    Tomasso, J.C.3    Hamuro, Y.4
  • 38
  • 40
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati, V. (1952) Traitement statistique des erreurs dans la determination des structures cristallines. Acta Cryst. 5, 802-810
    • (1952) Acta Cryst. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 41
    • 75449110786 scopus 로고    scopus 로고
    • Dynamin- and clathrin-dependent endocytosis in African swine fever virus entry
    • Hernaez, B., and Alonso, C. (2010) Dynamin- and clathrin-dependent endocytosis in African swine fever virus entry. J. Virol. 84, 2100-2109
    • (2010) J. Virol. , vol.84 , pp. 2100-2109
    • Hernaez, B.1    Alonso, C.2
  • 43
    • 79953206941 scopus 로고    scopus 로고
    • Neutralization of Clostridium difficile toxin A with single-domain antibodies targeting the cell receptor binding domain
    • Hussack, G., Arbabi-Ghahroudi, M., van Faassen, H., Songer, J. G., Ng, K. K., MacKenzie, R., and Tanha, J. (2011) Neutralization of Clostridium difficile toxin A with single-domain antibodies targeting the cell receptor binding domain. J. Biol. Chem. 286, 8961-8976
    • (2011) J. Biol. Chem. , vol.286 , pp. 8961-8976
    • Hussack, G.1    Arbabi-Ghahroudi, M.2    Van Faassen, H.3    Songer, J.G.4    Ng, K.K.5    MacKenzie, R.6    Tanha, J.7
  • 44
    • 84884597711 scopus 로고    scopus 로고
    • United States Centers for Disease Control and Prevention, United States Department of Health and Human Services, Atlanta, GA
    • United States Centers for Disease Control and Prevention (2013) Antibiotic Resistance Threats in the United States, 2013, United States Department of Health and Human Services, Atlanta, GA
    • (2013) Antibiotic Resistance Threats in the United States, 2013


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.