메뉴 건너뛰기




Volumn 289, Issue 4, 2014, Pages 2331-2343

Structural basis for antibody recognition in the receptorbinding domains of toxins a and B from clostridium difficile

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; CLOSTRIDIUM; MASS SPECTROMETRY; SIZE EXCLUSION CHROMATOGRAPHY;

EID: 84893137156     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.505917     Document Type: Article
Times cited : (38)

References (40)
  • 1
    • 80053253206 scopus 로고    scopus 로고
    • Biology of Clostridium difficile. Implications for epidemiology and diagnosis
    • Carroll, K. C., and Bartlett, J. G. (2011) Biology of Clostridium difficile. Implications for epidemiology and diagnosis. Annu. Rev. Microbiol. 65, 501-521
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 501-521
    • Carroll, K.C.1    Bartlett, J.G.2
  • 2
    • 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
    • 84860605588 scopus 로고    scopus 로고
    • Clostridium difficile infection prevention. Biotherapeutics, immunologics, and vaccines
    • Gerding, D. N. (2012) Clostridium difficile infection prevention. Biotherapeutics, immunologics, and vaccines. Discov. Med. 13, 75-83
    • (2012) Discov. Med. , vol.13 , pp. 75-83
    • Gerding, D.N.1
  • 4
    • 84868014572 scopus 로고    scopus 로고
    • Clostridium difficile infections (CDI) in hospital stays, 2009, statistical brief #124
    • Agency for Healthcare Research and Quality, Rockville, MD
    • Lucado, J., Gould, C., and Elixhauser, A. (2012) Clostridium difficile infections (CDI) in hospital stays, 2009, statistical brief #124. in Healthcare Cost and Utilization Project (HCUP) Statistical Briefs, pp. 1-12, Agency for Healthcare Research and Quality, Rockville, MD
    • (2012) Healthcare Cost and Utilization Project (HCUP) Statistical Briefs , pp. 1-12
    • Lucado, J.1    Gould, C.2    Elixhauser, A.3
  • 5
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins. Mechanism of action and role in disease
    • Voth, D. E., and Ballard, J. D. (2005) Clostridium difficile toxins. Mechanism of action and role in disease. Clin. Microbiol. Rev. 18, 247-263
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 247-263
    • Voth, D.E.1    Ballard, J.D.2
  • 6
    • 77958004353 scopus 로고    scopus 로고
    • Medical microbiology. A toxin contest
    • Ballard, J. D. (2010) Medical microbiology. A toxin contest. Nature 467, 665-666
    • (2010) Nature , vol.467 , pp. 665-666
    • Ballard, J.D.1
  • 7
    • 33947260554 scopus 로고    scopus 로고
    • Rho-glucosylating Clostridium difficile toxins A and B. New insights into structure and function
    • Jank, T., Giesemann, T., and Aktories, K. (2007) Rho-glucosylating Clostridium difficile toxins A and B. New insights into structure and function. Glycobiology 17, 15R-22R
    • (2007) Glycobiology , vol.17
    • Jank, T.1    Giesemann, T.2    Aktories, K.3
  • 8
    • 79957761288 scopus 로고    scopus 로고
    • Super toxins from a super bug. Structure and function of Clostridium difficile toxins
    • Davies, A. H., Roberts, A. K., Shone, C. C., and Acharya, K. R. (2011) Super toxins from a super bug. Structure and function of Clostridium difficile toxins. Biochem. J. 436, 517-526
    • (2011) Biochem. J. , vol.436 , pp. 517-526
    • Davies, A.H.1    Roberts, A.K.2    Shone, C.C.3    Acharya, K.R.4
  • 9
    • 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, 1-14
    • (2012) Front. Cell. Infect. Microbiol. , vol.2 , pp. 1-14
    • Pruitt, R.N.1    Lacy, D.B.2
  • 10
    • 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
  • 12
    • 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
  • 14
    • 0031446325 scopus 로고    scopus 로고
    • The C-terminal ligand-binding domain of Clostridium difficile toxin A (TcdA) abrogates TcdA-specific binding to cells and prevents mouse lethality
    • Sauerborn, M., Leukel, P., and von Eichel-Streiber, C. (1997) The C-terminal ligand-binding domain of Clostridium difficile toxin A (TcdA) abrogates TcdA-specific binding to cells and prevents mouse lethality. FEMS Microbiol Lett. 155, 45-54
    • (1997) FEMS Microbiol Lett. , vol.155 , pp. 45-54
    • Sauerborn, M.1    Leukel, P.2    Von Eichel-Streiber, C.3
  • 15
    • 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
  • 17
    • 79959449569 scopus 로고    scopus 로고
    • Immunization with Bacillus spores expressing toxin A peptide repeats protects against infection with Clostridium difficile strains producing toxins A and B
    • Permpoonpattana, P., Hong, H. A., Phetcharaburanin, J., Huang, J. M., Cook, J., Fairweather, N. F., and Cutting, S. M. (2011) Immunization with Bacillus spores expressing toxin A peptide repeats protects against infection with Clostridium difficile strains producing toxins A and B. Infect. Immun. 79, 2295-2302
    • (2011) Infect. Immun. , vol.79 , pp. 2295-2302
    • Permpoonpattana, P.1    Hong, H.A.2    Phetcharaburanin, J.3    Huang, J.M.4    Cook, J.5    Fairweather, N.F.6    Cutting, S.M.7
  • 19
    • 67349187243 scopus 로고    scopus 로고
    • ADNAvaccine targeting the receptor-binding domain of Clostridium difficile toxin A
    • Gardiner, D. F., Rosenberg, T., Zaharatos, J., Franco, D., and Ho, D. D. (2009) ADNAvaccine targeting the receptor-binding domain of Clostridium difficile toxin A. Vaccine 27, 3598-3604
    • (2009) Vaccine , vol.27 , pp. 3598-3604
    • Gardiner, D.F.1    Rosenberg, T.2    Zaharatos, J.3    Franco, D.4    Ho, D.D.5
  • 21
    • 79952062024 scopus 로고    scopus 로고
    • Toxin-specific antibodies for the treatment of Clostridium difficile. Current status and future perspectives
    • Hussack, G., and Tanha, J. (2010) Toxin-specific antibodies for the treatment of Clostridium difficile. Current status and future perspectives. Toxins 2, 998-1018
    • (2010) Toxins , vol.2 , pp. 998-1018
    • Hussack, G.1    Tanha, J.2
  • 24
    • 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
  • 25
    • 84934440453 scopus 로고    scopus 로고
    • Isolation and characterization of Clostridium difficile toxin-specific single-domain antibodies
    • Hussack, G., Arbabi-Ghahroudi, M., Mackenzie, C. R., and Tanha, J. (2012) Isolation and characterization of Clostridium difficile toxin-specific single-domain antibodies. Methods Mol. Biol. 911, 211-239
    • (2012) Methods Mol. Biol. , vol.911 , pp. 211-239
    • Hussack, G.1    Arbabi-Ghahroudi, M.2    Mackenzie, C.R.3    Tanha, J.4
  • 26
    • 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
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R. J. (2001) Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. D 57, 1373-1382
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 32
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 33
    • 13244281317 scopus 로고    scopus 로고
    • Coot. Model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot. Model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 35
    • 0037197254 scopus 로고    scopus 로고
    • Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature
    • Tsodikov, O. V., Record, M. T., Jr., and Sergeev, Y. V. (2002) Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature. J. Comput. Chem. 23, 600-609
    • (2002) J. Comput. Chem. , vol.23 , pp. 600-609
    • Tsodikov, O.V.1    Record Jr., M.T.2    Sergeev, Y.V.3
  • 36
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence, M. C., and Colman, P. M. (1993) Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234, 946-950
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 38
    • 84878935042 scopus 로고    scopus 로고
    • Nanobodies. Natural single-domain antibodies
    • Muyldermans, S. (2013) Nanobodies. Natural single-domain antibodies. Annu. Rev. Biochem. 82, 775-797
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 775-797
    • Muyldermans, S.1
  • 39
    • 33745728310 scopus 로고    scopus 로고
    • Shapes of antibody binding sites. Qualitative and quantitative analyses based on a geomorphic classification scheme
    • Lee, M., Lloyd, P., Zhang, X., Schallhorn, J. M., Sugimoto, K., Leach, A. G., Sapiro, G., and Houk, K. N. (2006) Shapes of antibody binding sites. Qualitative and quantitative analyses based on a geomorphic classification scheme. J. Org Chem. 71, 5082-5092
    • (2006) J. Org Chem. , vol.71 , pp. 5082-5092
    • Lee, M.1    Lloyd, P.2    Zhang, X.3    Schallhorn, J.M.4    Sugimoto, K.5    Leach, A.G.6    Sapiro, G.7    Houk, K.N.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.