메뉴 건너뛰기




Volumn 83, Issue 1, 2015, Pages 405-416

Toxin-mediated paracellular transport of antitoxin antibodies facilitates protection against Clostridium difficile infection

Author keywords

[No Author keywords available]

Indexed keywords

ACTOXUMAB; ANTIBODY; ANTITOXIN ANTIBODY; BACTERIAL TOXIN; BEZLOTOXUMAB; FC RECEPTOR; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; ANTITOXIN; BACTERIAL PROTEIN; BACTERIUM ANTIBODY; ENTEROTOXIN; FC RECEPTOR, NEONATAL; HLA ANTIGEN CLASS 1; TCDA PROTEIN, CLOSTRIDIUM DIFFICILE; TOXB PROTEIN, CLOSTRIDIUM DIFFICILE;

EID: 84919478422     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.02550-14     Document Type: Article
Times cited : (40)

References (41)
  • 1
    • 3142680740 scopus 로고    scopus 로고
    • Clostridium difficile-associated diarrhea in adults
    • Poutanen SM, Simor AE. 2004. Clostridium difficile-associated diarrhea in adults. CMAJ 171:51-58. http://dx.doi.org/10.1503/cmaj.1031189.
    • (2004) CMAJ , vol.171 , pp. 51-58
    • Poutanen, S.M.1    Simor, A.E.2
  • 2
    • 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 7:526-536. http://dx.doi.org/10.1038/nrmicro2164.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 526-536
    • Rupnik, M.1    Wilcox, M.H.2    Gerding, D.N.3
  • 3
    • 42749095602 scopus 로고    scopus 로고
    • Structure and mode of action of clostridial glucosylating toxins: the ABCD model
    • Jank T, Aktories K. 2008. Structure and mode of action of clostridial glucosylating toxins: the ABCD model. Trends Microbiol 16:222-229. http://dx.doi.org/10.1016/j.tim.2008.01.011.
    • (2008) Trends Microbiol , vol.16 , pp. 222-229
    • Jank, T.1    Aktories, K.2
  • 4
    • 84878486491 scopus 로고    scopus 로고
    • Toward a structural understanding of Clostridium difficile toxins A and B
    • Pruitt RN, Lacy DB. 2012. Toward a structural understanding of Clostridium difficile toxins A and B. Front Cell Infect Microbiol 2:28. http://dx.doi.org/10.3389/fcimb.2012.00028.
    • (2012) Front Cell Infect Microbiol , vol.2 , pp. 28
    • Pruitt, R.N.1    Lacy, D.B.2
  • 5
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins: mechanism of action and role in disease
    • Voth DE, Ballard JD. 2005. Clostridium difficile toxins: mechanism of action and role in disease. Clin Microbiol Rev 18:247-263. http://dx.doi.org/10.1128/CMR.18.2.247-263.2005.
    • (2005) Clin Microbiol Rev , vol.18 , pp. 247-263
    • Voth, D.E.1    Ballard, J.D.2
  • 6
    • 77956461530 scopus 로고    scopus 로고
    • Clostridial glucosylating toxins enter cells via clathrin-mediated endocytosis
    • Papatheodorou P, Zamboglou C, Genisyuerek S, Guttenberg G, Aktories K. 2010. Clostridial glucosylating toxins enter cells via clathrin-mediated endocytosis. PLoS One 5:e10673. http://dx.doi.org/10.1371/journal.pone.0010673.
    • (2010) PLoS One , vol.5
    • Papatheodorou, P.1    Zamboglou, C.2    Genisyuerek, S.3    Guttenberg, G.4    Aktories, K.5
  • 8
    • 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 DK, Aktories K, 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. http://dx.doi.org/10.1074/jbc.M307540200.
    • (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
  • 9
    • 0034114105 scopus 로고    scopus 로고
    • pH-induced conformational changes in Clostridium difficile toxin B
    • Qa'Dan M, Spyres LM, Ballard JD. 2000. pH-induced conformational changes in Clostridium difficile toxin B. Infect Immun 68:2470-2474. http://dx.doi.org/10.1128/IAI.68.5.2470-2474.2000.
    • (2000) Infect Immun , vol.68 , pp. 2470-2474
    • Qa'Dan, M.1    Spyres, L.M.2    Ballard, J.D.3
  • 10
    • 84896259912 scopus 로고    scopus 로고
    • Translocation domain mutations affecting cellular toxicity identify the Clostridium difficile toxin B pore
    • Zhang Z, Park M, Tam J, Auger A, Beilhartz GL, Lacy DB, Melnyk RA. 2014. Translocation domain mutations affecting cellular toxicity identify the Clostridium difficile toxin B pore. Proc Natl Acad Sci U S A 111:3721-3726. http://dx.doi.org/10.1073/pnas.1400680111.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 3721-3726
    • Zhang, Z.1    Park, M.2    Tam, J.3    Auger, A.4    Beilhartz, G.L.5    Lacy, D.B.6    Melnyk, R.A.7
  • 12
    • 0029054398 scopus 로고
    • Glucosylation of Rho proteins by Clostridium difficile toxin B
    • Just I, Selzer J, Wilm M, von Eichel-Streiber C, Mann M, Aktories K. 1995. Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature 375:500-503. http://dx.doi.org/10.1038/375500a0.
    • (1995) Nature , vol.375 , pp. 500-503
    • Just, I.1    Selzer, J.2    Wilm, M.3    von Eichel-Streiber, C.4    Mann, M.5    Aktories, K.6
  • 13
    • 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. http://dx.doi.org/10.1159/000332946.
    • (2012) J Innate Immun , vol.4 , pp. 149-158
    • Shen, A.1
  • 14
    • 84871463724 scopus 로고    scopus 로고
    • Epidemiology, diagnosis and treatment of Clostridium difficile infection
    • Bassetti M, Villa G, Pecori D, Arzese A, Wilcox M. 2012. Epidemiology, diagnosis and treatment of Clostridium difficile infection. Expert Rev Anti Infect Ther 10:1405-1423. http://dx.doi.org/10.1586/eri.12.135.
    • (2012) Expert Rev Anti Infect Ther , vol.10 , pp. 1405-1423
    • Bassetti, M.1    Villa, G.2    Pecori, D.3    Arzese, A.4    Wilcox, M.5
  • 15
    • 0034628426 scopus 로고    scopus 로고
    • Asymptomatic carriage of Clostridium difficile and serum levels of IgG antibody against toxin A
    • Kyne L, Warny M, Qamar A, Kelly CP. 2000. Asymptomatic carriage of Clostridium difficile and serum levels of IgG antibody against toxin A. NEngl J Med 342:390-397. http://dx.doi.org/10.1056/NEJM200002103420604.
    • (2000) NEngl J Med , vol.342 , pp. 390-397
    • Kyne, L.1    Warny, M.2    Qamar, A.3    Kelly, C.P.4
  • 16
    • 0035915688 scopus 로고    scopus 로고
    • Association between antibody response to toxin A and protection against recurrent Clostridium difficile diarrhoea
    • Kyne L, Warny M, Qamar A, Kelly CP. 2001. Association between antibody response to toxin A and protection against recurrent Clostridium difficile diarrhoea. Lancet 357:189-193. http://dx.doi.org/10.1016/S0140-6736(00)03592-3.
    • (2001) Lancet , vol.357 , pp. 189-193
    • Kyne, L.1    Warny, M.2    Qamar, A.3    Kelly, C.P.4
  • 20
    • 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 JA, Williams JA. 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
  • 21
    • 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, Tzipori S. 2013. Antibody against TcdB, but not TcdA, prevents development of gastrointestinal and systemic Clostridium difficile disease. J Infect Dis 207:323-330. http://dx.doi.org/10.1093/infdis/jis669.
    • (2013) J Infect Dis , vol.207 , pp. 323-330
    • Steele, J.1    Mukherjee, J.2    Parry, N.3    Tzipori, S.4
  • 22
    • 79959413785 scopus 로고    scopus 로고
    • Mouse relapse model of Clostridium difficile infection
    • Sun X, Wang H, Zhang Y, Chen K, Davis B, Feng H. 2011. Mouse relapse model of Clostridium difficile infection. Infect Immun 79:2856-2864. http://dx.doi.org/10.1128/IAI.01336-10.
    • (2011) Infect Immun , vol.79 , pp. 2856-2864
    • Sun, X.1    Wang, H.2    Zhang, Y.3    Chen, K.4    Davis, B.5    Feng, H.6
  • 24
    • 0037008670 scopus 로고    scopus 로고
    • Functional reconstitution of human FcRn in Madin-Darby canine kidney cells requires co-expressed human beta 2-microglobulin
    • Claypool SM, Dickinson BL, Yoshida M, Lencer WI, Blumberg RS. 2002. Functional reconstitution of human FcRn in Madin-Darby canine kidney cells requires co-expressed human beta 2-microglobulin. J Biol Chem 277:28038-28050. http://dx.doi.org/10.1074/jbc.M202367200.
    • (2002) J Biol Chem , vol.277 , pp. 28038-28050
    • Claypool, S.M.1    Dickinson, B.L.2    Yoshida, M.3    Lencer, W.I.4    Blumberg, R.S.5
  • 29
    • 2942516894 scopus 로고    scopus 로고
    • Human neonatal Fc receptor mediates transport of IgG into luminal secretions for delivery of antigens to mucosal dendritic cells
    • Yoshida M, Claypool SM, Wagner JS, Mizoguchi E, Mizoguchi A, Roopenian DC, Lencer WI, Blumberg RS. 2004. Human neonatal Fc receptor mediates transport of IgG into luminal secretions for delivery of antigens to mucosal dendritic cells. Immunity 20:769-783. http://dx.doi.org/10.1016/j.immuni.2004.05.007.
    • (2004) Immunity , vol.20 , pp. 769-783
    • Yoshida, M.1    Claypool, S.M.2    Wagner, J.S.3    Mizoguchi, E.4    Mizoguchi, A.5    Roopenian, D.C.6    Lencer, W.I.7    Blumberg, R.S.8
  • 30
    • 2442667691 scopus 로고    scopus 로고
    • Translocation of Clostridium difficile toxin B across polarized Caco-2 cell monolayers is enhanced by toxin A
    • Du T, Alfa MJ. 2004. Translocation of Clostridium difficile toxin B across polarized Caco-2 cell monolayers is enhanced by toxin A. Can J Infect Dis 15:83-88.
    • (2004) Can J Infect Dis , vol.15 , pp. 83-88
    • Du, T.1    Alfa, M.J.2
  • 31
    • 0035112067 scopus 로고    scopus 로고
    • Clostridium difficile toxins disrupt epithelial barrier function by altering membrane microdomain localization of tight junction proteins
    • Nusrat A, von Eichel-Streiber C, Turner JR, Verkade P, Madara JL, Parkos CA. 2001. Clostridium difficile toxins disrupt epithelial barrier function by altering membrane microdomain localization of tight junction proteins. Infect Immun 69:1329-1336. http://dx.doi.org/10.1128/IAI.69.3.1329-1336.2001.
    • (2001) Infect Immun , vol.69 , pp. 1329-1336
    • Nusrat, A.1    von Eichel-Streiber, C.2    Turner, J.R.3    Verkade, P.4    Madara, J.L.5    Parkos, C.A.6
  • 32
    • 20044371666 scopus 로고    scopus 로고
    • The Caco-2 cell line as a model of the intestinal barrier: influence of cell and culture-related factors on Caco-2 cell functional characteristics
    • Sambuy Y, De Angelis I, Ranaldi G, Scarino ML, Stammati A, Zucco F. 2005. The Caco-2 cell line as a model of the intestinal barrier: influence of cell and culture-related factors on Caco-2 cell functional characteristics. Cell Biol Toxicol 21:1-26. http://dx.doi.org/10.1007/s10565-005-0085-6.
    • (2005) Cell Biol Toxicol , vol.21 , pp. 1-26
    • Sambuy, Y.1    De Angelis, I.2    Ranaldi, G.3    Scarino, M.L.4    Stammati, A.5    Zucco, F.6
  • 33
    • 49649103133 scopus 로고    scopus 로고
    • Essential role of toxin A in C. difficile 027 and reference strain supernatant-mediated disruption of Caco-2 intestinal epithelial barrier function
    • Sutton PA, Li S, Webb J, Solomon K, Brazier J, Mahida YR. 2008. Essential role of toxin A in C. difficile 027 and reference strain supernatant-mediated disruption of Caco-2 intestinal epithelial barrier function. Clin Exp Immunol 153:439-447. http://dx.doi.org/10.1111/j.1365-2249.2008.03690.x.
    • (2008) Clin Exp Immunol , vol.153 , pp. 439-447
    • Sutton, P.A.1    Li, S.2    Webb, J.3    Solomon, K.4    Brazier, J.5    Mahida, Y.R.6
  • 35
    • 34248593791 scopus 로고    scopus 로고
    • Restoration of barrier function in injured intestinal mucosa
    • Blikslager AT, Moeser AJ, Gookin JL, Jones SL, Odle J. 2007. Restoration of barrier function in injured intestinal mucosa. Physiol Rev 87:545-564. http://dx.doi.org/10.1152/physrev.00012.2006.
    • (2007) Physiol Rev , vol.87 , pp. 545-564
    • Blikslager, A.T.1    Moeser, A.J.2    Gookin, J.L.3    Jones, S.L.4    Odle, J.5
  • 36
    • 78650541367 scopus 로고    scopus 로고
    • Immunology of gut mucosal vaccines
    • Pasetti MF, Simon JK, Sztein MB, Levine MM. 2011. Immunology of gut mucosal vaccines. Immunol Rev 239:125-148. http://dx.doi.org/10.1111/j.1600-065X.2010.00970.x.
    • (2011) Immunol Rev , vol.239 , pp. 125-148
    • Pasetti, M.F.1    Simon, J.K.2    Sztein, M.B.3    Levine, M.M.4
  • 37
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: the neonatal Fc receptor comes of age
    • Roopenian DC, Akilesh S. 2007. FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunol 7:715-725. http://dx.doi.org/10.1038/nri2155.
    • (2007) Nat Rev Immunol , vol.7 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 38
    • 84893014123 scopus 로고    scopus 로고
    • Protection from Clostridium difficile infection in CD4 T cell-and polymeric immunoglobulin receptor-deficient mice
    • Johnston PF, Gerding DN, Knight KL. 2014. Protection from Clostridium difficile infection in CD4 T cell-and polymeric immunoglobulin receptor-deficient mice. Infect Immun 82:522-531. http://dx.doi.org/10.1128/IAI.01273-13.
    • (2014) Infect Immun , vol.82 , pp. 522-531
    • Johnston, P.F.1    Gerding, D.N.2    Knight, K.L.3
  • 39
    • 33749023005 scopus 로고    scopus 로고
    • Identification of Clostridium difficile toxin B cardiotoxicity using a zebrafish embryo model of intoxication
    • Hamm EE, Voth DE, Ballard JD. 2006. Identification of Clostridium difficile toxin B cardiotoxicity using a zebrafish embryo model of intoxication. Proc Natl Acad Sci U S A 103:14176-14181. http://dx.doi.org/10.1073/pnas.0604725103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 14176-14181
    • Hamm, E.E.1    Voth, D.E.2    Ballard, J.D.3
  • 40
    • 84862907897 scopus 로고    scopus 로고
    • Systemic dissemination of Clostridium difficile toxins A and B is associated with severe, fatal disease in animal models
    • Steele J, Chen K, Sun X, Zhang Y, Wang H, Tzipori S, Feng H. 2012. Systemic dissemination of Clostridium difficile toxins A and B is associated with severe, fatal disease in animal models. J Infect Dis 205:384-391. http://dx.doi.org/10.1093/infdis/jir748.
    • (2012) J Infect Dis , vol.205 , pp. 384-391
    • Steele, J.1    Chen, K.2    Sun, X.3    Zhang, Y.4    Wang, H.5    Tzipori, S.6    Feng, H.7
  • 41
    • 0037369552 scopus 로고    scopus 로고
    • Intestinal epithelial responses to enteric pathogens: effects on the tight junction barrier, ion transport, and inflammation
    • Berkes J, Viswanathan VK, Savkovic SD, Hecht G. 2003. Intestinal epithelial responses to enteric pathogens: effects on the tight junction barrier, ion transport, and inflammation. Gut 52:439-451. http://dx.doi.org/10.1136/gut.52.3.439.
    • (2003) Gut , vol.52 , pp. 439-451
    • Berkes, J.1    Viswanathan, V.K.2    Savkovic, S.D.3    Hecht, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.