메뉴 건너뛰기




Volumn 590, Issue 24, 2016, Pages 4550-4563

Evidence for dual receptor-binding sites in Clostridium difficile toxin A

Author keywords

Clostridium difficile; receptor binding domain; TcdA

Indexed keywords

CLOSTRIDIUM DIFFICILE TOXIN A; BACTERIAL PROTEIN; BACTERIAL TOXIN; ENTEROTOXIN; OLIGOPEPTIDE; PROTEIN BINDING; RECOMBINANT PROTEIN; TCDA PROTEIN, CLOSTRIDIUM DIFFICILE; TOXB PROTEIN, CLOSTRIDIUM DIFFICILE;

EID: 85006162898     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1002/1873-3468.12487     Document Type: Article
Times cited : (4)

References (52)
  • 1
    • 55249105923 scopus 로고    scopus 로고
    • Clostridium difficile – more difficult than ever
    • Kelly CP and LaMont JT (2008) Clostridium difficile – more difficult than ever. N Engl J Med 359, 1932–1940.
    • (2008) N Engl J Med , vol.359 , pp. 1932-1940
    • Kelly, C.P.1    LaMont, J.T.2
  • 4
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins: mechanism of action and role in disease
    • Voth DE and Ballard JD (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
  • 5
    • 79959213985 scopus 로고    scopus 로고
    • Bacterial protein toxins that modify host regulatory GTPases
    • Aktories K (2011) Bacterial protein toxins that modify host regulatory GTPases. Nat Rev Microbiol 9, 487–498.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 487-498
    • Aktories, K.1
  • 6
    • 0033787469 scopus 로고    scopus 로고
    • Microbial toxins and the glycosylation of rho family GTPases
    • Busch C and Aktories K (2000) Microbial toxins and the glycosylation of rho family GTPases. Curr Opin Struct Biol 10, 528–535.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 528-535
    • Busch, C.1    Aktories, K.2
  • 10
    • 0030271882 scopus 로고    scopus 로고
    • Large clostridial cytotoxins – a family of glycosyltransferases modifying small GTP-binding proteins
    • von Eichel-Streiber C, Boquet P, Sauerborn M and Thelestam M (1996) Large clostridial cytotoxins – a family of glycosyltransferases modifying small GTP-binding proteins. Trends Microbiol 4, 375–382.
    • (1996) Trends Microbiol , vol.4 , pp. 375-382
    • von Eichel-Streiber, C.1    Boquet, P.2    Sauerborn, M.3    Thelestam, M.4
  • 11
    • 3042568878 scopus 로고    scopus 로고
    • Large clostridial cytotoxins: cellular biology of Rho/Ras-glucosylating toxins
    • Schirmer J and Aktories K (2004) Large clostridial cytotoxins: cellular biology of Rho/Ras-glucosylating toxins. Biochim Biophys Acta 1673, 66–74.
    • (2004) Biochim Biophys Acta , vol.1673 , pp. 66-74
    • Schirmer, J.1    Aktories, K.2
  • 12
    • 0030891386 scopus 로고    scopus 로고
    • Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxin
    • Hofmann F, Busch C, Prepens U, Just I and Aktories K (1997) Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxin. J Biol Chem 272, 11074–11078.
    • (1997) J Biol Chem , vol.272 , pp. 11074-11078
    • Hofmann, F.1    Busch, C.2    Prepens, U.3    Just, I.4    Aktories, K.5
  • 13
    • 0032831781 scopus 로고    scopus 로고
    • Monoglucosylation of RhoA at threonine 37 blocks cytosol-membrane cycling
    • Genth H, Aktories K and Just I (1999) Monoglucosylation of RhoA at threonine 37 blocks cytosol-membrane cycling. J Biol Chem 274, 29050–29056.
    • (1999) J Biol Chem , vol.274 , pp. 29050-29056
    • Genth, H.1    Aktories, K.2    Just, I.3
  • 14
    • 0032584665 scopus 로고    scopus 로고
    • A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins
    • Busch C, Hofmann F, Selzer J, Munro S, Jeckel D and Aktories K (1998) A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins. J Biol Chem 273, 19566–19572.
    • (1998) J Biol Chem , vol.273 , pp. 19566-19572
    • Busch, C.1    Hofmann, F.2    Selzer, J.3    Munro, S.4    Jeckel, D.5    Aktories, K.6
  • 15
    • 36849050145 scopus 로고    scopus 로고
    • Clostridium difficile glucosyltransferase toxin B-essential amino acids for substrate binding
    • Jank T, Giesemann T and Aktories K (2007) Clostridium difficile glucosyltransferase toxin B-essential amino acids for substrate binding. J Biol Chem 282, 35222–35231.
    • (2007) J Biol Chem , vol.282 , pp. 35222-35231
    • Jank, T.1    Giesemann, T.2    Aktories, K.3
  • 16
    • 23644460027 scopus 로고    scopus 로고
    • Structural basis for the function of Clostridium difficile toxin B
    • Reinert DJ, Jank T, Aktories K and Schulz GE (2005) Structural basis for the function of Clostridium difficile toxin B. J Mol Biol 351, 973–981.
    • (2005) J Mol Biol , vol.351 , pp. 973-981
    • Reinert, D.J.1    Jank, T.2    Aktories, K.3    Schulz, G.E.4
  • 18
    • 34548472183 scopus 로고    scopus 로고
    • Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity
    • Egerer M, Giesemann T, Jank T, Satchell KJ and Aktories K (2007) Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity. J Biol Chem 282, 25314–25321.
    • (2007) J Biol Chem , vol.282 , pp. 25314-25321
    • Egerer, M.1    Giesemann, T.2    Jank, T.3    Satchell, K.J.4    Aktories, K.5
  • 19
    • 69249090956 scopus 로고    scopus 로고
    • Structure-function analysis of inositol hexakisphosphate-induced autoprocessing in Clostridium difficile toxin A
    • Pruitt RN, Chagot B, Cover M, Chazin WJ, Spiller B and Lacy DB (2009) Structure-function analysis of inositol hexakisphosphate-induced autoprocessing in Clostridium difficile toxin A. J Biol Chem 284, 21934–21940.
    • (2009) J Biol Chem , vol.284 , pp. 21934-21940
    • Pruitt, R.N.1    Chagot, B.2    Cover, M.3    Chazin, W.J.4    Spiller, B.5    Lacy, D.B.6
  • 20
    • 79952418425 scopus 로고    scopus 로고
    • Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B
    • Genisyuerek S, Papatheodorou P, Guttenberg G, Schubert R, Benz R and Aktories K (2011) Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B. Mol Microbiol 79, 1643–1654.
    • (2011) Mol Microbiol , vol.79 , pp. 1643-1654
    • Genisyuerek, S.1    Papatheodorou, P.2    Guttenberg, G.3    Schubert, R.4    Benz, R.5    Aktories, K.6
  • 21
    • 63649106579 scopus 로고    scopus 로고
    • Autocatalytic processing of Clostridium difficile toxin B. Binding of inositol hexakisphosphate
    • Egerer M, Giesemann T, Herrmann C and Aktories K (2009) Autocatalytic processing of Clostridium difficile toxin B. Binding of inositol hexakisphosphate. J Biol Chem 284, 3389–3395.
    • (2009) J Biol Chem , vol.284 , pp. 3389-3395
    • Egerer, M.1    Giesemann, T.2    Herrmann, C.3    Aktories, K.4
  • 22
    • 0035815642 scopus 로고    scopus 로고
    • Low pH-induced formation of ion channels by Clostridium difficile toxin B in target cells
    • Barth H, Pfeifer G, Hofmann F, Maier E, Benz R and Aktories K (2001) Low pH-induced formation of ion channels by Clostridium difficile toxin B in target cells. J Biol Chem 276, 10670–10676.
    • (2001) J Biol Chem , vol.276 , pp. 10670-10676
    • Barth, H.1    Pfeifer, G.2    Hofmann, F.3    Maier, E.4    Benz, R.5    Aktories, K.6
  • 23
    • 0034114105 scopus 로고    scopus 로고
    • pH-induced conformational changes in Clostridium difficile toxin B
    • Qa'Dan M, Spyres LM and Ballard JD (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
  • 25
    • 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 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
  • 26
    • 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 and Lacy DB (2010) Structural organization of the functional domains of Clostridium difficile toxins A and B. Proc Natl Acad Sci USA 107, 13467–13472.
    • (2010) Proc Natl Acad Sci USA , 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
  • 27
    • 42749095602 scopus 로고    scopus 로고
    • Structure and mode of action of clostridial glucosylating toxins: the ABCD model
    • Jank T and Aktories K (2008) Structure and mode of action of clostridial glucosylating toxins: the ABCD model. Trends Microbiol 16, 222–229.
    • (2008) Trends Microbiol , vol.16 , pp. 222-229
    • Jank, T.1    Aktories, K.2
  • 28
    • 0025667927 scopus 로고
    • Clostridium difficile toxin A 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 toxin A 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
  • 29
    • 29444439842 scopus 로고    scopus 로고
    • Crystal structure of receptor-binding C-terminal repeats from Clostridium difficile toxin A
    • Ho JG, Greco A, Rupnik M and Ng KK (2005) Crystal structure of receptor-binding C-terminal repeats from Clostridium difficile toxin A. Proc Natl Acad Sci USA 102, 18373–18378.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18373-18378
    • Ho, J.G.1    Greco, A.2    Rupnik, M.3    Ng, K.K.4
  • 32
    • 0022525082 scopus 로고
    • Cell surface binding site for Clostridium difficile enterotoxin: evidence for a glycoconjugate containing the sequence Gal alpha 1-3Gal beta 1-4GlcNAc
    • Krivan HC, Clark GF, Smith DF and 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.
    • (1986) Infect Immun , vol.53 , pp. 573-581
    • Krivan, H.C.1    Clark, G.F.2    Smith, D.F.3    Wilkins, T.D.4
  • 33
    • 46449130378 scopus 로고    scopus 로고
    • gp96 is a human colonocyte plasma membrane binding protein for Clostridium difficile toxin A
    • Na X, Kim H, Moyer MP, Pothoulakis C and LaMont JT (2008) gp96 is a human colonocyte plasma membrane binding protein for Clostridium difficile toxin A. Infect Immun 76, 2862–2871.
    • (2008) Infect Immun , vol.76 , pp. 2862-2871
    • Na, X.1    Kim, H.2    Moyer, M.P.3    Pothoulakis, C.4    LaMont, J.T.5
  • 37
    • 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
  • 38
    • 84881571463 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium difficile TcdA and truncated TcdA lacking the receptor binding domain
    • Gerhard R, Frenzel E, Goy S and Olling A (2013) Cellular uptake of Clostridium difficile TcdA and truncated TcdA lacking the receptor binding domain. J Med Microbiol 62 (Pt 9), 1414–1422.
    • (2013) J Med Microbiol , vol.62 , pp. 1414-1422
    • Gerhard, R.1    Frenzel, E.2    Goy, S.3    Olling, A.4
  • 39
    • 34247229774 scopus 로고    scopus 로고
    • A novel toxin homologous to large clostridial cytotoxins found in culture supernatant of Clostridium perfringens type C
    • Amimoto K, Noro T, Oishi E and Shimizu M (2007) A novel toxin homologous to large clostridial cytotoxins found in culture supernatant of Clostridium perfringens type C. Microbiology 153 (Pt 9), 1198–1206.
    • (2007) Microbiology , vol.153 , pp. 1198-1206
    • Amimoto, K.1    Noro, T.2    Oishi, E.3    Shimizu, M.4
  • 40
    • 84864105928 scopus 로고    scopus 로고
    • Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells
    • Guttenberg G, Hornei S, Jank T, Schwan C, Lu W, Einsle O, Papatheodorou P and Aktories K (2012) Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells. J Biol Chem 287, 24929–24940.
    • (2012) J Biol Chem , vol.287 , pp. 24929-24940
    • Guttenberg, G.1    Hornei, S.2    Jank, T.3    Schwan, C.4    Lu, W.5    Einsle, O.6    Papatheodorou, P.7    Aktories, K.8
  • 42
    • 84930965989 scopus 로고    scopus 로고
    • Identification of an epithelial cell receptor responsible for Clostridium difficile TcdB-induced cytotoxicity
    • LaFrance ME, Farrow MA, Chandrasekaran R, Sheng J, Rubin DH and Lacy DB (2015) Identification of an epithelial cell receptor responsible for Clostridium difficile TcdB-induced cytotoxicity. Proc Natl Acad Sci U S A 112, 7073–7078.
    • (2015) Proc Natl Acad Sci U S A , vol.112 , pp. 7073-7078
    • LaFrance, M.E.1    Farrow, M.A.2    Chandrasekaran, R.3    Sheng, J.4    Rubin, D.H.5    Lacy, D.B.6
  • 44
    • 84922252575 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycan 4 functions as the cellular receptor for Clostridium difficile toxin B
    • Yuan P, Zhang H, Cai C, Zhu S, Zhou Y, Yang X, He R, Li C, Guo S, Li S et al. (2015) Chondroitin sulfate proteoglycan 4 functions as the cellular receptor for Clostridium difficile toxin B. Cell Res 25, 157–168.
    • (2015) Cell Res , vol.25 , pp. 157-168
    • Yuan, P.1    Zhang, H.2    Cai, C.3    Zhu, S.4    Zhou, Y.5    Yang, X.6    He, R.7    Li, C.8    Guo, S.9    Li, S.10
  • 46
    • 0041670743 scopus 로고    scopus 로고
    • Expression of recombinant Clostridium difficile toxin A using the Bacillus megaterium system
    • Burger S, Tatge H, Hofmann F, Genth H, Just I and Gerhard R (2003) Expression of recombinant Clostridium difficile toxin A using the Bacillus megaterium system. Biochem Biophys Res Commun 307, 584–588.
    • (2003) Biochem Biophys Res Commun , vol.307 , pp. 584-588
    • Burger, S.1    Tatge, H.2    Hofmann, F.3    Genth, H.4    Just, I.5    Gerhard, R.6
  • 47
    • 56649108115 scopus 로고    scopus 로고
    • Expression of recombinant Clostridium difficile toxin A and B in Bacillus megaterium
    • Yang G, Zhou B, Wang J, He X, Sun X, Nie W, Tzipori S and Feng H (2008) Expression of recombinant Clostridium difficile toxin A and B in Bacillus megaterium. BMC Microbiol 8, 192.
    • (2008) BMC Microbiol , vol.8 , pp. 192
    • Yang, G.1    Zhou, B.2    Wang, J.3    He, X.4    Sun, X.5    Nie, W.6    Tzipori, S.7    Feng, H.8
  • 48
    • 84955254203 scopus 로고    scopus 로고
    • Binding and entry of Clostridium difficile toxin B is mediated by multiple domains
    • Manse JS and Baldwin MR (2015) Binding and entry of Clostridium difficile toxin B is mediated by multiple domains. FEBS Lett 589 (Pt B), 3945–51.
    • (2015) FEBS Lett , vol.589 , pp. 3945-3951
    • Manse, J.S.1    Baldwin, M.R.2
  • 49
    • 0347994116 scopus 로고    scopus 로고
    • On the analysis of membrane protein circular dichroism spectra
    • Sreerama N and Woody RW (2004) On the analysis of membrane protein circular dichroism spectra. Protein Sci 13, 100–112.
    • (2004) Protein Sci , vol.13 , pp. 100-112
    • Sreerama, N.1    Woody, R.W.2
  • 51
    • 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 and 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.
    • (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
  • 52
    • 84918515229 scopus 로고    scopus 로고
    • The combined repetitive oligopeptides of Clostridium difficile toxin A counteract premature cleavage of the glucosyl-transferase domain by stabilizing protein conformation
    • Olling A, Huls C, Goy S, Muller M, Krooss S, Rudolf I, Tatge H and Gerhard R (2014) The combined repetitive oligopeptides of Clostridium difficile toxin A counteract premature cleavage of the glucosyl-transferase domain by stabilizing protein conformation. Toxins (Basel) 6, 2162–2176.
    • (2014) Toxins (Basel) , vol.6 , pp. 2162-2176
    • Olling, A.1    Huls, C.2    Goy, S.3    Muller, M.4    Krooss, S.5    Rudolf, I.6    Tatge, H.7    Gerhard, R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.