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Volumn 17, Issue 8, 2015, Pages 1133-1143

Translocation of botulinum neurotoxin serotype A and associated proteins across the intestinal epithelia

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM TOXIN A; NEUROTOXIN ASSOCIATED PROTEIN; PROTEIN; UNCLASSIFIED DRUG; CARRIER PROTEIN; MACROMOLECULE;

EID: 84937163658     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/cmi.12424     Document Type: Article
Times cited : (18)

References (40)
  • 1
    • 27744456489 scopus 로고    scopus 로고
    • Visualization of binding and transcytosis of botulinum toxin by human intestinal epithelial cells
    • Ahsan, C.R., Hajnoczky, G., Maksymowych, A.B., and Simpson, L.L. (2005) Visualization of binding and transcytosis of botulinum toxin by human intestinal epithelial cells. J Pharmacol Exp Ther 315: 1028-1035.
    • (2005) J Pharmacol Exp Ther , vol.315 , pp. 1028-1035
    • Ahsan, C.R.1    Hajnoczky, G.2    Maksymowych, A.B.3    Simpson, L.L.4
  • 2
    • 84870827073 scopus 로고    scopus 로고
    • Analysis of the mechanisms that underlie absorption of botulinum toxin by the inhalation route
    • Al-Saleem, F.H., Ancharski, D.M., Joshi, S.G., Elias, M., Singh, A., Nasser, Z., and Simpson, L.L. (2012) Analysis of the mechanisms that underlie absorption of botulinum toxin by the inhalation route. Infect Immun 80: 4133-4142.
    • (2012) Infect Immun , vol.80 , pp. 4133-4142
    • Al-Saleem, F.H.1    Ancharski, D.M.2    Joshi, S.G.3    Elias, M.4    Singh, A.5    Nasser, Z.6    Simpson, L.L.7
  • 4
    • 84878658076 scopus 로고    scopus 로고
    • Substrates and controls for the quantitative detection of active botulinum neurotoxin in protease-containing samples
    • Bagramyan, K., Kaplan, B.E., Cheng, L.W., Strotmeier, J., Rummel, A., and Kalkum, M. (2013) Substrates and controls for the quantitative detection of active botulinum neurotoxin in protease-containing samples. Anal Chem 85: 5569-5576.
    • (2013) Anal Chem , vol.85 , pp. 5569-5576
    • Bagramyan, K.1    Kaplan, B.E.2    Cheng, L.W.3    Strotmeier, J.4    Rummel, A.5    Kalkum, M.6
  • 5
    • 84891543590 scopus 로고    scopus 로고
    • A novel strain of Clostridium botulinum that produces type B and type H botulinum toxins
    • Barash, J.R., and Arnon, S.S. (2014) A novel strain of Clostridium botulinum that produces type B and type H botulinum toxins. J Infect Dis 209: 183-191.
    • (2014) J Infect Dis , vol.209 , pp. 183-191
    • Barash, J.R.1    Arnon, S.S.2
  • 6
    • 26044454078 scopus 로고    scopus 로고
    • Medical aspects of toxin weapons
    • Bigalke, H., and Rummel, A. (2005) Medical aspects of toxin weapons. Toxicology 214: 210-220.
    • (2005) Toxicology , vol.214 , pp. 210-220
    • Bigalke, H.1    Rummel, A.2
  • 7
    • 0031866118 scopus 로고    scopus 로고
    • Biophysical characterization of the stability of the 150-kilodalton botulinum toxin, the nontoxic component, and the 900-kilodalton botulinum toxin complex species
    • Chen, F., Kuziemko, G.M., and Stevens, R.C. (1998) Biophysical characterization of the stability of the 150-kilodalton botulinum toxin, the nontoxic component, and the 900-kilodalton botulinum toxin complex species. Infect Immun 66: 2420-2425.
    • (1998) Infect Immun , vol.66 , pp. 2420-2425
    • Chen, F.1    Kuziemko, G.M.2    Stevens, R.C.3
  • 8
    • 46249127036 scopus 로고    scopus 로고
    • Effects of purification on the bioavailability of botulinum neurotoxin type A
    • Cheng, L.W., Onisko, B., Johnson, E.A., Reader, J.R., Griffey, S.M., Larson, A.E., etal. (2008) Effects of purification on the bioavailability of botulinum neurotoxin type A. Toxicology 249: 123-129.
    • (2008) Toxicology , vol.249 , pp. 123-129
    • Cheng, L.W.1    Onisko, B.2    Johnson, E.A.3    Reader, J.R.4    Griffey, S.M.5    Larson, A.E.6
  • 9
    • 70349432307 scopus 로고    scopus 로고
    • Antibody protection against botulinum neurotoxin intoxication in mice
    • Cheng, L.W., Stanker, L.H., Henderson, T.D., 2nd, Lou, J., and Marks, J.D. (2009) Antibody protection against botulinum neurotoxin intoxication in mice. Infect Immun 77: 4305-4313.
    • (2009) Infect Immun , vol.77 , pp. 4305-4313
    • Cheng, L.W.1    Stanker, L.H.2    Henderson, T.D.3    Lou, J.4    Marks, J.D.5
  • 10
    • 84861215299 scopus 로고    scopus 로고
    • Preferential entry of botulinum neurotoxin A Hc domain through intestinal crypt cells and targeting to cholinergic neurons of the mouse intestine
    • Couesnon, A., Molgo, J., Connan, C., and Popoff, M.R. (2012) Preferential entry of botulinum neurotoxin A Hc domain through intestinal crypt cells and targeting to cholinergic neurons of the mouse intestine. PLoS Pathog 8: e1002583.
    • (2012) PLoS Pathog , vol.8
    • Couesnon, A.1    Molgo, J.2    Connan, C.3    Popoff, M.R.4
  • 11
    • 79952364126 scopus 로고    scopus 로고
    • Studies on the dissociation of botulinum neurotoxin type A complexes
    • Eisele, K.H., Fink, K., Vey, M., and Taylor, H.V. (2011) Studies on the dissociation of botulinum neurotoxin type A complexes. Toxicon 57: 555-565.
    • (2011) Toxicon , vol.57 , pp. 555-565
    • Eisele, K.H.1    Fink, K.2    Vey, M.3    Taylor, H.V.4
  • 12
    • 77954575803 scopus 로고    scopus 로고
    • Interaction of botulinum toxin with the epithelial barrier
    • Fujinaga, Y. (2010) Interaction of botulinum toxin with the epithelial barrier. J Biomed Biotechnol 2010: 974943.
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 974943
    • Fujinaga, Y.1
  • 13
    • 68849102962 scopus 로고    scopus 로고
    • A novel function of botulinum toxin-associated proteins: HA proteins disrupt intestinal epithelial barrier to increase toxin absorption
    • Fujinaga, Y., Matsumura, T., Jin, Y., Takegahara, Y., and Sugawara, Y. (2009) A novel function of botulinum toxin-associated proteins: HA proteins disrupt intestinal epithelial barrier to increase toxin absorption. Toxicon 54: 583-586.
    • (2009) Toxicon , vol.54 , pp. 583-586
    • Fujinaga, Y.1    Matsumura, T.2    Jin, Y.3    Takegahara, Y.4    Sugawara, Y.5
  • 14
    • 84863229206 scopus 로고    scopus 로고
    • Botulinum neurotoxin is shielded by NTNHA in an interlocked complex
    • Gu, S., Rumpel, S., Zhou, J., Strotmeier, J., Bigalke, H., Perry, K., etal. (2012) Botulinum neurotoxin is shielded by NTNHA in an interlocked complex. Science 335: 977-981.
    • (2012) Science , vol.335 , pp. 977-981
    • Gu, S.1    Rumpel, S.2    Zhou, J.3    Strotmeier, J.4    Bigalke, H.5    Perry, K.6
  • 15
    • 34548312483 scopus 로고    scopus 로고
    • A novel subunit structure of Clostridium botulinum serotype D toxin complex with three extended arms
    • Hasegawa, K., Watanabe, T., Suzuki, T., Yamano, A., Oikawa, T., Sato, Y., etal. (2007) A novel subunit structure of Clostridium botulinum serotype D toxin complex with three extended arms. J Biol Chem 282: 24777-24783.
    • (2007) J Biol Chem , vol.282 , pp. 24777-24783
    • Hasegawa, K.1    Watanabe, T.2    Suzuki, T.3    Yamano, A.4    Oikawa, T.5    Sato, Y.6
  • 17
    • 23744508421 scopus 로고    scopus 로고
    • Characterization of botulinum progenitor toxins by mass spectrometry
    • Hines, H.B., Lebeda, F., Hale, M., and Brueggemann, E.E. (2005) Characterization of botulinum progenitor toxins by mass spectrometry. Appl Environ Microbiol 71: 4478-4486.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 4478-4486
    • Hines, H.B.1    Lebeda, F.2    Hale, M.3    Brueggemann, E.E.4
  • 18
    • 0029877553 scopus 로고    scopus 로고
    • Molecular composition of Clostridium botulinum type A progenitor toxins
    • Inoue, K., Fujinaga, Y., Watanabe, T., Ohyama, T., Takeshi, K., Moriishi, K., etal. (1996) Molecular composition of Clostridium botulinum type A progenitor toxins. Infect Immun 64: 1589-1594.
    • (1996) Infect Immun , vol.64 , pp. 1589-1594
    • Inoue, K.1    Fujinaga, Y.2    Watanabe, T.3    Ohyama, T.4    Takeshi, K.5    Moriishi, K.6
  • 19
    • 79952612789 scopus 로고    scopus 로고
    • HA-33 facilitates transport of the serotype D botulinum toxin across a rat intestinal epithelial cell monolayer
    • Ito, H., Sagane, Y., Miyata, K., Inui, K., Matsuo, T., Horiuchi, R., etal. (2011) HA-33 facilitates transport of the serotype D botulinum toxin across a rat intestinal epithelial cell monolayer. FEMS Immunol Med Microbiol 61: 323-331.
    • (2011) FEMS Immunol Med Microbiol , vol.61 , pp. 323-331
    • Ito, H.1    Sagane, Y.2    Miyata, K.3    Inui, K.4    Matsuo, T.5    Horiuchi, R.6
  • 20
    • 61449163955 scopus 로고    scopus 로고
    • Disruption of the epithelial barrier by botulinum haemagglutinin (HA) proteins - differences in cell tropism and the mechanism of action between HA proteins of types A or B, and HA proteins of type C
    • Jin, Y., Takegahara, Y., Sugawara, Y., Matsumura, T., and Fujinaga, Y. (2009) Disruption of the epithelial barrier by botulinum haemagglutinin (HA) proteins - differences in cell tropism and the mechanism of action between HA proteins of types A or B, and HA proteins of type C. Microbiology 155: 35-45.
    • (2009) Microbiology , vol.155 , pp. 35-45
    • Jin, Y.1    Takegahara, Y.2    Sugawara, Y.3    Matsumura, T.4    Fujinaga, Y.5
  • 21
    • 84887286760 scopus 로고    scopus 로고
    • Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity
    • Lee, K., Gu, S., Jin, L., Le, T.T., Cheng, L.W., Strotmeier, J., etal. (2013) Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity. PLoS Pathog 9: e1003690.
    • (2013) PLoS Pathog , vol.9
    • Lee, K.1    Gu, S.2    Jin, L.3    Le, T.T.4    Cheng, L.W.5    Strotmeier, J.6
  • 22
    • 84902682720 scopus 로고    scopus 로고
    • Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex
    • Lee, K., Zhong, X., Gu, S., Kruel, A.M., Dorner, M.B., Perry, K., etal. (2014) Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex. Science 344: 1405-1410.
    • (2014) Science , vol.344 , pp. 1405-1410
    • Lee, K.1    Zhong, X.2    Gu, S.3    Kruel, A.M.4    Dorner, M.B.5    Perry, K.6
  • 23
    • 0032555584 scopus 로고    scopus 로고
    • Binding and transcytosis of botulinum neurotoxin by polarized human colon carcinoma cells
    • Maksymowych, A.B., and Simpson, L.L. (1998) Binding and transcytosis of botulinum neurotoxin by polarized human colon carcinoma cells. J Biol Chem 273: 21950-21957.
    • (1998) J Biol Chem , vol.273 , pp. 21950-21957
    • Maksymowych, A.B.1    Simpson, L.L.2
  • 24
    • 3342955474 scopus 로고    scopus 로고
    • Structural features of the botulinum neurotoxin molecule that govern binding and transcytosis across polarized human intestinal epithelial cells
    • Maksymowych, A.B., and Simpson, L.L. (2004) Structural features of the botulinum neurotoxin molecule that govern binding and transcytosis across polarized human intestinal epithelial cells. J Pharmacol Exp Ther 310: 633-641.
    • (2004) J Pharmacol Exp Ther , vol.310 , pp. 633-641
    • Maksymowych, A.B.1    Simpson, L.L.2
  • 25
    • 0032767291 scopus 로고    scopus 로고
    • Pure botulinum neurotoxin is absorbed from the stomach and small intestine and produces peripheral neuromuscular blockade
    • Maksymowych, A.B., Reinhard, M., Malizio, C.J., Goodnough, M.C., Johnson, E.A., and Simpson, L.L. (1999) Pure botulinum neurotoxin is absorbed from the stomach and small intestine and produces peripheral neuromuscular blockade. Infect Immun 67: 4708-4712.
    • (1999) Infect Immun , vol.67 , pp. 4708-4712
    • Maksymowych, A.B.1    Reinhard, M.2    Malizio, C.J.3    Goodnough, M.C.4    Johnson, E.A.5    Simpson, L.L.6
  • 26
    • 38049150493 scopus 로고    scopus 로고
    • The HA proteins of botulinum toxin disrupt intestinal epithelial intercellular junctions to increase toxin absorption
    • Matsumura, T., Jin, Y., Kabumoto, Y., Takegahara, Y., Oguma, K., Lencer, W.I., and Fujinaga, Y. (2008) The HA proteins of botulinum toxin disrupt intestinal epithelial intercellular junctions to increase toxin absorption. Cell Microbiol 10: 355-364.
    • (2008) Cell Microbiol , vol.10 , pp. 355-364
    • Matsumura, T.1    Jin, Y.2    Kabumoto, Y.3    Takegahara, Y.4    Oguma, K.5    Lencer, W.I.6    Fujinaga, Y.7
  • 27
    • 0028310404 scopus 로고
    • Mechanism of action of tetanus and botulinum neurotoxins
    • Montecucco, C., and Schiavo, G. (1994) Mechanism of action of tetanus and botulinum neurotoxins. Mol Microbiol 13: 1-8.
    • (1994) Mol Microbiol , vol.13 , pp. 1-8
    • Montecucco, C.1    Schiavo, G.2
  • 28
    • 0030461941 scopus 로고    scopus 로고
    • Bacterial protein toxins and cell vesicle trafficking
    • Montecucco, C., Papini, E., and Schiavo, G. (1996) Bacterial protein toxins and cell vesicle trafficking. Experientia 52: 1026-1032.
    • (1996) Experientia , vol.52 , pp. 1026-1032
    • Montecucco, C.1    Papini, E.2    Schiavo, G.3
  • 29
    • 80055120794 scopus 로고    scopus 로고
    • Transcytosis of Listeria monocytogenes across the intestinal barrier upon specific targeting of goblet cell accessible E-cadherin
    • Nikitas, G., Deschamps, C., Disson, O., Niault, T., Cossart, P., and Lecuit, M. (2011) Transcytosis of Listeria monocytogenes across the intestinal barrier upon specific targeting of goblet cell accessible E-cadherin. J Exp Med 11: 2263-2277.
    • (2011) J Exp Med , vol.11 , pp. 2263-2277
    • Nikitas, G.1    Deschamps, C.2    Disson, O.3    Niault, T.4    Cossart, P.5    Lecuit, M.6
  • 30
    • 0017579106 scopus 로고
    • Oral toxicities of Clostridium botulinum toxins in response to molecular size
    • Ohishi, I., Sugii, S., and Sakaguchi, G. (1977) Oral toxicities of Clostridium botulinum toxins in response to molecular size. Infect Immun 16: 107-109.
    • (1977) Infect Immun , vol.16 , pp. 107-109
    • Ohishi, I.1    Sugii, S.2    Sakaguchi, G.3
  • 31
    • 33645777012 scopus 로고    scopus 로고
    • Listeria monocytogenes invades the epithelial junctions at sites of cell extrusion
    • Pentecost, M., Otto, G., Theriot, J.A., and Amieva, M.R. (2006) Listeria monocytogenes invades the epithelial junctions at sites of cell extrusion. PLoS Pathog 2: e3.
    • (2006) PLoS Pathog , vol.2
    • Pentecost, M.1    Otto, G.2    Theriot, J.A.3    Amieva, M.R.4
  • 32
    • 77954040534 scopus 로고    scopus 로고
    • Listeria monocytogenes invades the epithelial junctions at sites of cell extrusion
    • Pentecost, M., Kumaran, J., Ghosh, P., and Amieva, M.R. (2010) Listeria monocytogenes invades the epithelial junctions at sites of cell extrusion. PLoS Pathog 6: e1000900.
    • (2010) PLoS Pathog , vol.6
    • Pentecost, M.1    Kumaran, J.2    Ghosh, P.3    Amieva, M.R.4
  • 33
    • 0020286209 scopus 로고
    • Clostridium botulinum toxins
    • Sakaguchi, G. (1982) Clostridium botulinum toxins. Pharmacol Ther 19: 165-194.
    • (1982) Pharmacol Ther , vol.19 , pp. 165-194
    • Sakaguchi, G.1
  • 34
    • 27544478181 scopus 로고    scopus 로고
    • Methods for detecting botulinum toxin with applicability to screening foods against biological terrorist attacks
    • Scarlatos, A., Welt, B.A., Cooper, B.Y., Archer, D., DeMarse, T., and Chau, K.V. (2005) Methods for detecting botulinum toxin with applicability to screening foods against biological terrorist attacks. J Food Sci 70: 121-130.
    • (2005) J Food Sci , vol.70 , pp. 121-130
    • Scarlatos, A.1    Welt, B.A.2    Cooper, B.Y.3    Archer, D.4    DeMarse, T.5    Chau, K.V.6
  • 35
    • 0027438184 scopus 로고
    • Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds
    • Schiavo, G., Santucci, A., Dasgupta, B.R., Mehta, P.P., Jontes, J., Benfenati, F., etal. (1993) Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds. FEBS Lett 335: 99-103.
    • (1993) FEBS Lett , vol.335 , pp. 99-103
    • Schiavo, G.1    Santucci, A.2    Dasgupta, B.R.3    Mehta, P.P.4    Jontes, J.5    Benfenati, F.6
  • 36
    • 84877619817 scopus 로고    scopus 로고
    • The life history of a botulinum toxin molecule
    • Simpson, L. (2013) The life history of a botulinum toxin molecule. Toxicon 68: 40-59.
    • (2013) Toxicon , vol.68 , pp. 40-59
    • Simpson, L.1
  • 37
    • 84888194256 scopus 로고    scopus 로고
    • A monoclonal antibody based capture ELISA for botulinum neurotoxin serotype B: toxin detection in food
    • Stanker, L.H., Scotcher, M.C., Cheng, L., Ching, K., McGarvey, J., Hodge, D., and Hnasko, R. (2013) A monoclonal antibody based capture ELISA for botulinum neurotoxin serotype B: toxin detection in food. Toxins 5: 2212-2226.
    • (2013) Toxins , vol.5 , pp. 2212-2226
    • Stanker, L.H.1    Scotcher, M.C.2    Cheng, L.3    Ching, K.4    McGarvey, J.5    Hodge, D.6    Hnasko, R.7
  • 38
    • 77952360192 scopus 로고    scopus 로고
    • Botulinum hemagglutinin disrupts the intercellular epithelial barrier by directly binding E-cadherin
    • Sugawara, Y., Matsumura, T., Takegahara, Y., Jin, Y., Tsukasaki, Y., Takeichi, M., and Fujinaga, Y. (2010) Botulinum hemagglutinin disrupts the intercellular epithelial barrier by directly binding E-cadherin. J Cell Biol 189: 691-700.
    • (2010) J Cell Biol , vol.189 , pp. 691-700
    • Sugawara, Y.1    Matsumura, T.2    Takegahara, Y.3    Jin, Y.4    Tsukasaki, Y.5    Takeichi, M.6    Fujinaga, Y.7
  • 39
    • 0017744686 scopus 로고
    • Correlation between oral toxicity and in vitro stability of Clostridium botulinum type A and B toxins of different molecular sizes
    • Sugii, S., Ohishi, I., and Sakaguchi, G. (1977) Correlation between oral toxicity and in vitro stability of Clostridium botulinum type A and B toxins of different molecular sizes. Infect Immun 16: 910-914.
    • (1977) Infect Immun , vol.16 , pp. 910-914
    • Sugii, S.1    Ohishi, I.2    Sakaguchi, G.3
  • 40
    • 84894087114 scopus 로고    scopus 로고
    • Botulinum neurotoxin A complex recognizes host carbohydrates through its hemagglutinin component
    • Yao, G., Lee, K., Gu, S., Lam, K.H., and Jin, R. (2014) Botulinum neurotoxin A complex recognizes host carbohydrates through its hemagglutinin component. Toxins 6: 624-635.
    • (2014) Toxins , vol.6 , pp. 624-635
    • Yao, G.1    Lee, K.2    Gu, S.3    Lam, K.H.4    Jin, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.