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Volumn 288, Issue 49, 2013, Pages 35617-35625

Crystal structure of clostridium botulinum whole hemagglutinin reveals a huge triskelion-shaped molecular complex

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

EID: 84890278174     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.521179     Document Type: Article
Times cited : (52)

References (42)
  • 1
    • 67649292434 scopus 로고    scopus 로고
    • How do the botulinum neurotoxins block neurotransmitter release: From botulism to the molecular mechanism of action
    • Poulain, B., Popoff, M. R., and Molgo, J. (2008) How do the botulinum neurotoxins block neurotransmitter release: from botulism to the molecular mechanism of action. Botulinum J. 1, 14-87
    • (2008) Botulinum J. , vol.1 , pp. 14-87
    • Poulain, B.1    Popoff, M.R.2    Molgo, J.3
  • 2
    • 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
  • 4
    • 84875806832 scopus 로고    scopus 로고
    • Genetic diversity within Clostridium botulinum serotypes, botulinum neurotoxin gene clusters and toxin subtypes
    • Hill, K. K., and Smith, T. J. (2013) Genetic diversity within Clostridium botulinum serotypes, botulinum neurotoxin gene clusters and toxin subtypes. Curr. Top. Microbiol. Immunol. 364, 1-20
    • (2013) Curr. Top. Microbiol. Immunol. , vol.364 , pp. 1-20
    • Hill, K.K.1    Smith, T.J.2
  • 8
    • 0031435919 scopus 로고    scopus 로고
    • The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin
    • Fujinaga, Y., Inoue, K., Watanabe, S., Yokota, K., Hirai, Y., Nagamachi, E., and Oguma, K. (1997) The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin. Microbiology 143, 3841-3847
    • (1997) Microbiology , vol.143 , pp. 3841-3847
    • Fujinaga, Y.1    Inoue, K.2    Watanabe, S.3    Yokota, K.4    Hirai, Y.5    Nagamachi, E.6    Oguma, K.7
  • 9
    • 0033952269 scopus 로고    scopus 로고
    • Identification and characterization of functional subunits of Clostridium botulinum typeAprogenitor toxin involved in binding to intestinal microvilli and erythrocytes
    • Fujinaga, Y., Inoue, K., Nomura, T., Sasaki, J., Marvaud, J. C., Popoff, M. R., Kozaki, S., and Oguma, K. (2000) Identification and characterization of functional subunits of Clostridium botulinum typeAprogenitor toxin involved in binding to intestinal microvilli and erythrocytes. FEBS Lett. 467, 179-183
    • (2000) FEBS Lett. , vol.467 , pp. 179-183
    • Fujinaga, Y.1    Inoue, K.2    Nomura, T.3    Sasaki, J.4    Marvaud, J.C.5    Popoff, M.R.6    Kozaki, S.7    Oguma, K.8
  • 13
  • 14
    • 33947285071 scopus 로고    scopus 로고
    • Role of nontoxic components of serotype D botulinum toxin complex in permeation through a Caco-2 cell monolayer, a model for intestinal epithelium
    • Niwa, K., Koyama, K., Inoue, S., Suzuki, T., Hasegawa, K., Watanabe, T., Ikeda, T., and Ohyama, T. (2007) Role of nontoxic components of serotype D botulinum toxin complex in permeation through a Caco-2 cell monolayer, a model for intestinal epithelium. FEMS Immunol. Med. Microbiol. 49, 346-352
    • (2007) FEMS Immunol. Med. Microbiol. , vol.49 , pp. 346-352
    • Niwa, K.1    Koyama, K.2    Inoue, S.3    Suzuki, T.4    Hasegawa, K.5    Watanabe, T.6    Ikeda, T.7    Ohyama, T.8
  • 17
    • 77958457608 scopus 로고    scopus 로고
    • Involvement of sialic acid in transport of serotype C1 botulinum toxins through rat intestinal epithelial cells
    • Inui, K., Ito, H., Miyata, K., Matsuo, T., Horiuchi, R., Ikeda, T., Watanabe, T., Ohyama, T., and Niwa, K. (2010) Involvement of sialic acid in transport of serotype C1 botulinum toxins through rat intestinal epithelial cells. J. Vet. Med. Sci. 72, 1251-1255
    • (2010) J. Vet. Med. Sci. , vol.72 , pp. 1251-1255
    • Inui, K.1    Ito, H.2    Miyata, K.3    Matsuo, T.4    Horiuchi, R.5    Ikeda, T.6    Watanabe, T.7    Ohyama, T.8    Niwa, K.9
  • 19
    • 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
  • 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
    • 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
  • 22
    • 78650828434 scopus 로고    scopus 로고
    • The botulinum toxin complex meets E-cadherin on the way to its destination
    • Sugawara, Y., and Fujinaga, Y. (2011) The botulinum toxin complex meets E-cadherin on the way to its destination. Cell Adh. Migr. 5, 34-36
    • (2011) Cell Adh. Migr. , vol.5 , pp. 34-36
    • Sugawara, Y.1    Fujinaga, Y.2
  • 23
  • 24
    • 0025913445 scopus 로고
    • Crystallization and preliminary X-ray diffraction study of the ligand- binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium
    • Jancarik, J., Scott, W. G., Milligan, D. L., Koshland, D. E., Jr., and Kim, S. H. (1991) Crystallization and preliminary X-ray diffraction study of the ligand- binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium. J. Mol. Biol. 221, 31-34
    • (1991) J. Mol. Biol. , vol.221 , pp. 31-34
    • Jancarik, J.1    Scott, W.G.2    Milligan, D.L.3    Koshland Jr., D.E.4    Kim, S.H.5
  • 26
    • 77950798648 scopus 로고    scopus 로고
    • Recent developments in classical density modification
    • Cowtan, K. (2010) Recent developments in classical density modification. Acta Crystallogr. D Biol. Crystallogr. 66, 470-478
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 470-478
    • Cowtan, K.1
  • 27
    • 0347123535 scopus 로고    scopus 로고
    • Structure of the integrin -2-1-binding collagen peptide
    • Emsley, J., Knight, C. G., Farndale, R. W., and Barnes, M. J. (2004) Structure of the integrin -2-1-binding collagen peptide. J. Mol. Biol. 335, 1019-1028
    • (2004) J. Mol. Biol. , vol.335 , pp. 1019-1028
    • Emsley, J.1    Knight, C.G.2    Farndale, R.W.3    Barnes, M.J.4
  • 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
  • 30
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal -hemolysin, a heptameric transmembrane pore
    • Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., and Gouaux, J. E. (1996) Structure of staphylococcal -hemolysin, a heptameric transmembrane pore. Science 274, 1859-1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 31
    • 58149344932 scopus 로고    scopus 로고
    • Crystal structure of the HA3 subcomponent of Clostridium botulinum type C progenitor toxin
    • Nakamura, T., Kotani, M., Tonozuka, T., Ide, A., Oguma, K., and Nishikawa, A. (2009) Crystal structure of the HA3 subcomponent of Clostridium botulinum type C progenitor toxin. J. Mol. Biol. 385, 1193-1206
    • (2009) J. Mol. Biol. , vol.385 , pp. 1193-1206
    • Nakamura, T.1    Kotani, M.2    Tonozuka, T.3    Ide, A.4    Oguma, K.5    Nishikawa, A.6
  • 32
    • 0347513218 scopus 로고    scopus 로고
    • Structural analysis by X-ray crystallography and calorimetry of a haemagglutinin component (HA1) of the progenitor toxin from Clostridium botulinum
    • Inoue, K., Sobhany, M., Transue, T. R., Oguma, K., Pedersen, L. C., and Negishi, M. (2003) Structural analysis by X-ray crystallography and calorimetry of a haemagglutinin component (HA1) of the progenitor toxin from Clostridium botulinum. Microbiology 149, 3361-3370
    • (2003) Microbiology , vol.149 , pp. 3361-3370
    • Inoue, K.1    Sobhany, M.2    Transue, T.R.3    Oguma, K.4    Pedersen, L.C.5    Negishi, M.6
  • 33
    • 38649091349 scopus 로고    scopus 로고
    • Sugar-binding sites of the HA1 subcomponent of Clostridium botulinum type C progenitor toxin
    • Nakamura, T., Tonozuka, T., Ide, A., Yuzawa, T., Oguma, K., and Nishikawa, A. (2008) Sugar-binding sites of the HA1 subcomponent of Clostridium botulinum type C progenitor toxin. J. Mol. Biol. 376, 854-867
    • (2008) J. Mol. Biol. , vol.376 , pp. 854-867
    • Nakamura, T.1    Tonozuka, T.2    Ide, A.3    Yuzawa, T.4    Oguma, K.5    Nishikawa, A.6
  • 34
    • 79959824749 scopus 로고    scopus 로고
    • Molecular diversity of the two sugarbinding sites of the -trefoil lectin HA33/C (HA1) from Clostridium botulinum type C neurotoxin
    • Nakamura, T., Tonozuka, T., Ito, S., Takeda, Y., Sato, R., Matsuo, I., Ito, Y., Oguma, K., and Nishikawa, A. (2011) Molecular diversity of the two sugarbinding sites of the -trefoil lectin HA33/C (HA1) from Clostridium botulinum type C neurotoxin. Arch. Biochem. Biophys. 512, 69-77
    • (2011) Arch. Biochem. Biophys. , vol.512 , pp. 69-77
    • Nakamura, T.1    Tonozuka, T.2    Ito, S.3    Takeda, Y.4    Sato, R.5    Matsuo, I.6    Ito, Y.7    Oguma, K.8    Nishikawa, A.9
  • 35
    • 13444263345 scopus 로고    scopus 로고
    • The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring -trefoil fold in the progenitor toxin complex
    • Arndt, J. W., Gu, J., Jaroszewski, L., Schwarzenbacher, R., Hanson, M. A., Lebeda, F. J., and Stevens, R. C. (2005) The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring -trefoil fold in the progenitor toxin complex. J. Mol. Biol. 346, 1083-1093
    • (2005) J. Mol. Biol. , vol.346 , pp. 1083-1093
    • Arndt, J.W.1    Gu, J.2    Jaroszewski, L.3    Schwarzenbacher, R.4    Hanson, M.A.5    Lebeda, F.J.6    Stevens, R.C.7
  • 36
    • 0033523773 scopus 로고    scopus 로고
    • Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: Evidence for direct involvement of claudins in tight junction barrier
    • Sonoda, N., Furuse, M., Sasaki, H., Yonemura, S., Katahira, J., Horiguchi, Y., and Tsukita, S. (1999) Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: evidence for direct involvement of claudins in tight junction barrier. J. Cell Biol. 147, 195-204
    • (1999) J. Cell Biol. , vol.147 , pp. 195-204
    • Sonoda, N.1    Furuse, M.2    Sasaki, H.3    Yonemura, S.4    Katahira, J.5    Horiguchi, Y.6    Tsukita, S.7
  • 39
    • 0037169538 scopus 로고    scopus 로고
    • In vitro reconstitution of the Clostridium botulinum type D progenitor toxin
    • Kouguchi, H., Watanabe, T., Sagane, Y., Sunagawa, H., and Ohyama, T. (2002) In vitro reconstitution of the Clostridium botulinum type D progenitor toxin. J. Biol. Chem. 277, 2650-2656
    • (2002) J. Biol. Chem. , vol.277 , pp. 2650-2656
    • Kouguchi, H.1    Watanabe, T.2    Sagane, Y.3    Sunagawa, H.4    Ohyama, T.5
  • 40
    • 84864287475 scopus 로고    scopus 로고
    • Carbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharides
    • Yamashita, S., Yoshida, H., Uchiyama, N., Nakakita, Y., Nakakita, S., Tonozuka, T., Oguma, K., Nishikawa, A., and Kamitori, S. (2012) Carbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharides. FEBS Lett. 586, 2404-2410
    • (2012) FEBS Lett. , vol.586 , pp. 2404-2410
    • Yamashita, S.1    Yoshida, H.2    Uchiyama, N.3    Nakakita, Y.4    Nakakita, S.5    Tonozuka, T.6    Oguma, K.7    Nishikawa, A.8    Kamitori, S.9
  • 42
    • 80053329693 scopus 로고    scopus 로고
    • Structure of the food-poisoning Clostridium perfringens enterotoxin reveals similarity to the aerolysin-like pore-forming toxins
    • Briggs, D. C., Naylor, C. E., Smedley, J. G., 3rd, Lukoyanova, N., Robertson, S., Moss, D. S., McClane, B. A., and Basak, A. K. (2011) Structure of the food-poisoning Clostridium perfringens enterotoxin reveals similarity to the aerolysin-like pore-forming toxins. J. Mol. Biol. 413, 138-149
    • (2011) J. Mol. Biol. , vol.413 , pp. 138-149
    • Briggs, D.C.1    Naylor, C.E.2    Smedley Iii., J.G.3    Lukoyanova, N.4    Robertson, S.5    Moss, D.S.6    McClane, B.A.7    Basak, A.K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.