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Volumn 28, Issue 1, 2010, Pages 85-93

Human monoclonal ScFv that inhibits cellular entry and metalloprotease activity of tetanus neurotoxin

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; METALLOPROTEINASE; NEUROTOXIN; RECOMBINANT PROTEIN; RETINOIC ACID; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; SYNAPTOBREVIN; TETANUS TOXIN; TETANUS TOXOID; UNCLASSIFIED DRUG; ZINC METALLOPROTEINASE;

EID: 77954561384     PISSN: 0125877X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (25)
  • 2
    • 19344372277 scopus 로고    scopus 로고
    • Structural analysis of the catalytic domain of tetanus neurotoxin
    • Rao KN, Kumaran D, Binz T, Swanminathan S. Structural analysis of the catalytic domain of tetanus neurotoxin. Toxicon 2005; 45: 929-39.
    • (2005) Toxicon , vol.45 , pp. 929-939
    • Rao, K.N.1    Kumaran, D.2    Binz, T.3    Swanminathan, S.4
  • 3
    • 0029115155 scopus 로고
    • Neurospecific binding, internalization, and retrograde axonal transport
    • Halpern JL, Neale EA. Neurospecific binding, internalization, and retrograde axonal transport. Curr Top Microbiol Immunol 1995; 195: 221-41.
    • (1995) Curr Top Microbiol Immunol , vol.195 , pp. 221-241
    • Halpern, J.L.1    Neale, E.A.2
  • 4
    • 0030785294 scopus 로고    scopus 로고
    • Identification of a ganglioside recognition domain of tetanus toxin using a novel ganglioside photoaffinity ligand
    • Shapiro ER, Specht DC, Collins EB, et al. Identification of a ganglioside recognition domain of tetanus toxin using a novel ganglioside photoaffinity ligand. J Biol Chem 1997; 272: 30380-6.
    • (1997) J Biol Chem , vol.272 , pp. 30380-30386
    • Shapiro, E.R.1    Specht, D.C.2    Collins, E.B.3
  • 5
    • 0026497466 scopus 로고
    • Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
    • Schiavo G, Benfenati F, Poulain B, et al. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 1992; 359: 832-5.
    • (1992) Nature , vol.359 , pp. 832-835
    • Schiavo, G.1    Benfenati, F.2    Poulain, B.3
  • 6
    • 51049104533 scopus 로고    scopus 로고
    • Substrate recognition mechanism of VAMP/synaptobrevincleaving clostridial neurotoxins
    • Sikorra S, Henke T, Galli T, Binz T. Substrate recognition mechanism of VAMP/synaptobrevincleaving clostridial neurotoxins. J Biol Chem 2008; 283: 21145-52.
    • (2008) J Biol Chem , vol.283 , pp. 21145-21152
    • Sikorra, S.1    Henke, T.2    Galli, T.3    Binz, T.4
  • 7
    • 0017353945 scopus 로고
    • Structure of tetanus toxin: I. Break-down of the molecule and discrimination between polypeptide fragments
    • Helting BT, Zwisler O. Structure of tetanus toxin: I. Break-down of the molecule and discrimination between polypeptide fragments. J Biol Chem 1977; 252: 187-193.
    • (1977) J Biol Chem , vol.252 , pp. 187-193
    • Helting, B.T.1    Zwisler, O.2
  • 8
    • 0018775424 scopus 로고
    • Tetanus toxin
    • Bernard B. Tetanus toxin. Microbiol Rev 1979; 43: 224-40.
    • (1979) Microbiol Rev , vol.43 , pp. 224-240
    • Bernard, B.1
  • 9
    • 0021880433 scopus 로고
    • Antibodies against the light chain of tetanus toxin in human sera
    • Clara SL, William HH, Carolyn HM. Antibodies against the light chain of tetanus toxin in human sera. Infect Immun 1985; 49: 111-5.
    • (1985) Infect Immun , vol.49 , pp. 111-115
    • Clara, S.L.1    William, H.H.2    Carolyn, H.M.3
  • 10
    • 67349223719 scopus 로고    scopus 로고
    • Tetanus Toxoid
    • In: 5th edition, Plotkin SA, Orenstein WA, eds. Philadelphia, PA, WB Saunders
    • Wassilak SGF, Orenstein WA, Sutter RW. Tetanus Toxoid. In: Vaccines, 5th edition, Plotkin SA, Orenstein WA, eds. Philadelphia, PA, WB Saunders, 2008, pp. 805-39.
    • (2008) Vaccines , pp. 805-839
    • Wassilak, S.G.F.1    Orenstein, W.A.2    Sutter, R.W.3
  • 11
    • 0021151281 scopus 로고
    • Neonatal tetanus in the world today
    • Stanfield JP, Galazka A. Neonatal tetanus in the world today. Bull WHO 1984; 62: 647-69.
    • (1984) Bull WHO , vol.62 , pp. 647-669
    • Stanfield, J.P.1    Galazka, A.2
  • 12
    • 0017293853 scopus 로고
    • Changes in antitetanus antibodies under serotoxoid therapy. Study in 50 patients with tetanus
    • Goulon M, Girard O, Grosbuis S, Desormeau JP, Capponi MF. Changes in antitetanus antibodies under serotoxoid therapy. Study in 50 patients with tetanus. Nouv Presse Med 1976; 5: 847-50.
    • (1976) Nouv Presse Med , vol.5 , pp. 847-850
    • Goulon, M.1    Girard, O.2    Grosbuis, S.3    Desormeau, J.P.4    Capponi, M.F.5
  • 13
    • 77954553318 scopus 로고
    • The quantitative changes in the protein in the blood plasma of horse in the course of immunization
    • Gibson RB, Banzhaf EJ. The quantitative changes in the protein in the blood plasma of horse in the course of immunization. J Exp Med 1910; 12: 411-34.
    • (1910) J Exp Med , vol.12 , pp. 411-434
    • Gibson, R.B.1    Banzhaf, E.J.2
  • 14
    • 60149088262 scopus 로고    scopus 로고
    • Human monoclonal ScFv neutralize lethal Thai cobra, Naja kaouthia, neurotoxin
    • Kulkeaw K, Sakolvaree Y, Srimanote P, et al. Human monoclonal ScFv neutralize lethal Thai cobra, Naja kaouthia, neurotoxin. J Proteomics 2009; 72: 270-82.
    • (2009) J Proteomics , vol.72 , pp. 270-282
    • Kulkeaw, K.1    Sakolvaree, Y.2    Srimanote, P.3
  • 15
    • 67349114873 scopus 로고    scopus 로고
    • Human single chain monoclonal antibody that recognizes matrix protein of heterologous influenza A virus subtypes
    • Poungpair O, Chaicumpa W, Kulkeaw K, et al. Human single chain monoclonal antibody that recognizes matrix protein of heterologous influenza A virus subtypes. J Virol Methods 2009; 159: 105-11.
    • (2009) J Virol Methods , vol.159 , pp. 105-111
    • Poungpair, O.1    Chaicumpa, W.2    Kulkeaw, K.3
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of proteindye-binding
    • Bradford MM. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of proteindye-binding. Anal Biochem 1976; 72: 248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmili UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmili, U.K.1
  • 18
    • 45349105001 scopus 로고    scopus 로고
    • Human monoclonal single chain antibodies (huScFv) that bind to the polymerase proteins of influenza A virus
    • Thathaisong U, Maneewatch S, Kulkeaw K, et al. Human monoclonal single chain antibodies (huScFv) that bind to the polymerase proteins of influenza A virus. Asian Pac J Allergy Immunol. 2008; 26: 23-35.
    • (2008) Asian Pac J Allergy Immunol , vol.26 , pp. 23-35
    • Thathaisong, U.1    Maneewatch, S.2    Kulkeaw, K.3
  • 19
    • 0030883923 scopus 로고    scopus 로고
    • Characterization of the cholinergic differentiation of the human neuroblastoma cell line LA-N-5 after treatment with retinoic acid
    • Hill PD, Robertson AK. Characterization of the cholinergic differentiation of the human neuroblastoma cell line LA-N-5 after treatment with retinoic acid. Dev Brain Res 1997; 102: 53-67.
    • (1997) Dev Brain Res , vol.102 , pp. 53-67
    • Hill, P.D.1    Robertson, A.K.2
  • 20
    • 0028952820 scopus 로고
    • Tetanus-forgotten but not gone
    • Sanford PJ. Tetanus-forgotten but not gone. N Engl J Med 1995; 332: 812-3.
    • (1995) N Engl J Med , vol.332 , pp. 812-813
    • Sanford, P.J.1
  • 21
    • 0020963039 scopus 로고
    • Studies on the antibody composition and neutralizing activity of tetanus antitoxin sera from various species of animals in relation to the antigenic substructure of the tetanus toxin molecule
    • Matsuda M, Makinaga G, Hirai T. Studies on the antibody composition and neutralizing activity of tetanus antitoxin sera from various species of animals in relation to the antigenic substructure of the tetanus toxin molecule. Biken J 1983; 26: 133-43.
    • (1983) Biken J , vol.26 , pp. 133-143
    • Matsuda, M.1    Makinaga, G.2    Hirai, T.3
  • 22
    • 0026599858 scopus 로고
    • Reductive cleavage of tetanus toxin and botulinum neurotoxin A by the thioredoxin system from brain
    • Kistner A, Habermann E. Reductive cleavage of tetanus toxin and botulinum neurotoxin A by the thioredoxin system from brain. Naunyn Schmiedebergs Arch Pharmacol 1992; 345: 227-34.
    • (1992) Naunyn Schmiedebergs Arch Pharmacol , vol.345 , pp. 227-234
    • Kistner, A.1    Habermann, E.2
  • 23
    • 35948991091 scopus 로고    scopus 로고
    • Single domain antibodies from llama effectively and specifically block T cell ecto-ADP-ribosyltransferase ART2.2 in vivo
    • Koch-Nolte F, Reyelt J, Schössow B, et al. Single domain antibodies from llama effectively and specifically block T cell ecto-ADP-ribosyltransferase ART2.2 in vivo. FASEB 2007; 21: 3490-8.
    • (2007) FASEB , vol.21 , pp. 3490-3498
    • Koch-Nolte, F.1    Reyelt, J.2    Schössow, B.3
  • 24
    • 67149113906 scopus 로고    scopus 로고
    • Human single-chain antibodies that neutralize homologous and heterologous strains and clades of influenza A virus subtype H5N1
    • Maneewatch S, Thanongsaksrikul J, Songserm T, et al. Human single-chain antibodies that neutralize homologous and heterologous strains and clades of influenza A virus subtype H5N1. Antivir Ther 2009; 14: 221-30.
    • (2009) Antivir Ther , vol.14 , pp. 221-230
    • Maneewatch, S.1    Thanongsaksrikul, J.2    Songserm, T.3
  • 25
    • 77951215115 scopus 로고    scopus 로고
    • A VHH that neutralizes the zinc metalloproteinase activity of botulinum neurotoxin type A
    • Thanongsaksrikul J, Srimanote P, Maneewatch S, et al. A VHH that neutralizes the zinc metalloproteinase activity of botulinum neurotoxin type A. J Biol Chem 2010; 285: 9657-66.
    • (2010) J Biol Chem , vol.285 , pp. 9657-9666
    • Thanongsaksrikul, J.1    Srimanote, P.2    Maneewatch, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.