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Volumn 26, Issue 31, 2008, Pages 3835-3841

Residual enzymatic activity of the tetanus toxin light chain present in tetanus toxoid batches used for vaccine production

Author keywords

Residual proteolytic activity; Synaptobrevin; Tetanus toxoid

Indexed keywords

FORMALDEHYDE; NEUROTOXIN; PROTEINASE; SYNAPTOBREVIN; TETANUS ANTIBODY; TETANUS TOXIN; TETANUS TOXOID;

EID: 46149104356     PISSN: 0264410X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vaccine.2008.05.014     Document Type: Article
Times cited : (15)

References (40)
  • 1
    • 0027097028 scopus 로고
    • Tetanus toxin action: inhibition of neurotransmitter release linked to synaptobrevin proteolysis
    • Link E., Edelmann L., Chou J.H., Binz T., Yamasaki S., Eisel U., et al. Tetanus toxin action: inhibition of neurotransmitter release linked to synaptobrevin proteolysis. Biochem Biophys Res Commun 189 2 (1992) 1017-1023
    • (1992) Biochem Biophys Res Commun , vol.189 , Issue.2 , pp. 1017-1023
    • Link, E.1    Edelmann, L.2    Chou, J.H.3    Binz, T.4    Yamasaki, S.5    Eisel, U.6
  • 2
    • 0026497466 scopus 로고
    • Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
    • Schiavo G., Benfenati F., Poulain B., Rossetto O., Polverino de Laureto P., DasGupta B.R., et al. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 359 6398 (1992) 832-835
    • (1992) Nature , vol.359 , Issue.6398 , pp. 832-835
    • Schiavo, G.1    Benfenati, F.2    Poulain, B.3    Rossetto, O.4    Polverino de Laureto, P.5    DasGupta, B.R.6
  • 3
    • 0026673922 scopus 로고
    • Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc
    • Schiavo G., Poulain B., Rossetto O., Benfenati F., Tauc L., and Montecucco C. Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc. EMBO J 11 10 (1992) 3577-3583
    • (1992) EMBO J , vol.11 , Issue.10 , pp. 3577-3583
    • Schiavo, G.1    Poulain, B.2    Rossetto, O.3    Benfenati, F.4    Tauc, L.5    Montecucco, C.6
  • 4
    • 0020073392 scopus 로고
    • Bacterial toxins: a table of lethal amounts
    • Gill D.M. Bacterial toxins: a table of lethal amounts. Microbiol Rev 46 1 (1982) 86-94
    • (1982) Microbiol Rev , vol.46 , Issue.1 , pp. 86-94
    • Gill, D.M.1
  • 6
    • 46149086427 scopus 로고    scopus 로고
    • World Health Organization (WHO). WHO vaccine-preventable diseases: monitoring system, 2006 global summary. WHO document no. WHO/IVB/2006. Geneva, WHO; 2006.
    • World Health Organization (WHO). WHO vaccine-preventable diseases: monitoring system, 2006 global summary. WHO document no. WHO/IVB/2006. Geneva, WHO; 2006.
  • 7
    • 0000979175 scopus 로고
    • Diphtheria toxoid as an immunising agent
    • Glenny A.T., and Hopkins B.E. Diphtheria toxoid as an immunising agent. Brit J Exp Pathol 4 (1923) 283-288
    • (1923) Brit J Exp Pathol , vol.4 , pp. 283-288
    • Glenny, A.T.1    Hopkins, B.E.2
  • 8
    • 0002678757 scopus 로고
    • Sur la toxine et sur l'anatoxine diphthériques
    • Ramon G. Sur la toxine et sur l'anatoxine diphthériques. Ann Inst Pasteur 38 (1924) 1-10
    • (1924) Ann Inst Pasteur , vol.38 , pp. 1-10
    • Ramon, G.1
  • 9
    • 0030330456 scopus 로고    scopus 로고
    • Reasons for instability of bacterial vaccines
    • Corbel M.J. Reasons for instability of bacterial vaccines. Dev Biol Stand 87 (1996) 113-124
    • (1996) Dev Biol Stand , vol.87 , pp. 113-124
    • Corbel, M.J.1
  • 10
    • 36048960030 scopus 로고    scopus 로고
    • Toxin-based vaccines (diphtheria, tetanus, pertussis)
    • Rappuoli R., and Pizza M. Toxin-based vaccines (diphtheria, tetanus, pertussis). Handbook Exp Pharmacol 133 (1999) 201-224
    • (1999) Handbook Exp Pharmacol , vol.133 , pp. 201-224
    • Rappuoli, R.1    Pizza, M.2
  • 11
    • 0038064377 scopus 로고    scopus 로고
    • Novel configurations of high molecular weight species of the pertussis toxin vaccine component
    • Fowler S., Byron O., Jumel K., Xing D., Corbel M.J., and Bolgiano B. Novel configurations of high molecular weight species of the pertussis toxin vaccine component. Vaccine 21 19-20 (2003) 2678-2688
    • (2003) Vaccine , vol.21 , Issue.19-20 , pp. 2678-2688
    • Fowler, S.1    Byron, O.2    Jumel, K.3    Xing, D.4    Corbel, M.J.5    Bolgiano, B.6
  • 12
    • 0034572014 scopus 로고    scopus 로고
    • Monitoring of diphtheria, pertussis and tetanus toxoids by circular dichroism, fluorescence spectroscopy and size-exclusion chromatography
    • Bolgiano B., Fowler S., Turner K., Sesardic D., Xing D.K.L., Crane D.T., et al. Monitoring of diphtheria, pertussis and tetanus toxoids by circular dichroism, fluorescence spectroscopy and size-exclusion chromatography. Dev Biol (Basel) 103 (2000) 51-59
    • (2000) Dev Biol (Basel) , vol.103 , pp. 51-59
    • Bolgiano, B.1    Fowler, S.2    Turner, K.3    Sesardic, D.4    Xing, D.K.L.5    Crane, D.T.6
  • 13
    • 2142645898 scopus 로고    scopus 로고
    • Modeling formalin fixation and antigen retrieval with bovine pancreatic ribonuclease A: I-structural and functional alterations
    • Rait V.K., O'Leary T.J., and Mason J.T. Modeling formalin fixation and antigen retrieval with bovine pancreatic ribonuclease A: I-structural and functional alterations. Lab Invest 84 3 (2004) 292-299
    • (2004) Lab Invest , vol.84 , Issue.3 , pp. 292-299
    • Rait, V.K.1    O'Leary, T.J.2    Mason, J.T.3
  • 14
    • 0026085951 scopus 로고
    • Effects of formaldehyde fixation on protein secondary structure: a calorimetric and infrared spectroscopic investigation
    • Mason J.T., and O'Leary T.J. Effects of formaldehyde fixation on protein secondary structure: a calorimetric and infrared spectroscopic investigation. J Histochem Cytochem 39 2 (1991) 225-229
    • (1991) J Histochem Cytochem , vol.39 , Issue.2 , pp. 225-229
    • Mason, J.T.1    O'Leary, T.J.2
  • 15
    • 0030030017 scopus 로고    scopus 로고
    • Comparison of the conformation, hydrophobicity, and model membrane interactions of diphtheria toxin to those of formaldehyde-treated toxin (diphtheria toxoid): formaldehyde stabilization of the native conformation inhibits changes that allow membrane insertion
    • Paliwal R., and London E. Comparison of the conformation, hydrophobicity, and model membrane interactions of diphtheria toxin to those of formaldehyde-treated toxin (diphtheria toxoid): formaldehyde stabilization of the native conformation inhibits changes that allow membrane insertion. Biochemistry 35 7 (1996) 2374-2379
    • (1996) Biochemistry , vol.35 , Issue.7 , pp. 2374-2379
    • Paliwal, R.1    London, E.2
  • 16
    • 0037159618 scopus 로고    scopus 로고
    • Detection of residual pertussis toxin in vaccines using a modified ribosylation assay
    • Yuen C.-T., Canthaboo C., Menzies J.A., Cyr T., Whitehouse L.W., Jones C., et al. Detection of residual pertussis toxin in vaccines using a modified ribosylation assay. Vaccine 21 1-2 (2002) 44-52
    • (2002) Vaccine , vol.21 , Issue.1-2 , pp. 44-52
    • Yuen, C.-T.1    Canthaboo, C.2    Menzies, J.A.3    Cyr, T.4    Whitehouse, L.W.5    Jones, C.6
  • 17
    • 34047169904 scopus 로고    scopus 로고
    • ADP-ribosylation activity in pertussis vaccines and its relationship to the in vivo histamine-sensitisation test
    • Gomez S.R., Yuen C.-T., Asokanathan C., Douglas-Bardsley A., Corbel M.J., Coote J.G., et al. ADP-ribosylation activity in pertussis vaccines and its relationship to the in vivo histamine-sensitisation test. Vaccine 25 17 (2007) 3311-3318
    • (2007) Vaccine , vol.25 , Issue.17 , pp. 3311-3318
    • Gomez, S.R.1    Yuen, C.-T.2    Asokanathan, C.3    Douglas-Bardsley, A.4    Corbel, M.J.5    Coote, J.G.6
  • 19
    • 36049037645 scopus 로고    scopus 로고
    • An in vitro assay for detection of tetanus neurotoxin activity: using antibodies for recognizing the proteolytically generated cleavage product
    • Kegel B., Behrensdorf-Nicol H.A., Bonifas U., Silberbach K., Klimek J., Krämer B., et al. An in vitro assay for detection of tetanus neurotoxin activity: using antibodies for recognizing the proteolytically generated cleavage product. Toxicol In Vitro 21 8 (2007) 1641-1649
    • (2007) Toxicol In Vitro , vol.21 , Issue.8 , pp. 1641-1649
    • Kegel, B.1    Behrensdorf-Nicol, H.A.2    Bonifas, U.3    Silberbach, K.4    Klimek, J.5    Krämer, B.6
  • 20
    • 46149093544 scopus 로고    scopus 로고
    • Tetanus vaccine (adsorbed), monograph 0452. In: European Pharmacopoeia, 6th ed. Strasbourg, France: Council of Europe; 2008.
    • Tetanus vaccine (adsorbed), monograph 0452. In: European Pharmacopoeia, 6th ed. Strasbourg, France: Council of Europe; 2008.
  • 21
    • 46149110862 scopus 로고    scopus 로고
    • Tetanus vaccine for veterinary use, monograph 01/2008:0697. In: European Pharmacopoeia, 6th ed. Strasbourg, France: Council of Europe; 2008.
    • Tetanus vaccine for veterinary use, monograph 01/2008:0697. In: European Pharmacopoeia, 6th ed. Strasbourg, France: Council of Europe; 2008.
  • 22
    • 0028176426 scopus 로고
    • 2+-binding domain of clostridial neurotoxins restore exocytosis in chromaffin cells treated with tetanus or botulinum A neurotoxin
    • 2+-binding domain of clostridial neurotoxins restore exocytosis in chromaffin cells treated with tetanus or botulinum A neurotoxin. J Biol Chem 269 11 (1994) 8122-8127
    • (1994) J Biol Chem , vol.269 , Issue.11 , pp. 8122-8127
    • Bartels, F.1    Bergel, H.2    Bigalke, H.3    Frevert, J.4    Halpern, J.5    Middlebrook, J.6
  • 23
    • 0038743050 scopus 로고    scopus 로고
    • VAMP/synaptobrevin cleavage by tetanus and botulinum neurotoxins is strongly enhanced by acidic liposomes
    • Caccin P., Rossetto O., Rigoni M., Johnson E., Schiavo G., and Montecucco C. VAMP/synaptobrevin cleavage by tetanus and botulinum neurotoxins is strongly enhanced by acidic liposomes. FEBS Lett 542 1-3 (2003) 132-136
    • (2003) FEBS Lett , vol.542 , Issue.1-3 , pp. 132-136
    • Caccin, P.1    Rossetto, O.2    Rigoni, M.3    Johnson, E.4    Schiavo, G.5    Montecucco, C.6
  • 24
    • 34548574820 scopus 로고    scopus 로고
    • Quality control of routine, experimental and real-time aged diphtheria toxoids by in vitro analytical techniques
    • Metz B., Jiskoot W., Mekkes D., Kingma R., Hennink W.E., Crommelin D.J.A., et al. Quality control of routine, experimental and real-time aged diphtheria toxoids by in vitro analytical techniques. Vaccine 25 39-40 (2007) 6863-6871
    • (2007) Vaccine , vol.25 , Issue.39-40 , pp. 6863-6871
    • Metz, B.1    Jiskoot, W.2    Mekkes, D.3    Kingma, R.4    Hennink, W.E.5    Crommelin, D.J.A.6
  • 25
    • 33846885899 scopus 로고    scopus 로고
    • Investigation of the detoxification mechanism of formaldehyde-treated tetanus toxin
    • Thaysen-Andersen M., Jorgensen S.B., Wilhelmsen E.S., Petersen J.W., and Hojrup P. Investigation of the detoxification mechanism of formaldehyde-treated tetanus toxin. Vaccine 25 12 (2007) 2213-2227
    • (2007) Vaccine , vol.25 , Issue.12 , pp. 2213-2227
    • Thaysen-Andersen, M.1    Jorgensen, S.B.2    Wilhelmsen, E.S.3    Petersen, J.W.4    Hojrup, P.5
  • 26
    • 0038306894 scopus 로고    scopus 로고
    • Application of an in vitro endopeptidase assay for detection of residual toxin activity in tetanus toxoids
    • Leung T., Corran P.H., Gee C., Ekong T.A.N., and Sesardic D. Application of an in vitro endopeptidase assay for detection of residual toxin activity in tetanus toxoids. Dev Biol (Basel) 111 (2002) 327-332
    • (2002) Dev Biol (Basel) , vol.111 , pp. 327-332
    • Leung, T.1    Corran, P.H.2    Gee, C.3    Ekong, T.A.N.4    Sesardic, D.5
  • 27
    • 0019500662 scopus 로고
    • Effect of formalin toxoiding on Pseudomonas aeruginosa toxin A: biological, chemical, and immunochemical studies
    • Cryz Jr. S.J., Friedman R.L., Pavlovskis O.R., and Iglewski B.H. Effect of formalin toxoiding on Pseudomonas aeruginosa toxin A: biological, chemical, and immunochemical studies. Infect Immun 32 2 (1981) 759-768
    • (1981) Infect Immun , vol.32 , Issue.2 , pp. 759-768
    • Cryz Jr., S.J.1    Friedman, R.L.2    Pavlovskis, O.R.3    Iglewski, B.H.4
  • 28
    • 0026344180 scopus 로고
    • An enzymatic mutant of Shiga-like toxin II variant is a vaccine candidate for edema disease of swine
    • Gordon V.M., Whipp S.C., Moon H.W., O'Brien A.D., and Samuel J.E. An enzymatic mutant of Shiga-like toxin II variant is a vaccine candidate for edema disease of swine. Infect Immun 60 2 (1992) 485-490
    • (1992) Infect Immun , vol.60 , Issue.2 , pp. 485-490
    • Gordon, V.M.1    Whipp, S.C.2    Moon, H.W.3    O'Brien, A.D.4    Samuel, J.E.5
  • 29
    • 0028889780 scopus 로고
    • Genetic detoxification of bacterial toxins: a new approach to vaccine development
    • Rappuoli R., Douce G., Dougan G., and Pizza M. Genetic detoxification of bacterial toxins: a new approach to vaccine development. Int Arch Allergy Immunol 108 4 (1995) 327-333
    • (1995) Int Arch Allergy Immunol , vol.108 , Issue.4 , pp. 327-333
    • Rappuoli, R.1    Douce, G.2    Dougan, G.3    Pizza, M.4
  • 30
    • 0025648954 scopus 로고
    • An intact interchain disulfide bond is required for the neurotoxicity of tetanus toxin
    • Schiavo G., Papini E., Genna G., and Montecucco C. An intact interchain disulfide bond is required for the neurotoxicity of tetanus toxin. Infect Immun 58 12 (1990) 4136-4141
    • (1990) Infect Immun , vol.58 , Issue.12 , pp. 4136-4141
    • Schiavo, G.1    Papini, E.2    Genna, G.3    Montecucco, C.4
  • 31
    • 0009470217 scopus 로고    scopus 로고
    • In vitro approaches for estimating activity of tetanus toxin as an alternative assay for specific toxicity
    • Balls M., van Zeller A.-M., and Halder M.E. (Eds), Elsevier, Amsterdam
    • Sesardic D., Corran P.H., Gee C., and Ekong T.A.N. In vitro approaches for estimating activity of tetanus toxin as an alternative assay for specific toxicity. In: Balls M., van Zeller A.-M., and Halder M.E. (Eds). Progress in the reduction, refinement and replacement of animal experimentation (2000), Elsevier, Amsterdam 969-974
    • (2000) Progress in the reduction, refinement and replacement of animal experimentation , pp. 969-974
    • Sesardic, D.1    Corran, P.H.2    Gee, C.3    Ekong, T.A.N.4
  • 32
    • 0030782182 scopus 로고    scopus 로고
    • Recombinant SNAP-25 is an effective substrate for Clostridium botulinum type A toxin endopeptidase activity in vitro
    • Ekong T.A.N., Feavers E.M., and Sesardic D. Recombinant SNAP-25 is an effective substrate for Clostridium botulinum type A toxin endopeptidase activity in vitro. Microbiology 143 (1997) 3337-3347
    • (1997) Microbiology , vol.143 , pp. 3337-3347
    • Ekong, T.A.N.1    Feavers, E.M.2    Sesardic, D.3
  • 33
    • 36849053345 scopus 로고    scopus 로고
    • Development of improved SNAP25 endopeptidase immuno-assays for botulinum type A and E toxins
    • Jones R.G., Ochiai M., Liu Y., Ekong T., and Sesardic D. Development of improved SNAP25 endopeptidase immuno-assays for botulinum type A and E toxins. J Immunol Methods 329 1-2 (2008) 92-101
    • (2008) J Immunol Methods , vol.329 , Issue.1-2 , pp. 92-101
    • Jones, R.G.1    Ochiai, M.2    Liu, Y.3    Ekong, T.4    Sesardic, D.5
  • 34
    • 0018906584 scopus 로고
    • Kinetic studies on the interaction between botulinum toxin type A and the cholinergic neuromuscular junction
    • Simpson L.L. Kinetic studies on the interaction between botulinum toxin type A and the cholinergic neuromuscular junction. J Pharmacol Exp Ther 212 1 (1980) 16-21
    • (1980) J Pharmacol Exp Ther , vol.212 , Issue.1 , pp. 16-21
    • Simpson, L.L.1
  • 35
    • 0028964514 scopus 로고
    • The median paralysis unit: a more pharmacologically relevant unit of biologic activity for botulinum toxin
    • Pearce L.B., Borodic G.E., Johnson E.A., First E.R., and MacCallum R. The median paralysis unit: a more pharmacologically relevant unit of biologic activity for botulinum toxin. Toxicon 33 2 (1995) 217-227
    • (1995) Toxicon , vol.33 , Issue.2 , pp. 217-227
    • Pearce, L.B.1    Borodic, G.E.2    Johnson, E.A.3    First, E.R.4    MacCallum, R.5
  • 36
    • 46149090910 scopus 로고    scopus 로고
    • Botulinum toxin type A for injection, monograph 2113. In: European Pharmacopoeia, 6th ed. Strasbourg, France: Council of Europe; 2008.
    • Botulinum toxin type A for injection, monograph 2113. In: European Pharmacopoeia, 6th ed. Strasbourg, France: Council of Europe; 2008.
  • 37
    • 1042291316 scopus 로고    scopus 로고
    • Toxicity and potency evaluation of pertussis vaccines
    • Corbel M.J., and Xing D.K.L. Toxicity and potency evaluation of pertussis vaccines. Expert Rev Vac 3 1 (2004) 89-101
    • (2004) Expert Rev Vac , vol.3 , Issue.1 , pp. 89-101
    • Corbel, M.J.1    Xing, D.K.L.2
  • 38
    • 33747883626 scopus 로고    scopus 로고
    • Development of a carbohydrate binding assay for the B-oligomer of pertussis toxin and toxoid
    • Gomez S.R., Xing D.K.L., Corbel M.J., Coote J., Parton R., and Yuen C.-T. Development of a carbohydrate binding assay for the B-oligomer of pertussis toxin and toxoid. Anal Biochem 356 2 (2006) 244-253
    • (2006) Anal Biochem , vol.356 , Issue.2 , pp. 244-253
    • Gomez, S.R.1    Xing, D.K.L.2    Corbel, M.J.3    Coote, J.4    Parton, R.5    Yuen, C.-T.6
  • 39
    • 0022412787 scopus 로고
    • Interaction of solid-phase gangliosides with tetanus toxin and toxoid
    • Habermann E., and Tayot J.L. Interaction of solid-phase gangliosides with tetanus toxin and toxoid. Toxicon 23 6 (1985) 913-920
    • (1985) Toxicon , vol.23 , Issue.6 , pp. 913-920
    • Habermann, E.1    Tayot, J.L.2
  • 40
    • 33947153768 scopus 로고    scopus 로고
    • The rise in pertussis cases urges replacement of chemically-inactivated with genetically-inactivated toxoid for DTP
    • Robbins J.B., Schneerson R., Keith J.M., Shiloach J., Miller M., and Trollors B. The rise in pertussis cases urges replacement of chemically-inactivated with genetically-inactivated toxoid for DTP. Vaccine 25 15 (2007) 2811-2816
    • (2007) Vaccine , vol.25 , Issue.15 , pp. 2811-2816
    • Robbins, J.B.1    Schneerson, R.2    Keith, J.M.3    Shiloach, J.4    Miller, M.5    Trollors, B.6


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