메뉴 건너뛰기




Volumn 152, Issue 7, 2006, Pages 1891-1895

On the enchancement of anti-neurotoxin antibody production by subcomponents HA1 and HA3b of Clostridium botulinum type B 16S toxin-haemagglutinin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM ANTIBODY; BOTULINUM TOXIN A; BOTULINUM TOXIN B; BUFFER; EPITOPE; FORMALDEHYDE; HEMAGGLUTININ; HUMAN SERUM ALBUMIN; MAJOR HISTOCOMPATIBILITY ANTIGEN; SODIUM DIHYDROGEN PHOSPHATE; 16S TOXIN, CLOSTRIDIUM BOTULINUM; BACTERIAL TOXIN; IMMUNOLOGICAL ADJUVANT;

EID: 33746092491     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.28862-0     Document Type: Note
Times cited : (19)

References (38)
  • 1
    • 0042710491 scopus 로고    scopus 로고
    • Immunologic and other properties of therapeutic botulinum toxin serotypes
    • Edited by M. F. Brin, M. Hallett & J. Jankovic. Philadelphia: Lippincott Williams & Wilkins
    • Aoki, K. R. (2002). Immunologic and other properties of therapeutic botulinum toxin serotypes. In Scientific and Therapeutic Aspects of Botulinum Toxin, pp. 103-113. Edited by M. F. Brin, M. Hallett & J. Jankovic. Philadelphia: Lippincott Williams & Wilkins.
    • (2002) Scientific and Therapeutic Aspects of Botulinum Toxin , pp. 103-113
    • Aoki, K.R.1
  • 2
    • 0037369959 scopus 로고    scopus 로고
    • Purification of fully activated Clostridium botulinum serotype B toxin for treatment of patients with dystonia
    • Arimitsu, H., Inoue, K., Sakaguchi, Y., Lee, J., Fujinaga, Y., Watanabe, T., Ohyama, T., Hirst, R. & Oguma, K. (2003). Purification of fully activated Clostridium botulinum serotype B toxin for treatment of patients with dystonia. Infect Immun 71, 1599-1603.
    • (2003) Infect Immun , vol.71 , pp. 1599-1603
    • Arimitsu, H.1    Inoue, K.2    Sakaguchi, Y.3    Lee, J.4    Fujinaga, Y.5    Watanabe, T.6    Ohyama, T.7    Hirst, R.8    Oguma, K.9
  • 3
    • 0002348547 scopus 로고
    • Chemical modification and cleavage of proteins and chemical strategy in immunochemical studies of proteins
    • Edited by M. Z. Atassi. New York: Plenum
    • Atassi, M. Z. (1977). Chemical modification and cleavage of proteins and chemical strategy in immunochemical studies of proteins. In Immunochemistry of Proteins, vol. 1, pp. 1-161. Edited by M. Z. Atassi. New York: Plenum.
    • (1977) Immunochemistry of Proteins , vol.1 , pp. 1-161
    • Atassi, M.Z.1
  • 4
    • 0021764621 scopus 로고
    • Antigenic structures of proteins. Their determination has revealed important aspects of immune recognition and generated strategies for synthetic mimicking of protein binding sites
    • Atassi, M. Z. (1984). Antigenic structures of proteins. Their determination has revealed important aspects of immune recognition and generated strategies for synthetic mimicking of protein binding sites. Eur J Biochem 145, 1-20.
    • (1984) Eur J Biochem , vol.145 , pp. 1-20
    • Atassi, M.Z.1
  • 5
    • 0011713252 scopus 로고    scopus 로고
    • Immune recognition and cross-reactivity of botulinum neurotoxins
    • Edited by M. F. Brin, M. Hallett & J. Jankovic. Philadelphia: Lippincott Williams & Wilkins
    • Atassi, M. Z. (2002). Immune recognition and cross-reactivity of botulinum neurotoxins. In Scientific and Therapeutic Aspects of Botulinum Toxins, pp. 385-408. Edited by M. F. Brin, M. Hallett & J. Jankovic. Philadelphia: Lippincott Williams & Wilkins.
    • (2002) Scientific and Therapeutic Aspects of Botulinum Toxins , pp. 385-408
    • Atassi, M.Z.1
  • 6
    • 3042774054 scopus 로고    scopus 로고
    • Basic immunological aspects of botulinum toxin therapy
    • Atassi, M. Z. (2004). Basic immunological aspects of botulinum toxin therapy. Mov Disord Suppl 8, S68-S84.
    • (2004) Mov Disord Suppl , vol.8
    • Atassi, M.Z.1
  • 7
    • 0033023671 scopus 로고    scopus 로고
    • Structure, activity, and immune (T and B cell) recognition of botulinum neurotoxins
    • Atassi, M. Z. & Oshima, M. (1999). Structure, activity, and immune (T and B cell) recognition of botulinum neurotoxins. Crit Rev Immunol 19, 219-260.
    • (1999) Crit Rev Immunol , vol.19 , pp. 219-260
    • Atassi, M.Z.1    Oshima, M.2
  • 8
    • 0030472583 scopus 로고    scopus 로고
    • Mapping of the antibody-binding regions on botulinum neurotoxin H-Chain domain 855-1296 with anti-toxin antibodies from three host species
    • Atassi, M. Z., Dolimbek, B. Z., Hayakari, M., Middlebrook, J. L., Whitney, B. & Oshima, M. (1996). Mapping of the antibody-binding regions on botulinum neurotoxin H-Chain domain 855-1296 with anti-toxin antibodies from three host species. J Protein Chem 15, 691-700.
    • (1996) J Protein Chem , vol.15 , pp. 691-700
    • Atassi, M.Z.1    Dolimbek, B.Z.2    Hayakari, M.3    Middlebrook, J.L.4    Whitney, B.5    Oshima, M.6
  • 9
    • 20444390489 scopus 로고    scopus 로고
    • Submolecular recognition profiles in two mouse strains of non-protective and protective anti-bodies against botulinum neurotoxin A
    • Atassi, M. Z., Dolimbek, G. S., Deitiker, P. R., Aoki, K. R. & Dolimbek, B. Z. (2005). Submolecular recognition profiles in two mouse strains of non-protective and protective anti-bodies against botulinum neurotoxin A. Mol Immunol 42, 1509-1520.
    • (2005) Mol Immunol , vol.42 , pp. 1509-1520
    • Atassi, M.Z.1    Dolimbek, G.S.2    Deitiker, P.R.3    Aoki, K.R.4    Dolimbek, B.Z.5
  • 10
    • 0034895356 scopus 로고    scopus 로고
    • Botulinum toxin therapy for pain and inflammatory disorders: Mechanisms and therapeutic effects
    • Borodic, G. E., Acquadro, M. & Johnson, E. A. (2001). Botulinum toxin therapy for pain and inflammatory disorders: mechanisms and therapeutic effects. Expert Opin Investig Drugs 10, 1531-1544.
    • (2001) Expert Opin Investig Drugs , vol.10 , pp. 1531-1544
    • Borodic, G.E.1    Acquadro, M.2    Johnson, E.A.3
  • 11
    • 0032718516 scopus 로고    scopus 로고
    • Safety and efficacy of NeuroBloc (botulinum toxin type B) in type A-responsive cervical dystonia
    • & 10 other authors
    • Brashear, A., Lew, M. F., Dykstra, D. D. & 10 other authors (1999). Safety and efficacy of NeuroBloc (botulinum toxin type B) in type A-responsive cervical dystonia. Neurology 53, 1439-1446.
    • (1999) Neurology , vol.53 , pp. 1439-1446
    • Brashear, A.1    Lew, M.F.2    Dykstra, D.D.3
  • 12
    • 2942642140 scopus 로고    scopus 로고
    • Botulinum toxin type B in upper-limb poststroke spasticity: A double-blind, placebo-controlled trial
    • Brashear, A., McAfee, A. L., Kuhn, E. R. & Fyffe, J. (2004). Botulinum toxin type B in upper-limb poststroke spasticity: a double-blind, placebo-controlled trial. Arch Phys Med Rehabil 85, 705-709.
    • (2004) Arch Phys Med Rehabil , vol.85 , pp. 705-709
    • Brashear, A.1    McAfee, A.L.2    Kuhn, E.R.3    Fyffe, J.4
  • 13
    • 0036558786 scopus 로고    scopus 로고
    • Botulinum toxin type B: An overview of its biochemistry and preclinical pharmacology
    • Callaway, J. E., Arezzo, J. C. & Grethlein, A. J. (2002). Botulinum toxin type B: an overview of its biochemistry and preclinical pharmacology. Dis Mon 48, 367-383.
    • (2002) Dis Mon , vol.48 , pp. 367-383
    • Callaway, J.E.1    Arezzo, J.C.2    Grethlein, A.J.3
  • 14
    • 29744448678 scopus 로고    scopus 로고
    • Chromatographic analysis of allosteric effects between ibuprofen and benzodiazepines on human serum albumin
    • Chen, J., Fitos, I. & Hage, D. S. (2006). Chromatographic analysis of allosteric effects between ibuprofen and benzodiazepines on human serum albumin. Chirality 18, 24-36.
    • (2006) Chirality , vol.18 , pp. 24-36
    • Chen, J.1    Fitos, I.2    Hage, D.S.3
  • 15
    • 33744465534 scopus 로고    scopus 로고
    • Practical applications of high-affinity, albumin-binding proteins from a group G streptococcal isolate
    • Coyle, E. M., Blazer, L. L., White, A. A., Hess, J. L. & Boyle, M. D. (2006). Practical applications of high-affinity, albumin-binding proteins from a group G streptococcal isolate. Appl Microbiol Biotechnol 71, 39-45.
    • (2006) Appl Microbiol Biotechnol , vol.71 , pp. 39-45
    • Coyle, E.M.1    Blazer, L.L.2    White, A.A.3    Hess, J.L.4    Boyle, M.D.5
  • 16
    • 18744383047 scopus 로고    scopus 로고
    • N domain (residues 449-859) of the heavy chain of botulinum neurotoxin A in two high-responder mouse strains
    • N domain (residues 449-859) of the heavy chain of botulinum neurotoxin A in two high-responder mouse strains. Immunol Invest 34, 119-142.
    • (2005) Immunol Invest , vol.34 , pp. 119-142
    • Dolimbek, G.S.1    Dolimbek, B.Z.2    Aoki, K.R.3    Atassi, M.Z.4
  • 17
    • 23944454472 scopus 로고    scopus 로고
    • Botulinum toxin type B de novo therapy of cervical dystonia frequency of antibody induced therapy failure
    • Dressler, D. & Bigalke, H. (2005). Botulinum toxin type B de novo therapy of cervical dystonia frequency of antibody induced therapy failure. J Neurol 252, 904-907.
    • (2005) J Neurol , vol.252 , pp. 904-907
    • Dressler, D.1    Bigalke, H.2
  • 18
    • 0031239673 scopus 로고    scopus 로고
    • Botulinum A toxin therapy: Neutralizing and nonneutralizing Abs - Therapeutic consequences
    • Göchel, H., Wohlfarth, K., Frevert, J., Dengler, R. & Bigalke, H. (1997). Botulinum A toxin therapy: neutralizing and nonneutralizing Abs - therapeutic consequences. Exp Neurol 147, 96-102.
    • (1997) Exp Neurol , vol.147 , pp. 96-102
    • Göchel, H.1    Wohlfarth, K.2    Frevert, J.3    Dengler, R.4    Bigalke, H.5
  • 20
    • 0002988277 scopus 로고    scopus 로고
    • Botulinum toxin clinical implications of antigenicity and immunoresistance
    • Edited by M. F. Brin, M. Hallett & J. Jankovic. Philadelphia: Lippincott Williams & Wilkins
    • Jankovic, J. (2002). Botulinum toxin clinical implications of antigenicity and immunoresistance. In Scientific and Therapeutic Aspects of Botulinum Toxin, pp. 409-415. Edited by M. F. Brin, M. Hallett & J. Jankovic. Philadelphia: Lippincott Williams & Wilkins.
    • (2002) Scientific and Therapeutic Aspects of Botulinum Toxin , pp. 409-415
    • Jankovic, J.1
  • 21
    • 3042747490 scopus 로고    scopus 로고
    • Botulinum toxin in clinical practice
    • Jankovic, J. (2004). Botulinum toxin in clinical practice. J Neurol Neurosurg Psychiatr 75, 951-957.
    • (2004) J Neurol Neurosurg Psychiatr , vol.75 , pp. 951-957
    • Jankovic, J.1
  • 23
  • 24
    • 0018642534 scopus 로고
    • Topographic antigenic determinants on cytochrome c. Immunoadsorbent separation of the rabbit antibody populations directed against horse cytochrome
    • Jemmerson, R. & Margoliash, E. (1979). Topographic antigenic determinants on cytochrome c. Immunoadsorbent separation of the rabbit antibody populations directed against horse cytochrome. J Biol Chem 254, 12706-12716.
    • (1979) J Biol Chem , vol.254 , pp. 12706-12716
    • Jemmerson, R.1    Margoliash, E.2
  • 25
    • 27844506038 scopus 로고    scopus 로고
    • 2 and CO binding properties of artificial hemoproteins formed by complexing iron protoporphyrin IX with human serum albumin mutants
    • 2 and CO binding properties of artificial hemoproteins formed by complexing iron protoporphyrin IX with human serum albumin mutants. J Am Chem Soc 127, 15933-15942.
    • (2005) J Am Chem Soc , vol.127 , pp. 15933-15942
    • Komatsu, T.1    Ohmichi, N.2    Nakagawa, A.3    Zunszain, P.A.4    Curry, S.5    Tsuchida, E.6
  • 26
    • 27744451445 scopus 로고    scopus 로고
    • Production of anti-neurotoxin antibody is enhanced by two subcomponents, HA1 and HA3b, of Clostridium botulinum type B 16S toxin-haemagglutinin
    • & 7 other authors
    • Lee, J.-C., Yokota, K., Arimitsu, H. & 7 other authors (2005). Production of anti-neurotoxin antibody is enhanced by two subcomponents, HA1 and HA3b, of Clostridium botulinum type B 16S toxin-haemagglutinin. Microbiology 151, 3739-3747.
    • (2005) Microbiology , vol.151 , pp. 3739-3747
    • Lee, J.-C.1    Yokota, K.2    Arimitsu, H.3
  • 27
    • 0346728689 scopus 로고    scopus 로고
    • Formation of tannin-albumin nano-particles at neutral pH as measured by light scattering techniques
    • Lin, H. C., Chen, P. C., Cheng, T. J. & Chen, R. L. (2004). Formation of tannin-albumin nano-particles at neutral pH as measured by light scattering techniques. Anal Biochem 325, 117-120.
    • (2004) Anal Biochem , vol.325 , pp. 117-120
    • Lin, H.C.1    Chen, P.C.2    Cheng, T.J.3    Chen, R.L.4
  • 28
    • 29344458115 scopus 로고    scopus 로고
    • Chaperone-like features of bovine serum albumin: A comparison with alpha-crystallin
    • Marini, I., Moschini, R., Corso, A. D. & Mura, U. (2005). Chaperone-like features of bovine serum albumin: a comparison with alpha-crystallin. Cell Mol Life Sci 62, 3092-3099.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 3092-3099
    • Marini, I.1    Moschini, R.2    Corso, A.D.3    Mura, U.4
  • 30
    • 1242271236 scopus 로고    scopus 로고
    • Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering
    • Militello, V., Casarino, C., Emanuele, A., Giostra, A., Pullara, F. & Leone, M. (2004). Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering. Biophys Chem 107, 175-187.
    • (2004) Biophys Chem , vol.107 , pp. 175-187
    • Militello, V.1    Casarino, C.2    Emanuele, A.3    Giostra, A.4    Pullara, F.5    Leone, M.6
  • 31
    • 0041825189 scopus 로고    scopus 로고
    • Effect of high shear rate on stability of proteins: Kinetic study
    • Oliva, A., Santovena, A., Farina, J. & Llabres, M. (2003). Effect of high shear rate on stability of proteins: kinetic study. J Pharm Biomed Anal 33, 145-155.
    • (2003) J Pharm Biomed Anal , vol.33 , pp. 145-155
    • Oliva, A.1    Santovena, A.2    Farina, J.3    Llabres, M.4
  • 32
    • 6844266275 scopus 로고    scopus 로고
    • What is the optimal dose of botulinum toxin A in the treatment of cervical dystonia? Results of a double blind, placebo controlled, dose ranging study using Dysport
    • & 8 other authors German Dystonia Study Group
    • Poewe, W., Deuschl, G., Nebe, A. & 8 other authors (1998). What is the optimal dose of botulinum toxin A in the treatment of cervical dystonia? Results of a double blind, placebo controlled, dose ranging study using Dysport. German Dystonia Study Group. J Neurol Neurosurg Psychiatr 64, 13-17.
    • (1998) J Neurol Neurosurg Psychiatr , vol.64 , pp. 13-17
    • Poewe, W.1    Deuschl, G.2    Nebe, A.3
  • 33
    • 0014939173 scopus 로고
    • Immunological activity of cytochrome c. 3. Enhancement of antibody detection and immune response initiation by cytochrome c polymers
    • Reichlin, M., Nisonoff, A. & Margoliash, E. (1970). Immunological activity of cytochrome c. 3. Enhancement of antibody detection and immune response initiation by cytochrome c polymers. J Biol Chem 245, 947-954.
    • (1970) J Biol Chem , vol.245 , pp. 947-954
    • Reichlin, M.1    Nisonoff, A.2    Margoliash, E.3
  • 34
    • 0030741208 scopus 로고    scopus 로고
    • Localization of the regions on the C-terminal domain of the heavy chain of botulinum toxin A recognized by T-lymphocytes and by antibodies after immunization of mice with pentavalent toxoid
    • Rosenberg, J. S., Middlebrook, J. L. & Atassi, M. Z. (1997). Localization of the regions on the C-terminal domain of the heavy chain of botulinum toxin A recognized by T-lymphocytes and by antibodies after immunization of mice with pentavalent toxoid. Immunol Invest 26, 491-504.
    • (1997) Immunol Invest , vol.26 , pp. 491-504
    • Rosenberg, J.S.1    Middlebrook, J.L.2    Atassi, M.Z.3
  • 35
    • 27844528378 scopus 로고    scopus 로고
    • G148-GA3: A streptococcal virulence module with atypical thermodynamics of folding optimally binds human serum albumin at physiological temperatures
    • Rozak, D. A., Orban, J. & Bryan, P. N. (2005). G148-GA3: a streptococcal virulence module with atypical thermodynamics of folding optimally binds human serum albumin at physiological temperatures. Biochim Biophys Acta 1753, 226-233.
    • (2005) Biochim Biophys Acta , vol.1753 , pp. 226-233
    • Rozak, D.A.1    Orban, J.2    Bryan, P.N.3
  • 36
    • 2542575542 scopus 로고    scopus 로고
    • Irreversible formation of intermediate BSA oligomers requires and induces conformational changes
    • Vaiana, S. M., Emanuele, A., Palma-Vittorelli, M. B. & Palma, M. U. (2004). Irreversible formation of intermediate BSA oligomers requires and induces conformational changes. Proteins 55, 1053-1062.
    • (2004) Proteins , vol.55 , pp. 1053-1062
    • Vaiana, S.M.1    Emanuele, A.2    Palma-Vittorelli, M.B.3    Palma, M.U.4
  • 37
    • 33745821319 scopus 로고    scopus 로고
    • Toxin neutralizing antibody formation with botulinum toxin type A (BoNTA) treatment
    • 57th Annual Meeting of the American Academy of Neurology, Abstract P01.153, 12 April 2005, Miami Beach, Florida
    • Yablon, S. A., Daggett, S. & Brin, M. F. (2005). Toxin neutralizing antibody formation with botulinum toxin type A (BoNTA) treatment. In 57th Annual Meeting of the American Academy of Neurology, Abstract P01.153, 12 April 2005, Miami Beach, Florida.
    • (2005)
    • Yablon, S.A.1    Daggett, S.2    Brin, M.F.3
  • 38
    • 0020433162 scopus 로고
    • Genetic control of the immune response to myoglobin. IX. Overcoming genetic control of antibody response to antigenic sites by increasing the dose of antigen used in immunization
    • Young, C. R. & Atassi, M. Z. (1982). Genetic control of the immune response to myoglobin. IX. Overcoming genetic control of antibody response to antigenic sites by increasing the dose of antigen used in immunization. Immunogen 9, 343-351.
    • (1982) Immunogen , vol.9 , pp. 343-351
    • Young, C.R.1    Atassi, M.Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.