메뉴 건너뛰기




Volumn 424, Issue 2, 2009, Pages 263-272

Identification of potent nanobodies to neutralize the most poisonous polypeptide from scorpion venom

Author keywords

Anti venom; Dromedary; Recombinant antibody; Scorpion toxin; Single domain antibody

Indexed keywords

DISSOCIATION; EPITOPES; EQUILIBRIUM CONSTANTS; MEDICAL PROBLEMS; MONOCLONAL ANTIBODIES; RATE CONSTANTS; TOXIC MATERIALS;

EID: 70450178687     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090697     Document Type: Article
Times cited : (53)

References (46)
  • 1
    • 0028016289 scopus 로고
    • Scorpionism and serotherapy in Mexico
    • Dehesa-Davila, M. and Possani, L. D. (1994) Scorpionism and serotherapy in Mexico. Toxicon 32, 1015-1018
    • (1994) Toxicon , vol.32 , pp. 1015-1018
    • Dehesa-Davila, M.1    Possani, L.D.2
  • 2
    • 0020014262 scopus 로고
    • Epidemiology and clinical characteristics of scorpion envenomation in Tunisia
    • Goyffon, M., Vachon, M. and Broglio, N. (1982) Epidemiology and clinical characteristics of scorpion envenomation in Tunisia. Toxicon 20, 337-344
    • (1982) Toxicon , vol.20 , pp. 337-344
    • Goyffon, M.1    Vachon, M.2    Broglio, N.3
  • 4
    • 0019181273 scopus 로고
    • Two types of scorpion neurotoxin characterized by their binding to two separate receptor sites on rat brain synaptosomes
    • Jover, E., Couraud, F. and Rochat, H. (1980) Two types of scorpion neurotoxin characterized by their binding to two separate receptor sites on rat brain synaptosomes. Biochem. Biophys. Res. Commun. 95, 1607-1614
    • (1980) Biochem. Biophys. Res. Commun , vol.95 , pp. 1607-1614
    • Jover, E.1    Couraud, F.2    Rochat, H.3
  • 5
    • 0003017338 scopus 로고
    • Scorpions neurotoxins. Effects and Mechanisms
    • Chang, L. W. and Dyer, R. S, eds, pp, Dekker, New York
    • Martin-Eauclaire, M. F. and Couraud, F. (1995) Scorpions neurotoxins. Effects and Mechanisms. In Handbook of Neurotoxicity (Chang, L. W. and Dyer, R. S., eds), pp. 683-716, Dekker, New York
    • (1995) Handbook of Neurotoxicity , pp. 683-716
    • Martin-Eauclaire, M.F.1    Couraud, F.2
  • 6
    • 1942436845 scopus 로고    scopus 로고
    • Quantitative variability in the biodistribution and in toxinokinetic studies of the three main alpha toxins from the Androctonus australis hector scorpion venom
    • Devaux, C., Jouirou, B., Naceur-Krifi, M., Clot-Faybesse, O., El Ayeb, M. and Rochat, H. (2004) Quantitative variability in the biodistribution and in toxinokinetic studies of the three main alpha toxins from the Androctonus australis hector scorpion venom. Toxicon 43, 661-669
    • (2004) Toxicon , vol.43 , pp. 661-669
    • Devaux, C.1    Jouirou, B.2    Naceur-Krifi, M.3    Clot-Faybesse, O.4    El Ayeb, M.5    Rochat, H.6
  • 7
    • 0014884098 scopus 로고
    • Purification of animal neurotoxins. Isolation and characterization of eleven neurotoxins from the venom of the scorpion Androctonus australis hector, Buthus occitanus tunetanus and Leiurus quinquestriatus quinquestriatus
    • Miranda, F., Kopeyan, C., Rochat, H. and Lissitzky, S. (1970) Purification of animal neurotoxins. Isolation and characterization of eleven neurotoxins from the venom of the scorpion Androctonus australis hector, Buthus occitanus tunetanus and Leiurus quinquestriatus quinquestriatus. Eur. J. Biochem. 16, 279-291
    • (1970) Eur. J. Biochem , vol.16 , pp. 279-291
    • Miranda, F.1    Kopeyan, C.2    Rochat, H.3    Lissitzky, S.4
  • 8
    • 0018400724 scopus 로고
    • Scorpion toxins: Chemistry and mode of action
    • Rochat, H., Bernard, P. and Couraud, F. (1979) Scorpion toxins: chemistry and mode of action. Adv. Cytopharmacol. 3, 325-330
    • (1979) Adv. Cytopharmacol , vol.3 , pp. 325-330
    • Rochat, H.1    Bernard, P.2    Couraud, F.3
  • 9
    • 0024094439 scopus 로고
    • Orthorhombic crystals and three-dimensional structure of the potent toxin II from the scorpion
    • Fontecilla-Camps, J. C., Habersetzer-Rochat, C. and Rochat, H. (1988) Orthorhombic crystals and three-dimensional structure of the potent toxin II from the scorpion. Proc. Natl. Acad. Sci. U.S.A. 85, 7443-7447
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 7443-7447
    • Fontecilla-Camps, J.C.1    Habersetzer-Rochat, C.2    Rochat, H.3
  • 10
    • 0028233375 scopus 로고
    • Crystal structure of toxinII from the scorpion Androctonus australis hector refined at 1.3 Å resolution
    • Housset, D., Haberstrer-Rochat, C., Artier, J. P. and Fontecilla-Camps, J. C. (1994) Crystal structure of toxinII from the scorpion Androctonus australis hector refined at 1.3 Å resolution. J. Mol. Biol. 238, 88-90
    • (1994) J. Mol. Biol , vol.238 , pp. 88-90
    • Housset, D.1    Haberstrer-Rochat, C.2    Artier, J.P.3    Fontecilla-Camps, J.C.4
  • 11
    • 0020523715 scopus 로고
    • Immunochemistry of scorpion α-neurotoxins. Determination of the antigenic site number and isolation of a highly enriched antibody specific to a single antigenic site of toxin II of Androctonus australis hector
    • El Ayeb, M., Martin, M. F., Delori, P., Bechis, G. and Rochat, H. (1983) Immunochemistry of scorpion α-neurotoxins. Determination of the antigenic site number and isolation of a highly enriched antibody specific to a single antigenic site of toxin II of Androctonus australis hector. Mol. Immunol. 20, 697-708
    • (1983) Mol. Immunol , vol.20 , pp. 697-708
    • El Ayeb, M.1    Martin, M.F.2    Delori, P.3    Bechis, G.4    Rochat, H.5
  • 12
    • 70450184155 scopus 로고
    • Use of antibodies specific to defined regions of scorpion α-toxin to study its interaction with its receptor sites on the sodium channel
    • El Ayeb, M., Bahraoui, E. M., Granier, C. and Rochat, H. (1986) Use of antibodies specific to defined regions of scorpion α-toxin to study its interaction with its receptor sites on the sodium channel. Biochemistry 139, 3371-3377
    • (1986) Biochemistry , vol.139 , pp. 3371-3377
    • El Ayeb, M.1    Bahraoui, E.M.2    Granier, C.3    Rochat, H.4
  • 14
    • 0031803535 scopus 로고    scopus 로고
    • Venoms, antivenoms and immunotherapy
    • Chippaux, J. P. and Goyffon, M. (1998) Venoms, antivenoms and immunotherapy. Toxicon 36, 823-846
    • (1998) Toxicon , vol.36 , pp. 823-846
    • Chippaux, J.P.1    Goyffon, M.2
  • 15
    • 0030297275 scopus 로고    scopus 로고
    • Immunoreactivity and pharmacokinetic of horse anti-scorpion venom F(ab')2 scorpion venom interactions
    • Pepin-Cavotta, S., Lutsch, C., Grandgeorge, M., Lang, J. and Scherrmann, J. M. (1996) Immunoreactivity and pharmacokinetic of horse anti-scorpion venom F(ab')2 scorpion venom interactions. Toxicol. App. Pharmacol. 141, 272-277
    • (1996) Toxicol. App. Pharmacol , vol.141 , pp. 272-277
    • Pepin-Cavotta, S.1    Lutsch, C.2    Grandgeorge, M.3    Lang, J.4    Scherrmann, J.M.5
  • 16
    • 0028023137 scopus 로고
    • The treatment of the scorpion envenoming syndrome: The Saudi experience with serotherapy
    • Ismail, M. (1994) The treatment of the scorpion envenoming syndrome: the Saudi experience with serotherapy. Toxicon 32, 1019-1026
    • (1994) Toxicon , vol.32 , pp. 1019-1026
    • Ismail, M.1
  • 17
  • 18
    • 0031796865 scopus 로고    scopus 로고
    • Immunotherapy for scorpion envenoming in Brazil
    • Rezende, N. A., Amaral, C. F. and Freire-Maia, L. (1998) Immunotherapy for scorpion envenoming in Brazil. Toxicon 36, 1507-1513
    • (1998) Toxicon , vol.36 , pp. 1507-1513
    • Rezende, N.A.1    Amaral, C.F.2    Freire-Maia, L.3
  • 19
    • 34247494331 scopus 로고    scopus 로고
    • Utility of scorpion antivenin vs prazosin in the management of severe Mesobuthus tamulus envenoming at rural settings
    • Bawaskar, H. S. and Bawaskar, P. H. (2007) Utility of scorpion antivenin vs prazosin in the management of severe Mesobuthus tamulus envenoming at rural settings. J. Assoc. Physicians India 55, 14-21
    • (2007) J. Assoc. Physicians India , vol.55 , pp. 14-21
    • Bawaskar, H.S.1    Bawaskar, P.H.2
  • 20
    • 0028225327 scopus 로고
    • Scorpion envenomation and antivenom therapy
    • Sofer, S., Shahak, E. and Gueron, M. (1994) Scorpion envenomation and antivenom therapy. J. Pediatr. 124, 973-978
    • (1994) J. Pediatr , vol.124 , pp. 973-978
    • Sofer, S.1    Shahak, E.2    Gueron, M.3
  • 21
    • 0024044244 scopus 로고
    • Monoclonal antobodies to scorpion toxins characterization and molecular mechanisms of neutralization
    • Bahraoui, E., Pichon, J., Muller, J. M., Darbon, H., El Ayeb, M., Granier, C., Marvaldi, J. and Rochat, H. (1988) Monoclonal antobodies to scorpion toxins characterization and molecular mechanisms of neutralization. J. Immunol. 141, 214-220
    • (1988) J. Immunol , vol.141 , pp. 214-220
    • Bahraoui, E.1    Pichon, J.2    Muller, J.M.3    Darbon, H.4    El Ayeb, M.5    Granier, C.6    Marvaldi, J.7    Rochat, H.8
  • 22
    • 0032910690 scopus 로고    scopus 로고
    • A recombinant single chain antibody fragment that neutralizes toxin II from the venom of the scorpion Androctonus australis hector
    • Mousli, M., Devaux, C., Rochat, H., Goyffon, M. and Billiad, P. (1999) A recombinant single chain antibody fragment that neutralizes toxin II from the venom of the scorpion Androctonus australis hector. FEBS Lett. 452, 183-188
    • (1999) FEBS Lett , vol.452 , pp. 183-188
    • Mousli, M.1    Devaux, C.2    Rochat, H.3    Goyffon, M.4    Billiad, P.5
  • 23
    • 0034834559 scopus 로고    scopus 로고
    • Construction and functional evaluation of a single-chain antibody fragment that neutralizes toxin AahI from the venom of the scorpion Androctonus australis hector
    • Devaux, C., Moreau, E., Goyffon, M., Rochat, H. and Billiald, P. (2001) Construction and functional evaluation of a single-chain antibody fragment that neutralizes toxin AahI from the venom of the scorpion Androctonus australis hector. Eur. J. Biochem. 268, 694-702
    • (2001) Eur. J. Biochem , vol.268 , pp. 694-702
    • Devaux, C.1    Moreau, E.2    Goyffon, M.3    Rochat, H.4    Billiald, P.5
  • 25
    • 18944365788 scopus 로고    scopus 로고
    • A strategy for the generation of specific human antibodies by directed evolution and phage display. An example of a single-chain antibody fragment that neutralizes a major component of scorpion venom
    • Riaño-Umbarila, L., Juárez-González, V. R., Olamendi-Portugal, T., Ortíz-León, M., Possani, L. D. and Becerril, B. (2005) A strategy for the generation of specific human antibodies by directed evolution and phage display. An example of a single-chain antibody fragment that neutralizes a major component of scorpion venom. FEBS J. 272, 2591-2601
    • (2005) FEBS J , vol.272 , pp. 2591-2601
    • Riaño-Umbarila, L.1    Juárez-González, V.R.2    Olamendi-Portugal, T.3    Ortíz-León, M.4    Possani, L.D.5    Becerril, B.6
  • 26
    • 0034755438 scopus 로고    scopus 로고
    • Functional heavy-chain antibodies in Camelidae
    • Nguyen, V. K., Desmyter, A. and Muyldermans, S. (2001) Functional heavy-chain antibodies in Camelidae. Adv. Immunol. 79, 261-296
    • (2001) Adv. Immunol , vol.79 , pp. 261-296
    • Nguyen, V.K.1    Desmyter, A.2    Muyldermans, S.3
  • 30
    • 0028168145 scopus 로고
    • Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains
    • Muyldermans, S., Atarhouch, T., Saldanha, J., Barbosa, J. A. and Hamers, R. (1994) Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Prot. Eng. 7, 1129-1135
    • (1994) Prot. Eng , vol.7 , pp. 1129-1135
    • Muyldermans, S.1    Atarhouch, T.2    Saldanha, J.3    Barbosa, J.A.4    Hamers, R.5
  • 32
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single-domain antibody fragments from camel heavy-chain antibodies
    • Arbabi-Ghahroudi, M., Desmyter, A., Wyns, L., Hamers, R. and Muyldermans, S. (1997) Selection and identification of single-domain antibody fragments from camel heavy-chain antibodies. FEBS Lett. 414, 521-526
    • (1997) FEBS Lett , vol.414 , pp. 521-526
    • Arbabi-Ghahroudi, M.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5
  • 39
    • 0019955670 scopus 로고
    • Neutralizing monoclonal antibody specific for Naja nigrcollis toxin α preparation, characterization and localization of the antigenic binding site
    • Boulain, J. C., Ménez, A., Couderc, J., Faure, G., Liacopoulos, P. and Fromageot, P. (1982) Neutralizing monoclonal antibody specific for Naja nigrcollis toxin α preparation, characterization and localization of the antigenic binding site. Biochemistry 21, 2910-2915
    • (1982) Biochemistry , vol.21 , pp. 2910-2915
    • Boulain, J.C.1    Ménez, A.2    Couderc, J.3    Faure, G.4    Liacopoulos, P.5    Fromageot, P.6
  • 40
    • 0022966726 scopus 로고
    • Two neutralizing monoclonal antibodies specific for Naja nigricollis cardiotoxin: Preparation, characterization and localisation of the epitopes
    • Grognet, J. M., Gatineau, E., Bougis, P., Harvey, A. L., Couderc, J., Fromageot, P. and Ménez, A. (1986) Two neutralizing monoclonal antibodies specific for Naja nigricollis cardiotoxin: preparation, characterization and localisation of the epitopes. Mol. Immunol. 23, 1329-1337
    • (1986) Mol. Immunol , vol.23 , pp. 1329-1337
    • Grognet, J.M.1    Gatineau, E.2    Bougis, P.3    Harvey, A.L.4    Couderc, J.5    Fromageot, P.6    Ménez, A.7
  • 41
    • 13844296953 scopus 로고    scopus 로고
    • Directed evolution, phage display and combination of evolved mutants: A strategy to recover the neutralization properties of the scFv version of BCF2 a neutralizing monoclonal antibody specific to scorpion toxin Cn2
    • Juarez-Gonzalez, V. R., Riano-Umbariala, L., Quintero-Hernandez, V., Olamendi-Portugal, T., Ortiz-Leon, M., Ortiz, E., Possani, L. D. and Becerril, B. (2005) Directed evolution, phage display and combination of evolved mutants: a strategy to recover the neutralization properties of the scFv version of BCF2 a neutralizing monoclonal antibody specific to scorpion toxin Cn2. J. Mol. Biol. 346, 1287-1297
    • (2005) J. Mol. Biol , vol.346 , pp. 1287-1297
    • Juarez-Gonzalez, V.R.1    Riano-Umbariala, L.2    Quintero-Hernandez, V.3    Olamendi-Portugal, T.4    Ortiz-Leon, M.5    Ortiz, E.6    Possani, L.D.7    Becerril, B.8
  • 42
    • 33748809530 scopus 로고    scopus 로고
    • The change of the scFv into the Fab format improves the stability and in vivo toxin neutralization capacity of recombinant antibodies
    • Quintero-Hernández, V., Juárez-González, V. R., Ortíz-León, M., Sánchez, R., Possani, L. D. and Becerril, B. (2007) The change of the scFv into the Fab format improves the stability and in vivo toxin neutralization capacity of recombinant antibodies. Mol. Immunol. 44, 1307-1315
    • (2007) Mol. Immunol , vol.44 , pp. 1307-1315
    • Quintero-Hernández, V.1    Juárez-González, V.R.2    Ortíz-León, M.3    Sánchez, R.4    Possani, L.D.5    Becerril, B.6
  • 43
    • 0035715877 scopus 로고    scopus 로고
    • Single domain camel antibodies: Current status
    • Muyldermans, S. (2001) Single domain camel antibodies: current status. J. Biotechnol. 74, 277-302
    • (2001) J. Biotechnol , vol.74 , pp. 277-302
    • Muyldermans, S.1
  • 44
    • 0037070507 scopus 로고    scopus 로고
    • Large-scale production of VHH antibody fragments by Saccharomyces cerevisiae
    • Thomassen, Y. E., Meijer, W., Sierkstra, L. and Verrips, T. C.. (2002) Large-scale production of VHH antibody fragments by Saccharomyces cerevisiae. Enzyme Microb. Technol. 30, 273-278
    • (2002) Enzyme Microb. Technol , vol.30 , pp. 273-278
    • Thomassen, Y.E.1    Meijer, W.2    Sierkstra, L.3    Verrips, T.C.4
  • 45
    • 0033961580 scopus 로고    scopus 로고
    • Frenken, L. G., van der Linden, R. H., Hermans, P. W., Bos, J. W., Ruuls, R. C., de Geus, B.Verrips C. T. and Verrips, C. T. (2000) Isolation of antigen specific Llama V HH antibody fragments and their high level secretion by Saccharomyces cerevisiae. J. Biotechnol. 78, 11-21
    • Frenken, L. G., van der Linden, R. H., Hermans, P. W., Bos, J. W., Ruuls, R. C., de Geus, B.Verrips C. T. and Verrips, C. T. (2000) Isolation of antigen specific Llama V HH antibody fragments and their high level secretion by Saccharomyces cerevisiae. J. Biotechnol. 78, 11-21
  • 46
    • 59149104037 scopus 로고    scopus 로고
    • General strategy to humanize a camel single domain antibody and identification of a universal humanized nanobody scaffold
    • Vincke, C., Loris, R., Saerens, D., Martinez-Rodriguez, S., Muyldermans, S. and Conrath, K. (2009) General strategy to humanize a camel single domain antibody and identification of a universal humanized nanobody scaffold. J. Biol. Chem. 284, 3273-3284
    • (2009) J. Biol. Chem , vol.284 , pp. 3273-3284
    • Vincke, C.1    Loris, R.2    Saerens, D.3    Martinez-Rodriguez, S.4    Muyldermans, S.5    Conrath, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.