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Volumn 6, Issue 8, 2014, Pages 2541-2567

Engineering Venom's toxin-neutralizing antibody fragments and its therapeutic potential

Author keywords

Antibody; Antivenom; Diabody; Nanobody; scFv; Scorpion stings; Serum therapy; Snakebite

Indexed keywords

BISPECIFIC ANTIBODY; DIPHTHERIA ANTIBODY; EPITOPE; NANOBODY; NEUTRALIZING ANTIBODY; NOXIUSTOXIN; RECOMBINANT ANTIBODY; SCORPION VENOM; SERRUMAB; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; SNAKE VENOM; SODIUM CHANNEL; TITYUS TOXIN; UNCLASSIFIED DRUG; VENOM ANTISERUM; IMMUNOGLOBULIN FRAGMENT; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN; VENOM;

EID: 84927172700     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins6082541     Document Type: Review
Times cited : (49)

References (101)
  • 1
    • 64949131873 scopus 로고    scopus 로고
    • Tentacles of venom: Toxic protein convergence in the Kingdom Animalia
    • Fry, B.G.; Roelants, K.; Norman, J.A. Tentacles of venom: Toxic protein convergence in the Kingdom Animalia. J. Mol. Evol. 2009, 68, 311-321
    • (2009) J. Mol. Evol , vol.68 , pp. 311-321
    • Fry, B.G.1    Roelants, K.2    Norman, J.A.3
  • 3
    • 84925840665 scopus 로고
    • Ueber das zustandekommen der diphterie-immunitaet und der tetanus-immunitatet bei thieren
    • Behring, E.; Kitasato, S. Ueber das zustandekommen der diphterie-immunitaet und der tetanus-immunitatet bei thieren. Deutsch. Med. Wochenschr. 1890, 16, 1113-1114
    • (1890) Deutsch. Med. Wochenschr , vol.16 , pp. 1113-1114
    • Behring, E.1    Kitasato, S.2
  • 4
    • 78149234586 scopus 로고    scopus 로고
    • Passive immunotherapy today: Brief history
    • Goyffon, M. Passive immunotherapy today: Brief history. Biol. Aujourdhui 2010, 204, 51-54
    • (2010) Biol. Aujourdhui , vol.204 , pp. 51-54
    • Goyffon, M.1
  • 5
    • 53649102120 scopus 로고    scopus 로고
    • History of immunoglobulin replacement
    • Eibl, M.M. History of immunoglobulin replacement. Immunol. Allergy Clin. N. Am. 2008, 28, 737-764
    • (2008) Immunol. Allergy Clin. N. Am , vol.28 , pp. 737-764
    • Eibl, M.M.1
  • 7
    • 0028876405 scopus 로고
    • Intravenous immunoglobins (IVIGs) to prevent and treat infectious diseases
    • Cross, A.S. Intravenous immunoglobins (IVIGs) to prevent and treat infectious diseases. Adv. Exp. Med. Biol. 1995, 383, 123-130
    • (1995) Adv. Exp. Med. Biol , vol.383 , pp. 123-130
    • Cross, A.S.1
  • 8
    • 64349107630 scopus 로고    scopus 로고
    • Development trends for therapeutic antibody fragments
    • Nelson, A.L.; Reichert, J.M. Development trends for therapeutic antibody fragments. Nat. Biotechnol. 2009, 27, 331-337
    • (2009) Nat. Biotechnol , vol.27 , pp. 331-337
    • Nelson, A.L.1    Reichert, J.M.2
  • 9
    • 84863480395 scopus 로고    scopus 로고
    • Molecular engineering of antibodies for therapeutic and diagnostic purposes
    • Ducancel, F.; Muller, B.H. Molecular engineering of antibodies for therapeutic and diagnostic purposes. mAbs 2012, 4, 445-457
    • (2012) MAbs , vol.4 , pp. 445-457
    • Ducancel, F.1    Muller, B.H.2
  • 10
    • 84892590856 scopus 로고    scopus 로고
    • Antibodies to watch in 2014
    • Reichert, J.M. Antibodies to watch in 2014. mAbs 2014, 6, 5-14
    • (2014) MAbs , vol.6 , pp. 5-14
    • Reichert, J.M.1
  • 11
    • 84877955125 scopus 로고    scopus 로고
    • What are biosimilars and are they important?
    • Anonymous
    • Anonymous. What are biosimilars and are they important? Drug Ther. Bull. 2013, 51, 57-60
    • (2013) Drug Ther. Bull , vol.51 , pp. 57-60
  • 12
    • 0022417415 scopus 로고
    • First clinical use of penicillin
    • Lawrie, R. First clinical use of penicillin. Br. Med. J. Clin. Res. Ed. 1985, 290, 397
    • (1985) Br. Med. J. Clin. Res. Ed , vol.290 , pp. 397
    • Lawrie, R.1
  • 15
    • 84867903466 scopus 로고    scopus 로고
    • Emerging options for the management of scorpion stings
    • Chippaux, J.-P. Emerging options for the management of scorpion stings. Drug Des. Dev. Ther. 2012, 6, 165-173
    • (2012) Drug Des. Dev. Ther , vol.6 , pp. 165-173
    • Chippaux, J.-P.1
  • 16
    • 47649126821 scopus 로고    scopus 로고
    • Epidemiology of scorpionism: A global appraisa
    • Chippaux, J.-P.; Goyffon, M. Epidemiology of scorpionism: A global appraisa. Acta Trop. 2008, 107, 71-79
    • (2008) Acta Trop , vol.107 , pp. 71-79
    • Chippaux, J.-P.1    Goyffon, M.2
  • 17
    • 9644272420 scopus 로고    scopus 로고
    • Loxoscelism: Old obstacles, new directions
    • Hogan, C.J.; Barbaro, K.C.; Winkel, K. Loxoscelism: Old obstacles, new directions. Ann. Emerg. Med. 2004, 44, 608-624
    • (2004) Ann. Emerg. Med , vol.44 , pp. 608-624
    • Hogan, C.J.1    Barbaro, K.C.2    Winkel, K.3
  • 19
    • 84889093473 scopus 로고    scopus 로고
    • Safety of intravenous equine F(ab')2: Insights following clinical trials involving 1534 recipients of scorpion antivenom
    • Boyer, L.; Degan, J.; Ruha, A.-M.; Mallie, J.; Mangin, E.; Alagón, A. Safety of intravenous equine F(ab')2: Insights following clinical trials involving 1534 recipients of scorpion antivenom. Toxicon Off. J. Int. Soc. Toxinol. 2013, 76, 386-393
    • (2013) Toxicon Off. J. Int. Soc. Toxinol , vol.76 , pp. 386-393
    • Boyer, L.1    Degan, J.2    Ruha, A.-M.3    Mallie, J.4    Mangin, E.5    Alagón, A.6
  • 20
    • 78149273779 scopus 로고    scopus 로고
    • Guidelines for the production, control and regulation of snake antivenom immunoglobulins
    • Chippaux, J.-P. Guidelines for the production, control and regulation of snake antivenom immunoglobulins. Biol. Aujourdhui 2010, 204, 87-91
    • (2010) Biol. Aujourdhui , vol.204 , pp. 87-91
    • Chippaux, J.-P.1
  • 21
    • 0025918553 scopus 로고
    • Isolation of IgGT from hyperimmune horse anti-snake venom serum: Its protective ability
    • Fernandes, I.; Takehara, H.A.; Mota, I. Isolation of IgGT from hyperimmune horse anti-snake venom serum: Its protective ability. Toxicon Off. J. Int. Soc. Toxinol. 1991, 29, 1373-1379
    • (1991) Toxicon Off. J. Int. Soc. Toxinol , vol.29 , pp. 1373-1379
    • Fernandes, I.1    Takehara, H.A.2    Mota, I.3
  • 23
    • 79957509785 scopus 로고    scopus 로고
    • Antivenoms for the treatment of snakebite envenomings: The road ahead
    • Gutiérrez, J.M.; León, G.; Burnouf, T. Antivenoms for the treatment of snakebite envenomings: The road ahead. Biol. J. Int. Assoc. Biol. Stand. 2011, 39, 129-142
    • (2011) Biol. J. Int. Assoc. Biol. Stand , vol.39 , pp. 129-142
    • Gutiérrez, J.M.1    León, G.2    Burnouf, T.3
  • 25
    • 78149274387 scopus 로고    scopus 로고
    • Production of highly purified therapeutic immunoglobulins (HPTI): Analysis of a purification process
    • Nguyen, L. Production of highly purified therapeutic immunoglobulins (HPTI): Analysis of a purification process. Biol. Aujourdhui 2010, 204, 55-59
    • (2010) Biol. Aujourdhui , vol.204 , pp. 55-59
    • Nguyen, L.1
  • 26
    • 0035133283 scopus 로고    scopus 로고
    • Efficacy, safety, and use of snake antivenoms in the United States
    • Dart, R.C.; McNally, J. Efficacy, safety, and use of snake antivenoms in the United States. Ann. Emerg. Med. 2001, 37, 181-188
    • (2001) Ann. Emerg. Med , vol.37 , pp. 181-188
    • Dart, R.C.1    McNally, J.2
  • 28
    • 21344448811 scopus 로고    scopus 로고
    • Intravenous immunoglobulin therapy
    • Mouthon, L. Intravenous immunoglobulin therapy. Rev. Prat. 2005, 55, 1049-1056
    • (2005) Rev. Prat , vol.55 , pp. 1049-1056
    • Mouthon, L.1
  • 29
    • 38449084690 scopus 로고    scopus 로고
    • Historical development of monoclonal antibody therapeutics
    • Nissim, A.; Chernajovsky, Y. Historical development of monoclonal antibody therapeutics. Handb. Exp. Pharmacol. 2008, 181, 3-18
    • (2008) Handb. Exp. Pharmacol , vol.181 , pp. 3-18
    • Nissim, A.1    Chernajovsky, Y.2
  • 30
    • 0023864065 scopus 로고
    • Monoclonal antibodies as magic bullets
    • Brodsky, F.M. Monoclonal antibodies as magic bullets. Pharm. Res. 1988, 5, 1-9
    • (1988) Pharm. Res , vol.5 , pp. 1-9
    • Brodsky, F.M.1
  • 31
    • 0019884081 scopus 로고
    • A million dollars for the magic bullet
    • Sun, M. A million dollars for the magic bullet. Science 1981, 214, 1326-1327
    • (1981) Science , vol.214 , pp. 1326-1327
    • Sun, M.1
  • 32
    • 0036277088 scopus 로고    scopus 로고
    • A personal history of the CAMPATH-1H antibody
    • Waldmann, H. A personal history of the CAMPATH-1H antibody. Med. Oncol. Northwood Lond. Engl. 2002, 19 (Suppl.), S3-S9
    • (2002) Med. Oncol. Northwood Lond. Engl , vol.19 , Issue.SUPPL.
    • Waldmann, H.1
  • 33
    • 0023957561 scopus 로고
    • Reversal of snake neurotoxin binding to mammalian acetylcholine receptor by specific antiserum
    • Gatineau, E.; Lee, C.Y.; Fromageot, P.; Menez, A. Reversal of snake neurotoxin binding to mammalian acetylcholine receptor by specific antiserum. Eur. J. Biochem. FEBS 1988, 171, 535-539
    • (1988) Eur. J. Biochem. FEBS , vol.171 , pp. 535-539
    • Gatineau, E.1    Lee, C.Y.2    Fromageot, P.3    Menez, A.4
  • 34
    • 0024044244 scopus 로고
    • Monoclonal antibodies to scorpion toxins. Characterization and molecular mechanisms of neutralization
    • Bahraoui, E.; Pichon, J.; Muller, J.M.; Darbon, H.; Elayeb, M.; Granier, C.; Marvaldi, J.; Rochat, H. Monoclonal antibodies to scorpion toxins. Characterization and molecular mechanisms of neutralization. J. Immunol. 1988, 141, 214-220
    • (1988) J. Immunol , vol.141 , pp. 214-220
    • Bahraoui, E.1    Pichon, J.2    Muller, J.M.3    Darbon, H.4    Elayeb, M.5    Granier, C.6    Marvaldi, J.7    Rochat, H.8
  • 35
    • 0036027994 scopus 로고    scopus 로고
    • Induction of neutralizing antibodies against Tityus serrulatus scorpion toxins by immunization with a mixture of defined synthetic epitopes
    • Alvarenga, L.M.; Diniz, C.R.; Granier, C.; Chávez-Olórtegui, C. Induction of neutralizing antibodies against Tityus serrulatus scorpion toxins by immunization with a mixture of defined synthetic epitopes. Toxicon Off. J. Int. Soc. Toxinol. 2002, 40, 89-95
    • (2002) Toxicon Off. J. Int. Soc. Toxinol , vol.40 , pp. 89-95
    • Alvarenga, L.M.1    Diniz, C.R.2    Granier, C.3    Chávez-Olórtegui, C.4
  • 36
    • 30944449218 scopus 로고    scopus 로고
    • Monoclonal and recombinant antibodies, 30 years after
    • Laffly, E.; Sodoyer, R. Monoclonal and recombinant antibodies, 30 years after .... Hum. Antibodies 2005, 14, 33-55
    • (2005) Hum. Antibodies , vol.14 , pp. 33-55
    • Laffly, E.1    Sodoyer, R.2
  • 37
    • 27144532832 scopus 로고    scopus 로고
    • Human antibodies from transgenic animals
    • Lonberg, N. Human antibodies from transgenic animals. Nat. Biotechnol. 2005, 23, 1117-1125
    • (2005) Nat. Biotechnol , vol.23 , pp. 1117-1125
    • Lonberg, N.1
  • 39
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • Hoogenboom, H.R. Selecting and screening recombinant antibody libraries. Nat. Biotechnol. 2005, 23, 1105-1116
    • (2005) Nat. Biotechnol , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 40
    • 38849132141 scopus 로고    scopus 로고
    • Subtractive single-chain antibody (scFv) phage-display: Tailoring phage-display for high specificity against function-specific conformations of cell membrane molecules
    • Eisenhardt, S.U.; Schwarz, M.; Bassler, N.; Peter, K. Subtractive single-chain antibody (scFv) phage-display: Tailoring phage-display for high specificity against function-specific conformations of cell membrane molecules. Nat. Protoc. 2007, 2, 3063-3073
    • (2007) Nat. Protoc , vol.2 , pp. 3063-3073
    • Eisenhardt, S.U.1    Schwarz, M.2    Bassler, N.3    Peter, K.4
  • 41
    • 60549116209 scopus 로고    scopus 로고
    • A compact phage display human scFv library for selection of antibodies to a wide variety of antigens
    • Pansri, P.; Jaruseranee, N.; Rangnoi, K.; Kristensen, P.; Yamabhai, M. A compact phage display human scFv library for selection of antibodies to a wide variety of antigens. BMC Biotechnol. 2009, 9, 6
    • (2009) BMC Biotechnol , vol.9 , pp. 6
    • Pansri, P.1    Jaruseranee, N.2    Rangnoi, K.3    Kristensen, P.4    Yamabhai, M.5
  • 44
    • 84879371196 scopus 로고    scopus 로고
    • Creation of recombinant antigen-binding molecules derived from hybridomas secreting specific antibodies
    • Fields, C.; O'Connell, D.; Xiao, S.; Lee, G.U.; Billiald, P.; Muzard, J. Creation of recombinant antigen-binding molecules derived from hybridomas secreting specific antibodies. Nat. Protoc. 2013, 8, 1125-1148
    • (2013) Nat. Protoc , vol.8 , pp. 1125-1148
    • Fields, C.1    O'Connell, D.2    Xiao, S.3    Lee, G.U.4    Billiald, P.5    Muzard, J.6
  • 46
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger, P.; Hudson, P.J. Engineered antibody fragments and the rise of single domains. Nat. Biotechnol. 2005, 23, 1126-1136
    • (2005) Nat. Biotechnol , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 48
    • 0027197493 scopus 로고
    • Diabodies: Small bivalent and bispecific antibody fragments
    • Holliger, P.; Prospero, T.; Winter, G. "Diabodies": Small bivalent and bispecific antibody fragments. Proc. Natl. Acad. Sci. USA 1993, 90, 6444-6448
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6444-6448
    • Holliger, P.1    Prospero, T.2    Winter, G.3
  • 49
    • 84884945180 scopus 로고    scopus 로고
    • Engineering of a recombinant trivalent single-chain variable fragment antibody directed against rabies virus glycoprotein G with improved neutralizing potency
    • Turki, I.; Hammami, A.; Kharmachi, H.; Mousli, M. Engineering of a recombinant trivalent single-chain variable fragment antibody directed against rabies virus glycoprotein G with improved neutralizing potency. Mol. Immunol. 2014, 57, 66-73
    • (2014) Mol. Immunol , vol.57 , pp. 66-73
    • Turki, I.1    Hammami, A.2    Kharmachi, H.3    Mousli, M.4
  • 50
    • 79958053952 scopus 로고    scopus 로고
    • A. Biotechnological applications of recombinant single-domain antibody fragments
    • De Marco, A. Biotechnological applications of recombinant single-domain antibody fragments. Microb. Cell Factories 2011, 10, 44
    • (2011) Microb. Cell Factories , vol.10 , pp. 44
    • De, M.1
  • 51
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
    • Ward, E.S.; Güssow, D.; Griffiths, A.D.; Jones, P.T.; Winter, G. Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature 1989, 341, 544-546
    • (1989) Nature , vol.341 , pp. 544-546
    • Ward, E.S.1    Güssow, D.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5
  • 52
    • 84878935042 scopus 로고    scopus 로고
    • Nanobodies: Natural single-domain antibodies
    • Muyldermans, S. Nanobodies: Natural single-domain antibodies. Annu. Rev. Biochem. 2013, 82, 775-797
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 775-797
    • Muyldermans, S.1
  • 53
    • 84934438262 scopus 로고    scopus 로고
    • Overview and discovery of IgNARs and generation of VNARs
    • Clifton, NJ, USA
    • Nuttall, S.D. Overview and discovery of IgNARs and generation of VNARs. Methods Mol. Biol. (Clifton, NJ, USA) 2012, 911, 27-36
    • (2012) Methods Mol. Biol , vol.911 , pp. 27-36
    • Nuttall, S.D.1
  • 54
    • 84857373689 scopus 로고    scopus 로고
    • Production of human antibody fragments binding to melittin and phospholipase A2 in Africanised bee venom: Minimising venom toxicity
    • Funayama, J.C.; Pucca, M.B.; Roncolato, E.C.; Bertolini, T.B.; Campos, L.B.; Barbosa, J.E. Production of human antibody fragments binding to melittin and phospholipase A2 in Africanised bee venom: Minimising venom toxicity. Basic Clin. Pharmacol. Toxicol. 2012, 110, 290-297
    • (2012) Basic Clin. Pharmacol. Toxicol , vol.110 , pp. 290-297
    • Funayama, J.C.1    Pucca, M.B.2    Roncolato, E.C.3    Bertolini, T.B.4    Campos, L.B.5    Barbosa, J.E.6
  • 55
    • 84881036564 scopus 로고    scopus 로고
    • New approaches & technologies of venomics to meet the challenge of human envenoming by snakebites in India
    • Warrell, D.A.; Gutiérrez, J.M.; Calvete, J.J.; Williams, D. New approaches & technologies of venomics to meet the challenge of human envenoming by snakebites in India. Indian J. Med. Res. 2013, 138, 38-59
    • (2013) Indian J. Med. Res , vol.138 , pp. 38-59
    • Warrell, D.A.1    Gutiérrez, J.M.2    Calvete, J.J.3    Williams, D.4
  • 59
    • 0026522064 scopus 로고
    • Neutralization of myotoxic phospholipases A2 from the venom of the snake Bothrops asper by monoclonal antibodies
    • Lomonte, B.; Gutiérrez, J.M.; Ramírez, M.; Díaz, C. Neutralization of myotoxic phospholipases A2 from the venom of the snake Bothrops asper by monoclonal antibodies. Toxicon Off. J. Int. Soc. Toxinol. 1992, 30, 239-245
    • (1992) Toxicon Off. J. Int. Soc. Toxinol , vol.30 , pp. 239-245
    • Lomonte, B.1    Gutiérrez, J.M.2    Ramírez, M.3    Díaz, C.4
  • 60
    • 0019940814 scopus 로고
    • Neurotoxin-specific immunoglobulins accelerate dissociation of the neurotoxin-acetylcholine receptor complex
    • Boulain, J.C.; Ménez, A. Neurotoxin-specific immunoglobulins accelerate dissociation of the neurotoxin-acetylcholine receptor complex. Science 1982, 217, 732-733
    • (1982) Science , vol.217 , pp. 732-733
    • Boulain, J.C.1    Ménez, A.2
  • 61
    • 84901792873 scopus 로고    scopus 로고
    • Immunological profile of antivenoms: Preclinical analysis of the efficacy of a polyspecific antivenom through antivenomics and neutralization assays
    • Gutiérrez, J.M.; Lomonte, B.; Sanz, L.; Calvete, J.J.; Pla, D. Immunological profile of antivenoms: Preclinical analysis of the efficacy of a polyspecific antivenom through antivenomics and neutralization assays. J. Proteomics 2014, 105, 340-350
    • (2014) J. Proteomics , vol.105 , pp. 340-350
    • Gutiérrez, J.M.1    Lomonte, B.2    Sanz, L.3    Calvete, J.J.4    Pla, D.5
  • 62
    • 33644512108 scopus 로고    scopus 로고
    • Neutralisation of venom-induced haemorrhage by IgG from camels and llamas immunised with viper venom and also by endogenous, non-IgG components in camelid sera
    • Harrison, R.A.; Hasson, S.S.; Harmsen, M.; Laing, G.D.; Conrath, K.; Theakston, R.D.G. Neutralisation of venom-induced haemorrhage by IgG from camels and llamas immunised with viper venom and also by endogenous, non-IgG components in camelid sera. Toxicon Off. J. Int. Soc. Toxinol. 2006, 47, 364-368
    • (2006) Toxicon Off. J. Int. Soc. Toxinol , vol.47 , pp. 364-368
    • Harrison, R.A.1    Hasson, S.S.2    Harmsen, M.3    Laing, G.D.4    Conrath, K.5    Theakston, R.D.G.6
  • 63
    • 77955014031 scopus 로고    scopus 로고
    • Analysis of camelid IgG for antivenom development: Immunoreactivity and preclinical neutralisation of venom-induced pathology by IgG subclasses, and the effect of heat treatment
    • Cook, D.A.N.; Samarasekara, C.L.; Wagstaff, S.C.; Kinne, J.; Wernery, U.; Harrison, R.A. Analysis of camelid IgG for antivenom development: Immunoreactivity and preclinical neutralisation of venom-induced pathology by IgG subclasses, and the effect of heat treatment. Toxicon Off. J. Int. Soc. Toxinol. 2010, 56, 596-603
    • (2010) Toxicon Off. J. Int. Soc. Toxinol , vol.56 , pp. 596-603
    • Cook, D.A.N.1    Samarasekara, C.L.2    Wagstaff, S.C.3    Kinne, J.4    Wernery, U.5    Harrison, R.A.6
  • 64
    • 68349108044 scopus 로고    scopus 로고
    • Expression of human recombinant antibody fragments capable of partially inhibiting the phospholypase activity of Crotalus durissus terrificus venom
    • Oliveira, J.G.; Soares, S.G.; Soares, A.M.; Giglio, J.R.; Teixeira, J.E.; Barbosa, J.E. Expression of human recombinant antibody fragments capable of partially inhibiting the phospholypase activity of Crotalus durissus terrificus venom. Basic Clin. Pharmacol. Toxicol. 2009, 105, 84-91
    • (2009) Basic Clin. Pharmacol. Toxicol , vol.105 , pp. 84-91
    • Oliveira, J.G.1    Soares, S.G.2    Soares, A.M.3    Giglio, J.R.4    Teixeira, J.E.5    Barbosa, J.E.6
  • 66
    • 84863841722 scopus 로고    scopus 로고
    • Recognition of Vipera ammodytes meridionalis neurotoxin vipoxin and its components using phage-displayed scFv and polyclonal antivenom sera
    • Stoyanova, V.; Aleksandrov, R.; Lukarska, M.; Duhalov, D.; Atanasov, V.; Petrova, S. Recognition of Vipera ammodytes meridionalis neurotoxin vipoxin and its components using phage-displayed scFv and polyclonal antivenom sera. Toxicon Off. J. Int. Soc. Toxinol. 2012, 60, 802-809
    • (2012) Toxicon Off. J. Int. Soc. Toxinol , vol.60 , pp. 802-809
    • Stoyanova, V.1    Aleksandrov, R.2    Lukarska, M.3    Duhalov, D.4    Atanasov, V.5    Petrova, S.6
  • 67
    • 84877717092 scopus 로고    scopus 로고
    • Human antibody fragments specific for Bothrops jararacussu venom reduce the toxicity of other Bothrops sp. venoms
    • Roncolato, E.C.; Pucca, M.B.; Funayama, J.C.; Bertolini, T.B.; Campos, L.B.; Barbosa, J.E. Human antibody fragments specific for Bothrops jararacussu venom reduce the toxicity of other Bothrops sp. venoms. J. Immunotoxicol. 2013, 10, 160-168
    • (2013) J. Immunotoxicol , vol.10 , pp. 160-168
    • Roncolato, E.C.1    Pucca, M.B.2    Funayama, J.C.3    Bertolini, T.B.4    Campos, L.B.5    Barbosa, J.E.6
  • 68
    • 84864332747 scopus 로고    scopus 로고
    • Humanized-single domain antibodies (VH/VHH) that bound specifically to Naja kaouthia phospholipase A2 and neutralized the enzymatic activity
    • Chavanayarn, C.; Thanongsaksrikul, J.; Thueng-In, K.; Bangphoomi, K.; Sookrung, N.; Chaicumpa, W. Humanized-single domain antibodies (VH/VHH) that bound specifically to Naja kaouthia phospholipase A2 and neutralized the enzymatic activity. Toxins 2012, 4, 554-567
    • (2012) Toxins , vol.4 , pp. 554-567
    • Chavanayarn, C.1    Thanongsaksrikul, J.2    Thueng-In, K.3    Bangphoomi, K.4    Sookrung, N.5    Chaicumpa, W.6
  • 69
    • 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.; Rochat, H. Quantitative variability in the biodistribution and in toxinokinetic studies of the three main alpha toxins from the Androctonus australis hector scorpion venom. Toxicon Off. J. Int. Soc. Toxinol. 2004, 43, 661-669
    • (2004) Toxicon Off. J. Int. Soc. Toxinol , vol.43 , pp. 661-669
    • Devaux, C.1    Jouirou, B.2    Naceur, K.M.3    Clot-Faybesse, O.4    El Ayeb, M.5    Rochat, H.6
  • 70
    • 79960699425 scopus 로고    scopus 로고
    • Isolation and characterization of a human antibody fragment specific for Ts1 toxin from Tityus serrulatus scorpion
    • Amaro, I.; Riaño-Umbarila, L.; Becerril, B.; Possani, L.D. Isolation and characterization of a human antibody fragment specific for Ts1 toxin from Tityus serrulatus scorpion. Immunol. Lett. 2011, 139, 73-79
    • (2011) Immunol. Lett , vol.139 , pp. 73-79
    • Amaro, I.1    Riaño-Umbarila, L.2    Becerril, B.3    Possani, L.D.4
  • 72
    • 84897861139 scopus 로고    scopus 로고
    • Serrumab: A novel human single chain-fragment antibody with multiple scorpion toxin-neutralizing capacities
    • Pucca, M.B.; Cerni, F.A.; Peigneur, S.; Arantes, E.C.; Tytgat, J.; Barbosa, J.E. Serrumab: A novel human single chain-fragment antibody with multiple scorpion toxin-neutralizing capacities. J. Immunotoxicol. 2014, 11, 133-140
    • (2014) J. Immunotoxicol , vol.11 , pp. 133-140
    • Pucca, M.B.1    Cerni, F.A.2    Peigneur, S.3    Arantes, E.C.4    Tytgat, J.5    Barbosa, J.E.6
  • 74
    • 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.; Becerril, B. 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. 2005, 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
  • 76
    • 0036838270 scopus 로고    scopus 로고
    • Functional aspects of co-variant surface charges in an antibody fragment
    • Hugo, N.; Lafont, V.; Beukes, M.; Altschuh, D. Functional aspects of co-variant surface charges in an antibody fragment. Protein Sci. Publ. Protein Soc. 2002, 11, 2697-2705
    • (2002) Protein Sci. Publ. Protein Soc , vol.11 , pp. 2697-2705
    • Hugo, N.1    Lafont, V.2    Beukes, M.3    Altschuh, D.4
  • 80
    • 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.; Billiald, P. A recombinant single-chain antibody fragment that neutralizes toxin II from the venom of the scorpion Androctonus australis hector. FEBS Lett. 1999, 442, 183-188
    • (1999) FEBS Lett , vol.442 , pp. 183-188
    • Mousli, M.1    Devaux, C.2    Rochat, H.3    Goyffon, M.4    Billiald, P.5
  • 81
    • 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.; Billiald, P. 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. FEBS 2001, 268, 694-702
    • (2001) Eur. J. Biochem. FEBS , vol.268 , pp. 694-702
    • Devaux, C.1    Moreau, E.2    Goyffon, M.3    Rochat, H.4    Billiald, P.5
  • 82
    • 0344080623 scopus 로고    scopus 로고
    • Design and evaluation of a diabody to improve protection against a potent scorpion neurotoxin
    • Aubrey, N.; Devaux, C.; Sizaret, P.Y.; Rochat, H.; Goyffon, M.; Billiald, P. Design and evaluation of a diabody to improve protection against a potent scorpion neurotoxin. Cell. Mol. Life Sci. 2003, 60, 617-628
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 617-628
    • Aubrey, N.1    Devaux, C.2    Sizaret, P.Y.3    Rochat, H.4    Goyffon, M.5    Billiald, P.6
  • 83
    • 1642389249 scopus 로고    scopus 로고
    • Engineering of a recombinant Fab from a neutralizing IgG directed against scorpion neurotoxin AahI, and functional evaluation versus other antibody fragments
    • Aubrey, N.; Muzard, J.; Christophe Peter, J.; Rochat, H.; Goyffon, M.; Devaux, C.; Billiald, P. Engineering of a recombinant Fab from a neutralizing IgG directed against scorpion neurotoxin AahI, and functional evaluation versus other antibody fragments. Toxicon Off. J. Int. Soc. Toxinol. 2004, 43, 233-241
    • (2004) Toxicon Off. J. Int. Soc. Toxinol , vol.43 , pp. 233-241
    • Aubrey, N.1    Muzard, J.2    Christophe, P.J.3    Rochat, H.4    Goyffon, M.5    Devaux, C.6    Billiald, P.7
  • 85
    • 84859962399 scopus 로고    scopus 로고
    • Diabody mixture providing full protection against experimental scorpion envenoming with crude Androctonus australis venom
    • Di Tommaso, A.; Juste, M.O.; Martin-Eauclaire, M.-F.; Dimier-Poisson, I.; Billiald, P.; Aubrey, N. Diabody mixture providing full protection against experimental scorpion envenoming with crude Androctonus australis venom. J. Biol. Chem. 2012, 287, 14149-14156
    • (2012) J. Biol. Chem , vol.287 , pp. 14149-14156
    • Di Tommaso, A.1    Juste, M.O.2    Martin-Eauclaire, M.-F.3    Dimier-Poisson, I.4    Billiald, P.5    Aubrey, N.6
  • 86
    • 0035715877 scopus 로고    scopus 로고
    • Single domain camel antibodies: Current status
    • Muyldermans, S. Single domain camel antibodies: Current status. J. Biotechnol. 2001, 74, 277-302
    • (2001) J. Biotechnol , vol.74 , pp. 277-302
    • Muyldermans, S.1
  • 95
    • 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
    • Juárez-González, V.R.; Riaño-Umbarila, L.; Quintero-Hernández, V.; Olamendi-Portugal, T.; Ortiz-León, M.; Ortíz, E.; Possani, L.D.; Becerril, B. 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. 2005, 346, 1287-1297
    • (2005) J. Mol. Biol , vol.346 , pp. 1287-1297
    • Juárez-González, V.R.1    Riaño-Umbarila, L.2    Quintero-Hernández, V.3    Olamendi-Portugal, T.4    Ortiz-León, M.5    Ortíz, E.6    Possani, L.D.7    Becerril, B.8
  • 98
    • 34248170673 scopus 로고    scopus 로고
    • Analyzing the "degree of humanness" of antibody sequences
    • Abhinandan, K.R.; Martin, A.C.R. Analyzing the "degree of humanness" of antibody sequences. J. Mol. Biol. 2007, 369, 852-862
    • (2007) J. Mol. Biol , vol.369 , pp. 852-862
    • Abhinandan, K.R.1    Martin, A.C.R.2
  • 99
    • 0028052724 scopus 로고
    • Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains
    • Parker, K.C.; Bednarek, M.A.; Coligan, J.E. Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains. J. Immunol. (Baltimore, MD, USA) 1950 1994, 152, 163-175
    • (1950) J. Immunol (Baltimore, MD, USA) , vol.152 , pp. 163-175
    • Parker, K.C.1    Bednarek, M.A.2    Coligan, J.E.3
  • 100
    • 77049107081 scopus 로고    scopus 로고
    • Antivenom efficacy or effectiveness: The Australian experience
    • Isbister, G.K. Antivenom efficacy or effectiveness: The Australian experience. Toxicology 2010, 268, 148-154
    • (2010) Toxicology , vol.268 , pp. 148-154
    • Isbister, G.K.1
  • 101
    • 2442460970 scopus 로고    scopus 로고
    • Epidemiological data, clinical admission gradation and biological quantification by ELISA of scorpion envenomations in Algeria: Effect of immunotherapy
    • Hammoudi-Triki, D.; Ferquel, E.; Robbe-Vincent, A.; Bon, C.; Choumet, V.; Laraba-Djebari, F. Epidemiological data, clinical admission gradation and biological quantification by ELISA of scorpion envenomations in Algeria: Effect of immunotherapy. Trans. R. Soc. Trop. Med. Hyg. 2004, 98, 240-250.
    • (2004) Trans. R. Soc. Trop. Med. Hyg , vol.98 , pp. 240-250
    • Hammoudi-Triki, D.1    Ferquel, E.2    Robbe-Vincent, A.3    Bon, C.4    Choumet, V.5    Laraba-Djebari, F.6


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