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Volumn 6, Issue 5, 2011, Pages

Neutralising antibodies against Ricin Toxin

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY RA36; MONOCLONAL ANTIBODY RB13; MONOCLONAL ANTIBODY RB14; MONOCLONAL ANTIBODY RB15; MONOCLONAL ANTIBODY RB24; MONOCLONAL ANTIBODY RB27; MONOCLONAL ANTIBODY RB34; MONOCLONAL ANTIBODY RB37; MONOCLONAL ANTIBODY RB42; MONOCLONAL ANTIBODY RB43; RICIN; RICIN A; RICIN B; UNCLASSIFIED DRUG; LACTOSE; NEUTRALIZING ANTIBODY; PROTEIN SUBUNIT;

EID: 79957476321     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0020166     Document Type: Article
Times cited : (62)

References (37)
  • 2
    • 26044454078 scopus 로고    scopus 로고
    • Medical aspects of toxin weapons
    • Bigalke H, Rummel A, (2005) Medical aspects of toxin weapons. Toxicology 214: 210-220.
    • (2005) Toxicology , vol.214 , pp. 210-220
    • Bigalke, H.1    Rummel, A.2
  • 3
    • 0141829264 scopus 로고    scopus 로고
    • Medical management of biological warfare and bioterrorism: place of the immunoprevention and the immunotherapy
    • Binder P, Attre O, Boutin JP, Cavallo JD, Debord T, et al. (2003) Medical management of biological warfare and bioterrorism: place of the immunoprevention and the immunotherapy. Comp Immunol Microbiol Infect Dis 26: 401-421.
    • (2003) Comp Immunol Microbiol Infect Dis , vol.26 , pp. 401-421
    • Binder, P.1    Attre, O.2    Boutin, J.P.3    Cavallo, J.D.4    Debord, T.5
  • 5
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • Cleveland DW, Fischer SG, Kirschner MW, Laemmli UK, (1977) Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J Biol Chem 252: 1102-1106.
    • (1977) J Biol Chem , vol.252 , pp. 1102-1106
    • Cleveland, D.W.1    Fischer, S.G.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 6
    • 0023182792 scopus 로고
    • Identification and characterization of a monoclonal antibody recognizing a galactose-binding domain of the toxin ricin
    • Colombatti M, Johnson VG, Skopicki HA, Fendley B, Lewis MS, et al. (1987) Identification and characterization of a monoclonal antibody recognizing a galactose-binding domain of the toxin ricin. J Immunol 138: 3339-3344.
    • (1987) J Immunol , vol.138 , pp. 3339-3344
    • Colombatti, M.1    Johnson, V.G.2    Skopicki, H.A.3    Fendley, B.4    Lewis, M.S.5
  • 7
    • 0034212499 scopus 로고    scopus 로고
    • A possible explanation for the discrepancy between ELISA and neutralising antibodies to tetanus toxin
    • Dokmetjian J, Della VC, Lavigne V, de Lujan CM, Manghi MA, (2000) A possible explanation for the discrepancy between ELISA and neutralising antibodies to tetanus toxin. Vaccine 18: 2698-2703.
    • (2000) Vaccine , vol.18 , pp. 2698-2703
    • Dokmetjian, J.1    Della, V.C.2    Lavigne, V.3    de Lujan, C.M.4    Manghi, M.A.5
  • 8
    • 1842787056 scopus 로고    scopus 로고
    • Characterizing high-affinity antigen/antibody complexes by kinetic- and equilibrium-based methods
    • Drake AW, Myszka DG, Klakamp SL, (2004) Characterizing high-affinity antigen/antibody complexes by kinetic- and equilibrium-based methods. Anal Biochem 328: 35-43.
    • (2004) Anal Biochem , vol.328 , pp. 35-43
    • Drake, A.W.1    Myszka, D.G.2    Klakamp, S.L.3
  • 10
    • 0023664263 scopus 로고
    • The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins
    • Endo Y, Mitsui K, Motizuki M, Tsurugi K, (1987) The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins. J Biol Chem 262: 5908-5912.
    • (1987) J Biol Chem , vol.262 , pp. 5908-5912
    • Endo, Y.1    Mitsui, K.2    Motizuki, M.3    Tsurugi, K.4
  • 11
    • 0017990368 scopus 로고
    • Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-sepharose
    • Ey PL, Prowse SJ, Jenkin CR, (1978) Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-sepharose. Immunochemistry 15: 429-436.
    • (1978) Immunochemistry , vol.15 , pp. 429-436
    • Ey, P.L.1    Prowse, S.J.2    Jenkin, C.R.3
  • 12
    • 0030851442 scopus 로고    scopus 로고
    • Clinical recognition and management of patients exposed to biological warfare agents
    • Franz DR, Jahrling PB, Friedlander AM, McClain DJ, Hoover DL, et al. (1997) Clinical recognition and management of patients exposed to biological warfare agents. JAMA 278: 399-411.
    • (1997) JAMA , vol.278 , pp. 399-411
    • Franz, D.R.1    Jahrling, P.B.2    Friedlander, A.M.3    McClain, D.J.4    Hoover, D.L.5
  • 13
    • 0023958458 scopus 로고
    • Screening of monoclonal antibodies using antigens labeled with acetylcholinesterase: application to the peripheral proteins of photosystem 1
    • Grassi J, Frobert Y, Lamourette P, Lagoutte B, (1988) Screening of monoclonal antibodies using antigens labeled with acetylcholinesterase: application to the peripheral proteins of photosystem 1. Anal Biochem 168: 436-450.
    • (1988) Anal Biochem , vol.168 , pp. 436-450
    • Grassi, J.1    Frobert, Y.2    Lamourette, P.3    Lagoutte, B.4
  • 14
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • Karlsson R, Michaelsson A, Mattsson L, (1991) Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J Immunol Methods 145: 229-240.
    • (1991) J Immunol Methods , vol.145 , pp. 229-240
    • Karlsson, R.1    Michaelsson, A.2    Mattsson, L.3
  • 15
    • 0025290784 scopus 로고
    • Production and characterization of monoclonal antibodies against the lethal factor component of Bacillus anthracis lethal toxin
    • Little SF, Leppla SH, Friedlander AM, (1990) Production and characterization of monoclonal antibodies against the lethal factor component of Bacillus anthracis lethal toxin. Infect Immun 58: 1606-1613.
    • (1990) Infect Immun , vol.58 , pp. 1606-1613
    • Little, S.F.1    Leppla, S.H.2    Friedlander, A.M.3
  • 16
    • 28444435513 scopus 로고    scopus 로고
    • Passive protection against anthrax by using a high-affinity antitoxin antibody fragment lacking an Fc region
    • Mabry R, Rani M, Geiger R, Hubbard GB, Carrion R Jr, et al. (2005) Passive protection against anthrax by using a high-affinity antitoxin antibody fragment lacking an Fc region. Infect Immun 73: 8362-8368.
    • (2005) Infect Immun , vol.73 , pp. 8362-8368
    • Mabry, R.1    Rani, M.2    Geiger, R.3    Hubbard, G.B.4    Carrion Jr., R.5
  • 17
    • 2442626550 scopus 로고    scopus 로고
    • Immunological characteristics associated with the protective efficacy of antibodies to ricin
    • Maddaloni M, Cooke C, Wilkinson R, Stout AV, Eng L, et al. (2004) Immunological characteristics associated with the protective efficacy of antibodies to ricin. J Immunol 172: 6221-6228.
    • (2004) J Immunol , vol.172 , pp. 6221-6228
    • Maddaloni, M.1    Cooke, C.2    Wilkinson, R.3    Stout, A.V.4    Eng, L.5
  • 18
    • 33646905629 scopus 로고    scopus 로고
    • Immunoglobulin A antibodies against ricin A and B subunits protect epithelial cells from ricin intoxication
    • Mantis NJ, McGuinness CR, Sonuyi O, Edwards G, Farrant SA, (2006) Immunoglobulin A antibodies against ricin A and B subunits protect epithelial cells from ricin intoxication. Infect Immun 74: 3455-3462.
    • (2006) Infect Immun , vol.74 , pp. 3455-3462
    • Mantis, N.J.1    McGuinness, C.R.2    Sonuyi, O.3    Edwards, G.4    Farrant, S.A.5
  • 19
    • 0035984720 scopus 로고    scopus 로고
    • Protection against anthrax toxin by recombinant antibody fragments correlates with antigen affinity
    • Maynard JA, Maassen CB, Leppla SH, Brasky K, Patterson JL, et al. (2002) Protection against anthrax toxin by recombinant antibody fragments correlates with antigen affinity. Nat Biotechnol 20: 597-601.
    • (2002) Nat Biotechnol , vol.20 , pp. 597-601
    • Maynard, J.A.1    Maassen, C.B.2    Leppla, S.H.3    Brasky, K.4    Patterson, J.L.5
  • 20
    • 33646905060 scopus 로고    scopus 로고
    • Characterization of a novel high-affinity monoclonal immunoglobulin G antibody against the ricin B subunit
    • McGuinness CR, Mantis NJ, (2006) Characterization of a novel high-affinity monoclonal immunoglobulin G antibody against the ricin B subunit. Infect Immun 74: 3463-3470.
    • (2006) Infect Immun , vol.74 , pp. 3463-3470
    • McGuinness, C.R.1    Mantis, N.J.2
  • 21
    • 73449123743 scopus 로고    scopus 로고
    • A monoclonal immunoglobulin G antibody directed against an immunodominant linear epitope on the ricin A chain confers systemic and mucosal immunity to ricin
    • Neal LM, O'Hara J, Brey RN 3rd, Mantis NJ, (2010) A monoclonal immunoglobulin G antibody directed against an immunodominant linear epitope on the ricin A chain confers systemic and mucosal immunity to ricin. Infect Immun 78: 552-61.
    • (2010) Infect Immun , vol.78 , pp. 552-561
    • Neal, L.M.1    O'Hara, J.2    Brey III, R.N.3    Mantis, N.J.4
  • 22
    • 0015951279 scopus 로고
    • Characterization of two plant lectins from Ricinus communis and their quantitative interaction with a murine lymphoma
    • Nicolson GL, Blaustein J, Etzler ME, (1974) Characterization of two plant lectins from Ricinus communis and their quantitative interaction with a murine lymphoma. Biochemistry 13: 196-204.
    • (1974) Biochemistry , vol.13 , pp. 196-204
    • Nicolson, G.L.1    Blaustein, J.2    Etzler, M.E.3
  • 24
    • 77957601374 scopus 로고    scopus 로고
    • Folding domains within the ricin toxin A subunit as targets of protective antibodies
    • O'Hara JM, Neal LM, McCarthy EA, Kasten-Jolly JA, Brey RN 3rd, et al. (2010) Folding domains within the ricin toxin A subunit as targets of protective antibodies. Vaccine 43: 7035-46.
    • (2010) Vaccine , vol.43 , pp. 7035-7046
    • O'Hara, J.M.1    Neal, L.M.2    McCarthy, E.A.3    Kasten-Jolly, J.A.4    Brey III, R.N.5
  • 25
    • 0015781481 scopus 로고
    • Different biological properties of the two constituent peptide chains of ricin, a toxic protein inhibiting protein synthesis
    • Olsnes S, Pihl A, (1973) Different biological properties of the two constituent peptide chains of ricin, a toxic protein inhibiting protein synthesis. Biochemistry 12: 3121-3126.
    • (1973) Biochemistry , vol.12 , pp. 3121-3126
    • Olsnes, S.1    Pihl, A.2
  • 27
    • 0023236381 scopus 로고
    • A simple, non-chromatographic purification procedure for monoclonal antibodies. Isolation of monoclonal antibodies against cytochrome P450 isozymes
    • Reik LM, Maines SL, Ryan DE, Levin W, Bandiera S, et al. (1987) A simple, non-chromatographic purification procedure for monoclonal antibodies. Isolation of monoclonal antibodies against cytochrome P450 isozymes. J Immunol Methods 100: 123-130.
    • (1987) J Immunol Methods , vol.100 , pp. 123-130
    • Reik, L.M.1    Maines, S.L.2    Ryan, D.E.3    Levin, W.4    Bandiera, S.5
  • 28
    • 54949121317 scopus 로고    scopus 로고
    • Post-exposure targeting of specific epitopes on ricin toxin abrogates toxin-induced hypoglycemia, hepatic injury, and lethality in a mouse model
    • Roche JK, Stone MK, Gross LK, Lindner M, Seaner R, et al. (2008) Post-exposure targeting of specific epitopes on ricin toxin abrogates toxin-induced hypoglycemia, hepatic injury, and lethality in a mouse model. Lab Invest 88: 1178-91.
    • (2008) Lab Invest , vol.88 , pp. 1178-1191
    • Roche, J.K.1    Stone, M.K.2    Gross, L.K.3    Lindner, M.4    Seaner, R.5
  • 29
    • 0025939115 scopus 로고
    • Structure of ricin B-chain at 2.5 A resolution
    • Rutenber E, Robertus JD, (1991) Structure of ricin B-chain at 2.5 A resolution. Proteins 10: 260-269.
    • (1991) Proteins , vol.10 , pp. 260-269
    • Rutenber, E.1    Robertus, J.D.2
  • 30
    • 0032998475 scopus 로고    scopus 로고
    • Endocytosis and intracellular transport of ricin: recent discoveries
    • Sandvig K, van Deurs B, (1999) Endocytosis and intracellular transport of ricin: recent discoveries. FEBS Lett 452: 67-70.
    • (1999) FEBS Lett , vol.452 , pp. 67-70
    • Sandvig, K.1    van Deurs, B.2
  • 31
    • 70349429612 scopus 로고    scopus 로고
    • Ricin as a weapon of mass terror--separating fact from fiction
    • Schep LJ, Temple WA, Butt GA, Beasley MD, (2009) Ricin as a weapon of mass terror--separating fact from fiction. Environ Int 35: 1267-1271.
    • (2009) Environ Int , vol.35 , pp. 1267-1271
    • Schep, L.J.1    Temple, W.A.2    Butt, G.A.3    Beasley, M.D.4
  • 32
    • 34748918488 scopus 로고    scopus 로고
    • RiVax, a recombinant ricin subunit vaccine, protects mice against ricin delivered by gavage or aerosol
    • Smallshaw JE, Richardson JA, Vitetta ES, (2007) RiVax, a recombinant ricin subunit vaccine, protects mice against ricin delivered by gavage or aerosol. Vaccine 25: 7459-7469.
    • (2007) Vaccine , vol.25 , pp. 7459-7469
    • Smallshaw, J.E.1    Richardson, J.A.2    Vitetta, E.S.3
  • 33
    • 77951735286 scopus 로고    scopus 로고
    • Inhibition of retrograde transport protects mice from lethal ricin challenge
    • Stechmann B, Bai SK, Gobbo E, Lopez R, Merer G, et al. (2010) Inhibition of retrograde transport protects mice from lethal ricin challenge. Cell 141: 231-242.
    • (2010) Cell , vol.141 , pp. 231-242
    • Stechmann, B.1    Bai, S.K.2    Gobbo, E.3    Lopez, R.4    Merer, G.5
  • 34
    • 0035849504 scopus 로고    scopus 로고
    • Ricin A-chain inhibitors resembling the oxacarbenium ion transition state
    • Tanaka KS, Chen XY, Ichikawa Y, Tyler PC, Furneaux RH, et al. (2001) Ricin A-chain inhibitors resembling the oxacarbenium ion transition state. Biochemistry 40: 6845-6851.
    • (2001) Biochemistry , vol.40 , pp. 6845-6851
    • Tanaka, K.S.1    Chen, X.Y.2    Ichikawa, Y.3    Tyler, P.C.4    Furneaux, R.H.5
  • 37
    • 0031567126 scopus 로고    scopus 로고
    • Structure-based identification of a ricin inhibitor
    • Yan X, Hollis T, Svinth M, Day P, Monzingo AF, et al. (1997) Structure-based identification of a ricin inhibitor. J Mol Biol 266: 1043-1049.
    • (1997) J Mol Biol , vol.266 , pp. 1043-1049
    • Yan, X.1    Hollis, T.2    Svinth, M.3    Day, P.4    Monzingo, A.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.