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Volumn 290, Issue 11, 2015, Pages 6715-6730

Mechanisms mediating enhanced neutralization efficacy of staphylococcal enterotoxin B by combinations of monoclonal antibodies

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; CELL MEMBRANES; EPITOPES; MAPPING; MIXTURES; MONOCLONAL ANTIBODIES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EID: 84924898040     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.630715     Document Type: Article
Times cited : (35)

References (53)
  • 1
    • 0025070203 scopus 로고
    • The toxicity of staphylococcal enterotoxin B in mice is mediated by T cells
    • Marrack, P., Blackman, M., Kushnir, E., and Kappler, J. (1990) The toxicity of staphylococcal enterotoxin B in mice is mediated by T cells. J. Exp. Med. 171, 455-464
    • (1990) J. Exp. Med. , vol.171 , pp. 455-464
    • Marrack, P.1    Blackman, M.2    Kushnir, E.3    Kappler, J.4
  • 2
    • 0027429426 scopus 로고
    • Toxicity of staphylococcal enterotoxins potentiated by lipopolysaccharide: Major histocompatibility complex class II molecule dependency and cytokine release
    • Stiles, B. G., Bavari, S., Krakauer, T., and Ulrich, R. G. (1993) Toxicity of staphylococcal enterotoxins potentiated by lipopolysaccharide: major histocompatibility complex class II molecule dependency and cytokine release. Infect. Immun. 61, 5333-5338
    • (1993) Infect. Immun. , vol.61 , pp. 5333-5338
    • Stiles, B.G.1    Bavari, S.2    Krakauer, T.3    Ulrich, R.G.4
  • 3
    • 79952098979 scopus 로고    scopus 로고
    • Staphylococcal enterotoxins
    • Pinchuk, I. V., Beswick, E. J., and Reyes, V. E. (2010) Staphylococcal enterotoxins. Toxins 2, 2177-2197
    • (2010) Toxins , vol.2 , pp. 2177-2197
    • Pinchuk, I.V.1    Beswick, E.J.2    Reyes, V.E.3
  • 5
    • 0028118361 scopus 로고
    • Neutralizing antibodies and immunoprotection against pertussis and tetanus obtained by use of a recombinant pertussis toxin-tetanus toxin fusion protein
    • Boucher, P., Sato, H., Sato, Y., and Locht, C. (1994) Neutralizing antibodies and immunoprotection against pertussis and tetanus obtained by use of a recombinant pertussis toxin-tetanus toxin fusion protein. Infect. Immun. 62, 449-456
    • (1994) Infect. Immun. , vol.62 , pp. 449-456
    • Boucher, P.1    Sato, H.2    Sato, Y.3    Locht, C.4
  • 6
    • 70249088378 scopus 로고    scopus 로고
    • Neutralization of Bothrops asper venom by antibodies, natural products and synthetic drugs: Contributions to understanding snakebite envenomings and their treatment
    • Lomonte, B., León, G., Angulo, Y., Rucavado, A., and Núñez, V. (2009) Neutralization of Bothrops asper venom by antibodies, natural products and synthetic drugs: contributions to understanding snakebite envenomings and their treatment. Toxicon 54, 1012-1028
    • (2009) Toxicon , vol.54 , pp. 1012-1028
    • Lomonte, B.1    León, G.2    Angulo, Y.3    Rucavado, A.4    Núñez, V.5
  • 8
    • 70349432307 scopus 로고    scopus 로고
    • Antibody protection against botulinum neurotoxin intoxication in mice
    • Cheng, L. W., Stanker, L. H., Henderson, T. D., 2nd, Lou, J., and Marks, J. D. (2009) Antibody protection against botulinum neurotoxin intoxication in mice. Infect. Immun. 77, 4305-4313
    • (2009) Infect. Immun. , vol.77 , pp. 4305-4313
    • Cheng, L.W.1    Stanker, L.H.2    Henderson, T.D.3    Lou, J.4    Marks, J.D.5
  • 12
    • 84865606365 scopus 로고    scopus 로고
    • Potent neutralization of botulinum neurotoxin/B by synergistic action of antibodies recognizing protein and ganglioside receptor binding domain
    • Chen, C., Wang, S., Wang, H., Mao, X., Zhang, T., Ji, G., Shi, X., Xia, T., Lu, W., Zhang, D., Dai, J., and Guo, Y. (2012) Potent neutralization of botulinum neurotoxin/B by synergistic action of antibodies recognizing protein and ganglioside receptor binding domain. PLoS One 7, e43845
    • (2012) PLoS One , vol.7 , pp. e43845
    • Chen, C.1    Wang, S.2    Wang, H.3    Mao, X.4    Zhang, T.5    Ji, G.6    Shi, X.7    Xia, T.8    Lu, W.9    Zhang, D.10    Dai, J.11    Guo, Y.12
  • 15
    • 78149455684 scopus 로고    scopus 로고
    • Inhibition of toxic shock by human monoclonal antibodies against staphylococcal enterotoxin B
    • Larkin, E. A., Stiles, B. G., and Ulrich, R. G. (2010) Inhibition of toxic shock by human monoclonal antibodies against staphylococcal enterotoxin B. PLoS One 5, e13253
    • (2010) PLoS One , vol.5 , pp. e13253
    • Larkin, E.A.1    Stiles, B.G.2    Ulrich, R.G.3
  • 17
    • 79953170197 scopus 로고    scopus 로고
    • Generation, characterization, and epitope mapping of neutralizing and protective monoclonal antibodies against staphylococcal enterotoxin B-induced lethal shock
    • Varshney, A. K., Wang, X., Cook, E., Dutta, K., Scharff, M. D., Goger, M. J., and Fries, B. C. (2011) Generation, characterization, and epitope mapping of neutralizing and protective monoclonal antibodies against staphylococcal enterotoxin B-induced lethal shock. J. Biol. Chem. 286, 9737-9747
    • (2011) J. Biol. Chem. , vol.286 , pp. 9737-9747
    • Varshney, A.K.1    Wang, X.2    Cook, E.3    Dutta, K.4    Scharff, M.D.5    Goger, M.J.6    Fries, B.C.7
  • 19
    • 0028332839 scopus 로고
    • Monoclonal antibodies defining functional sites on the toxin superantigen staphylococcal enterotoxin B
    • Hamad, A. R., Herman, A., Marrack, P., and Kappler, J. W. (1994) Monoclonal antibodies defining functional sites on the toxin superantigen staphylococcal enterotoxin B. J. Exp. Med. 180, 615-621
    • (1994) J. Exp. Med. , vol.180 , pp. 615-621
    • Hamad, A.R.1    Herman, A.2    Marrack, P.3    Kappler, J.W.4
  • 21
    • 0034996241 scopus 로고    scopus 로고
    • MBP fusion protein with a viral protease cleavage site: One-step cleavage/purification of insoluble proteins
    • Alexandrov, A., Dutta, K., and Pascal, S. M. (2001) MBP fusion protein with a viral protease cleavage site: one-step cleavage/purification of insoluble proteins. BioTechniques 30, 1194-1198
    • (2001) BioTechniques , vol.30 , pp. 1194-1198
    • Alexandrov, A.1    Dutta, K.2    Pascal, S.M.3
  • 22
    • 16644376635 scopus 로고    scopus 로고
    • Isolation and culture of murine macrophages
    • Davies, J. Q., and Gordon, S. (2005) Isolation and culture of murine macrophages. Methods Mol. Biol. 290, 91-103
    • (2005) Methods Mol. Biol. , vol.290 , pp. 91-103
    • Davies, J.Q.1    Gordon, S.2
  • 25
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler, M., Schleucher, J., and Griesinger, C. (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. Nucl. Mag. Res. Sp. 34, 93-158
    • (1999) Prog. Nucl. Mag. Res. Sp. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 26
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 27
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson, B. A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278, 313-352
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 28
    • 0000867858 scopus 로고    scopus 로고
    • Single transition-to-single transition polarization transfer (ST2-PT) in [15N,1H]-TROSY
    • Pervushin, K. V., Wider, G., and Wüthrich, K. (1998) Single transition-to-single transition polarization transfer (ST2-PT) in [15N,1H]-TROSY. J. Biomol. NMR 12, 345-348
    • (1998) J. Biomol. NMR , vol.12 , pp. 345-348
    • Pervushin, K.V.1    Wider, G.2    Wüthrich, K.3
  • 29
    • 0033609011 scopus 로고    scopus 로고
    • Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules
    • Riek, R., Wider, G., Pervushin, K., and Wüthrich, K. (1999) Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules. Proc. Natl. Acad. Sci. U.S.A. 96, 4918-4923
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4918-4923
    • Riek, R.1    Wider, G.2    Pervushin, K.3    Wüthrich, K.4
  • 30
    • 0032549518 scopus 로고    scopus 로고
    • Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 A resolution: Implications for superantigen recognition by MHC class II molecules and T-cell receptors
    • Papageorgiou, A. C., Tranter, H. S., and Acharya, K. R. (1998) Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors. J. Mol. Biol. 277, 61-79
    • (1998) J. Mol. Biol. , vol.277 , pp. 61-79
    • Papageorgiou, A.C.1    Tranter, H.S.2    Acharya, K.R.3
  • 31
    • 0032412391 scopus 로고    scopus 로고
    • Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B
    • Li, H., Llera, A., Tsuchiya, D., Leder, L., Ysern, X., Schlievert, P. M., Karjalainen, K., and Mariuzza, R. A. (1998) Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B. Immunity 9, 807-816
    • (1998) Immunity , vol.9 , pp. 807-816
    • Li, H.1    Llera, A.2    Tsuchiya, D.3    Leder, L.4    Ysern, X.5    Schlievert, P.M.6    Karjalainen, K.7    Mariuzza, R.A.8
  • 33
  • 35
    • 84892565858 scopus 로고    scopus 로고
    • Structural basis for the neutralization and specificity of Staphylococcal enterotoxin B against its MHC Class II binding site
    • Xia, T., Liang, S., Wang, H., Hu, S., Sun, Y., Yu, X., Han, J., Li, J., Guo, S., Dai, J., Lou, Z., and Guo, Y. (2014) Structural basis for the neutralization and specificity of Staphylococcal enterotoxin B against its MHC Class II binding site. mAbs 6, 119-129
    • (2014) mAbs , vol.6 , pp. 119-129
    • Xia, T.1    Liang, S.2    Wang, H.3    Hu, S.4    Sun, Y.5    Yu, X.6    Han, J.7    Li, J.8    Guo, S.9    Dai, J.10    Lou, Z.11    Guo, Y.12
  • 37
    • 67650096429 scopus 로고    scopus 로고
    • Monoclonal antibody 11E10, which neutralizes shiga toxin type 2 (Stx2), recognizes three regions on the Stx2 A subunit, blocks the enzymatic action of the toxin in vitro, and alters the overall cellular distribution of the toxin
    • Smith, M. J., Melton-Celsa, A. R., Sinclair, J. F., Carvalho, H. M., Robinson, C. M., and O'Brien, A. D. (2009) Monoclonal antibody 11E10, which neutralizes shiga toxin type 2 (Stx2), recognizes three regions on the Stx2 A subunit, blocks the enzymatic action of the toxin in vitro, and alters the overall cellular distribution of the toxin. Infect. Immun. 77, 2730-2740
    • (2009) Infect. Immun. , vol.77 , pp. 2730-2740
    • Smith, M.J.1    Melton-Celsa, A.R.2    Sinclair, J.F.3    Carvalho, H.M.4    Robinson, C.M.5    O'Brien, A.D.6
  • 38
    • 84881552466 scopus 로고    scopus 로고
    • Neutralizing monoclonal antibodies against ricin's enzymatic subunit interfere with protein disulfide isomerase-mediated reduction of ricin holotoxin in vitro
    • O'Hara, J. M., and Mantis, N. J. (2013) Neutralizing monoclonal antibodies against ricin's enzymatic subunit interfere with protein disulfide isomerase-mediated reduction of ricin holotoxin in vitro. J. Immunol. Methods 395, 71-78
    • (2013) J. Immunol. Methods , vol.395 , pp. 71-78
    • O'Hara, J.M.1    Mantis, N.J.2
  • 39
    • 84899829096 scopus 로고    scopus 로고
    • Antibody-mediated inhibition of ricin toxin retrograde transport
    • Yermakova, A., Klokk, T. I., Cole, R., Sandvig, K., and Mantis, N. J. (2014) Antibody-mediated inhibition of ricin toxin retrograde transport. mBio 5, e00995
    • (2014) mBio , vol.5 , pp. e00995
    • Yermakova, A.1    Klokk, T.I.2    Cole, R.3    Sandvig, K.4    Mantis, N.J.5
  • 40
    • 33745395593 scopus 로고    scopus 로고
    • EDEM is involved in retrotranslocation of ricin from the endoplasmic reticulum to the cytosol
    • Slominska-Wojewodzka, M., Gregers, T. F., Wälchli, S., and Sandvig, K. (2006) EDEM is involved in retrotranslocation of ricin from the endoplasmic reticulum to the cytosol. Mol. Biol. Cell 17, 1664-1675
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1664-1675
    • Slominska-Wojewodzka, M.1    Gregers, T.F.2    Wälchli, S.3    Sandvig, K.4
  • 42
    • 84903956909 scopus 로고    scopus 로고
    • Isotype switching increases efficacy of antibody protection against staphylococcal enterotoxin B-induced lethal shock and Staphylococcus aureus sepsis in mice
    • Varshney, A. K., Wang, X., Aguilar, J. L., Scharff, M. D., and Fries, B. C. (2014) Isotype switching increases efficacy of antibody protection against staphylococcal enterotoxin B-induced lethal shock and Staphylococcus aureus sepsis in mice. mBio 5, e01007-e01014
    • (2014) mBio , vol.5 , pp. e01007-e01014
    • Varshney, A.K.1    Wang, X.2    Aguilar, J.L.3    Scharff, M.D.4    Fries, B.C.5
  • 44
    • 76749160798 scopus 로고    scopus 로고
    • Efficient serum clearance of botulinum neurotoxin achieved using a pool of small antitoxin binding agents
    • Sepulveda, J., Mukherjee, J., Tzipori, S., Simpson, L. L., and Shoemaker, C. B. (2010) Efficient serum clearance of botulinum neurotoxin achieved using a pool of small antitoxin binding agents. Infect. Immun. 78, 756-763
    • (2010) Infect. Immun. , vol.78 , pp. 756-763
    • Sepulveda, J.1    Mukherjee, J.2    Tzipori, S.3    Simpson, L.L.4    Shoemaker, C.B.5
  • 45
    • 71049189254 scopus 로고    scopus 로고
    • Unraveling the allosteric mechanism of serine protease inhibition by an antibody
    • Ganesan, R., Eigenbrot, C., Wu, Y., Liang, W. C., Shia, S., Lipari, M. T., and Kirchhofer, D. (2009) Unraveling the allosteric mechanism of serine protease inhibition by an antibody. Structure 17, 1614-1624
    • (2009) Structure , vol.17 , pp. 1614-1624
    • Ganesan, R.1    Eigenbrot, C.2    Wu, Y.3    Liang, W.C.4    Shia, S.5    Lipari, M.T.6    Kirchhofer, D.7
  • 47
    • 4644358187 scopus 로고    scopus 로고
    • Anantibody specific for coagulation factor IX enhances the activity of the intrinsic factor X-activating complex
    • Kerschbaumer, R. J., Riedrich, K., Kral, M., Varadi, K., Dorner, F., Rosing, J., and Scheiflinger, F. (2004)Anantibody specific for coagulation factor IX enhances the activity of the intrinsic factor X-activating complex. J. Biol. Chem. 279, 40445-40450
    • (2004) J. Biol. Chem. , vol.279 , pp. 40445-40450
    • Kerschbaumer, R.J.1    Riedrich, K.2    Kral, M.3    Varadi, K.4    Dorner, F.5    Rosing, J.6    Scheiflinger, F.7
  • 48
    • 0030607253 scopus 로고    scopus 로고
    • Protein D2 porin of the Pseudomonas aeruginosa outer membrane bears the protease activity
    • Yoshihara, E., Gotoh, N., Nishino, T., and Nakae, T. (1996) Protein D2 porin of the Pseudomonas aeruginosa outer membrane bears the protease activity. FEBS Lett. 394, 179-182
    • (1996) FEBS Lett. , vol.394 , pp. 179-182
    • Yoshihara, E.1    Gotoh, N.2    Nishino, T.3    Nakae, T.4
  • 50
    • 0027208757 scopus 로고
    • Anovel superantigen isolated from pathogenic strains of Streptococcus pyogenes with aminoterminal homology to staphylococcal enterotoxins B and C
    • Mollick, J. A., Miller, G. G., Musser, J. M., Cook, R. G., Grossman, D., and Rich, R. R. (1993)Anovel superantigen isolated from pathogenic strains of Streptococcus pyogenes with aminoterminal homology to staphylococcal enterotoxins B and C. J. Clin. Invest. 92, 710-719
    • (1993) J. Clin. Invest. , vol.92 , pp. 710-719
    • Mollick, J.A.1    Miller, G.G.2    Musser, J.M.3    Cook, R.G.4    Grossman, D.5    Rich, R.R.6
  • 53
    • 84907344754 scopus 로고    scopus 로고
    • Humanized staphylococcal enterotoxin B (SEB)-specific monoclonal antibodies protect from SEB intoxication and Staphylococcus aureus infections alone or as adjunctive therapy with vancomycin
    • Varshney, A. K., Wang, X., MacIntyre, J., Zollner, R. S., Kelleher, K., Kovalenko, O. V., Pechuan, X., Byrne, F. R., and Fries, B. C. (2014) Humanized staphylococcal enterotoxin B (SEB)-specific monoclonal antibodies protect from SEB intoxication and Staphylococcus aureus infections alone or as adjunctive therapy with vancomycin. J. Infect. Dis. 210, 973-981
    • (2014) J. Infect. Dis. , vol.210 , pp. 973-981
    • Varshney, A.K.1    Wang, X.2    MacIntyre, J.3    Zollner, R.S.4    Kelleher, K.5    Kovalenko, O.V.6    Pechuan, X.7    Byrne, F.R.8    Fries, B.C.9


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