메뉴 건너뛰기




Volumn 524, Issue , 2009, Pages 87-101

Epitope mapping by proteolysis of antigen-antibody complexes

Author keywords

Antibody; Antigen; Epitope excision and extraction; Epitope foot printing; Epitope mapping; ESI MS; Limited proteolysis; Linear epitope; MALDI MS; Mass spectrometry

Indexed keywords

EPITOPE; IMMOBILIZED ANTIBODY; PEPTIDE HYDROLASE;

EID: 67650221877     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-450-6_7     Document Type: Article
Times cited : (17)

References (35)
  • 1
    • 0003536924 scopus 로고    scopus 로고
    • W.H. Freeman and Co., New York, NY
    • Kuby, J. (ed.) (1997) Immunology. W.H. Freeman and Co., New York, NY.
    • (1997) Immunology
    • Kuby, J.1
  • 2
    • 27144541763 scopus 로고    scopus 로고
    • Determination of protein-derived epitopes by mass spectrometry
    • DOI 10.1586/14789450.2.5.745
    • Hager-Braun, C., and Tomer, K. B. (2005) Determination of protein-derived epitopes by mass spectrometry. Expert Rev. Proteomics 2, 745-756. (Pubitemid 41492395)
    • (2005) Expert Review of Proteomics , vol.2 , Issue.5 , pp. 745-756
    • Hager-Braun, C.1    Tomer, K.B.2
  • 3
    • 0025351555 scopus 로고
    • Epitopes on protein antigens: Misconceptions and realities
    • Laver, W. G., Air, G. M., Webster, R. G., and Smithgill, S. J. (1990) Epitopes on protein antigens: misconceptions and realities. Cell 61, 553-556.
    • (1990) Cell , vol.61 , pp. 553-556
    • Laver, W.G.1    Air, G.M.2    Webster, R.G.3    Smithgill, S.J.4
  • 5
    • 30144437826 scopus 로고    scopus 로고
    • Characterization of the neutralizing activity of three anti-human TNF monoclonal antibodies and prediction of their TNF epitopes by molecular modeling and mutant protein approach
    • DOI 10.1016/j.imlet.2005.09.002, PII S0165247805002762
    • Zhu, C. S., Liu, X. S., Feng, J. N., Zhang, W., Shen, B. F., Ou'yang, W., Cao, Y. X., and Jin, B. Q. (2006) Characterization of the neutralizing activity of three anti-human TNF monoclonal antibodies and prediction of their TNF epitopes by molecular modeling and mutant protein approach. Immunol. Lett. 102, 177-183. (Pubitemid 43053087)
    • (2006) Immunology Letters , vol.102 , Issue.2 , pp. 177-183
    • Zhu, C.1    Liu, X.2    Feng, J.3    Zhang, W.4    Shen, B.5    Ou'yang, W.6    Cao, Y.7    Jin, B.8
  • 6
    • 33845984040 scopus 로고    scopus 로고
    • Antibody recognition of a flexible epitope at the DNA binding site of the human papillomaviras transcriptional regulator E2
    • DOI 10.1021/bi0615184
    • Cerutti, M. L., Ferreiro, D. U., Sanguineti, S., Goldbaum, F. A., and de Prat-Gay, G. (2006) Antibody recognition of a flexible epitope at the DNA binding site of the human papillomavirus transcriptional regulator E2. Biochemistry 45, 15520-15528. (Pubitemid 46043110)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15520-15528
    • Cerutti, M.L.1    Ferreiro, D.U.2    Sanguineti, S.3    Goldbaum, F.A.4    De Prat-Gay, G.5
  • 9
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • DOI 10.1016/0161-5890(94)90001-9
    • Padlan, E. A. (1994) Anatomy of the antibody molecule. Mol. Immunol. 31, 169-217. (Pubitemid 24071681)
    • (1994) Molecular Immunology , vol.31 , Issue.3 , pp. 169-217
    • Padlan, E.A.1
  • 10
    • 0028798104 scopus 로고
    • Identification of specificity-determining residues in antibodies
    • Padlan, E. A., Abergel, C., and Tipper, J. P. (1995) Identification of specificity-determining residues in antibodies. FASEB J. 9, 133-139.
    • (1995) FASEB J. , vol.9 , pp. 133-139
    • Padlan, E.A.1    Abergel, C.2    Tipper, J.P.3
  • 11
    • 0028304866 scopus 로고
    • Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2
    • Tormo, J., Blaas, D., Parry, N. R., Rowlands, D., Stuart, D., and Fita, I. (1994) Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2. EMBO J. 13, 2247-2256. (Pubitemid 24157598)
    • (1994) EMBO Journal , vol.13 , Issue.10 , pp. 2247-2256
    • Tormo, J.1    Blaas, D.2    Parry, N.R.3    Rowlands, D.4    Stuart, D.5    Fita, I.6
  • 12
    • 33744937069 scopus 로고    scopus 로고
    • The HIV-neutralizing monoclonal antibody 4E10 recognizes N-terminal sequences on the native antigen
    • Hager-Braun, C., Katinger, H., and Tomer, K. B. (2006) The HIV-neutralizing monoclonal antibody 4E10 recognizes N-terminal sequences on the native antigen. J. Immunol. 176, 7471-7481. (Pubitemid 43849050)
    • (2006) Journal of Immunology , vol.176 , Issue.12 , pp. 7471-7481
    • Hager-Braun, C.1    Katinger, H.2    Tomer, K.B.3
  • 13
    • 0028004403 scopus 로고
    • Epitope mapping of the gastrin-releasing peptide/anti-bombesin monoclonal antibody complex by proteolysis followed by matrix-assisted laser desorption ionization mass spectrometry
    • Papac, D. I., Hoyes, J., and Tomer, K. B. (1994) Epitope mapping of the gastrinreleasing peptide/antibombesin monoclonal antibody complex by proteolysis followed by matrix-assisted laser desorption ionization mass spectrometry. Protein Sci. 3, 1485-1492. (Pubitemid 24314467)
    • (1994) Protein Science , vol.3 , Issue.9 , pp. 1485-1492
    • Papac, D.I.1    Hoyes, J.2    Tomer, K.B.3
  • 14
    • 0029898211 scopus 로고    scopus 로고
    • Epitope mapping by mass spectrometry: Determination of an epitope on HIV-1 IIIB p26 recognized by a monoclonal antibody
    • Parker, C. E., Papac, D. I., Trojak, S. K., and Tomer, K. B. (1996) Epitope mapping by mass spectrometry: determination of an epitope on HIV-1 IIIB p26 recognized by a monoclonal antibody. J. Immunol. 157, 198-206.
    • (1996) J. Immunol. , vol.157 , pp. 198-206
    • Parker, C.E.1    Papac, D.I.2    Trojak, S.K.3    Tomer, K.B.4
  • 16
    • 0035880528 scopus 로고    scopus 로고
    • A general strategy for epitope mapping by direct MALDI-TOF mass spectrometry using secondary antibodies and cross-linking
    • DOI 10.1021/ac010258n
    • Peter, J. F., and Tomer, K. B. (2001) A general strategy for epitope mapping by direct MALDI-TOF mass spectrometry using secondary antibodies and cross-linking. Anal. Chem. 73, 4012-4019. (Pubitemid 32896179)
    • (2001) Analytical Chemistry , vol.73 , Issue.16 , pp. 4012-4019
    • Peter, J.F.1    Tomer, K.B.2
  • 17
    • 0035283133 scopus 로고    scopus 로고
    • The use of post-source decay in matrix-assisted laser desorption/ionisation mass spectrometry to delineate T cell determinants
    • DOI 10.1016/S0022-1759(00)00361-6, PII S0022175900003616
    • Purcell, A. W., and Gorman, J. J. (2001) The use of post-source decay in matrix-assisted laser desorption/ionisation mass spectrometry to delineate T cell determinants. J. Immunol. Methods 249, 17-31. (Pubitemid 32171955)
    • (2001) Journal of Immunological Methods , vol.249 , Issue.1-2 , pp. 17-31
    • Purcell, A.W.1    Gorman, J.J.2
  • 18
    • 2642578228 scopus 로고    scopus 로고
    • Immunoproteomics: Mass spectrometry-based methods to study the targets of the immune response
    • DOI 10.1074/mcp.R300013-MCP200
    • Purcell, A. W., and Gorman, J. J. (2004) Immunoproteomics: mass spectrometry-based methods to study the targets of the immune response. Mol. Cell Proteomics 3, 193-208. (Pubitemid 38714276)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.3 , pp. 193-208
    • Purcell, A.W.1    Gorman, J.J.2
  • 19
    • 0038617573 scopus 로고    scopus 로고
    • Dissecting the role of peptides in the immune response: Theory, practice and the application to vaccine design
    • DOI 10.1002/psc.456
    • Purcell, A. W., Zeng, W. G., Mifsud, N. A., Ely, L. K., MacDonald, W. A., and Jackson, D. C. (2003) Dissecting the role of peptides in the immune response: theory, practice and the application to vaccine design. J. Pept. Sci. 9, 255-281. (Pubitemid 36665524)
    • (2003) Journal of Peptide Science , vol.9 , Issue.5 , pp. 255-281
    • Purcell, A.W.1    Zeng, W.2    Mifsud, N.A.3    Ely, L.K.4    Macdonald, W.A.5    Jackson, D.C.6
  • 20
    • 0027275583 scopus 로고
    • Two-dimensional NMR investigations of the interactions of antibodies with peptide antigens
    • Anglister, J., Scherf, T., Zilber, B., Levy, R., Zvi, A., Hiller, R., and Feigelson, D. (1993) Two-dimensional NMR investigations of the interactions of antibodies with peptide antigens. FASEB J. 7, 1154-1162. (Pubitemid 23271035)
    • (1993) FASEB Journal , vol.7 , Issue.12 , pp. 1154-1162
    • Anglister, J.1    Scherf, T.2    Zilber, B.3    Levy, R.4    Zvi, A.5    Hiller, R.6    Feigelson, D.7
  • 21
    • 0027336415 scopus 로고
    • A T(1p)-filtered two-dimensional transferred NOE spectrum for studying antibody interactions with peptide antigens
    • Scherf, T., and Anglister, J. (1993) A T1 rho-filtered two-dimensional transferred NOE spectrum for studying antibody interactions with peptide antigens. Biophys. J. 64, 754-761. (Pubitemid 23130342)
    • (1993) Biophysical Journal , vol.64 , Issue.3 , pp. 754-761
    • Scherf, T.1    Anglister, J.2
  • 22
    • 0034429848 scopus 로고    scopus 로고
    • Solid supports in enzyme-linked immunosorbent assay and other solid-phase immunoassays
    • DOI 10.1006/meth.2000.1031
    • Butler, J. E. (2000) Solid supports in enzymelinked immunosorbent assay and other solidphase immunoassays. Methods 22, 4-23. (Pubitemid 32896726)
    • (2000) Methods , vol.22 , Issue.1 , pp. 4-23
    • Butler, J.E.1
  • 23
    • 0034431122 scopus 로고    scopus 로고
    • Surface plasmon resonance-based immunoassays
    • DOI 10.1006/meth.2000.1039
    • Mullett, W. M., Lai, E. P. C., and Yeung, J. M. (2000) Surface plasmon resonance-based immunoassays. Methods 22, 77-91. (Pubitemid 32896734)
    • (2000) Methods , vol.22 , Issue.1 , pp. 77-91
    • Mullett, W.M.1    Lai, E.P.C.2    Yeung, J.M.3
  • 24
    • 0346494733 scopus 로고    scopus 로고
    • Epitope identification and discovery using phage display libraries: Applications in vaccine development and diagnostics
    • Wang, L. F., and Yu, M. (2004) Epitope identification and discovery using phage display libraries: applications in vaccine development and diagnostics. Curr. Drug Targets 5, 1-15. (Pubitemid 38081739)
    • (2004) Current Drug Targets , vol.5 , Issue.1 , pp. 1-15
    • Wang, L.-F.1    Yu, M.2
  • 25
    • 33750987942 scopus 로고    scopus 로고
    • + T Cell Inhibiting Antibodies as Determined by Limited Proteolysis, Chemical Modification, and Mass Spectrometry
    • DOI 10.1016/j.jasms.2006.06.011, PII S1044030506005770
    • Williams, J. G., Tomer, K. B., Hioe, C. E., Zolla-Pazner, S., and Norris, P. J. (2006) The antigenic determinants on HIV p24 for CD4 + T cell inhibiting antibodies as determined by limited proteolysis, chemical modification, and mass spectrometry. J. Am. Soc. Mass Spectrom. 17, 1560-1569. (Pubitemid 44740400)
    • (2006) Journal of the American Society for Mass Spectrometry , vol.17 , Issue.11 , pp. 1560-1569
    • Williams, J.G.1    Tomer, K.B.2    Hioe, C.E.3    Zolla-Pazner, S.4    Norris, P.J.5
  • 26
    • 0024510297 scopus 로고
    • Affinity consideration in the design of synthetic vaccines intended to elicit antibodies
    • DOI 10.1016/0161-5890(89)90084-9
    • Jemmerson, R., and Blankenfeld, R. (1989) Affinity consideration in the design of synthetic vaccines intended to elicit antibodies. Mol. Immunol. 26, 301-307. (Pubitemid 19082783)
    • (1989) Molecular Immunology , vol.26 , Issue.3 , pp. 301-307
    • Jemmerson, R.1    Blankenfeld, R.2
  • 27
    • 0021042615 scopus 로고
    • On the fragmentation of monoclonal IgG1, IgG2a, and IgG2b from BALB/c mice
    • Parham, P. (1983) On the fragmentation of monoclonal IgG1, IgG2a, and IgG2b from BALB/c mice. J. Immunol. 131, 2895-2902. (Pubitemid 14208140)
    • (1983) Journal of Immunology , vol.131 , Issue.6 , pp. 2895-2902
    • Parham, P.1
  • 28
    • 0033533379 scopus 로고    scopus 로고
    • Characterization of the noncovalent complex of human immunodeficiency virus glycoprotein 120 with its cellular receptor CD4 by matrix-assisted laser desorption/ionization mass spectrometry
    • Borchers, C., and Tomer, K. B. (1999) Characterization of the noncovalent complex of human immunodeficiency virus glycoprotein 120 with its cellular receptor CD4 by matrix-assisted laser desorption/ionization mass spectrometry. Biochemistry 38, 11734-11740.
    • (1999) Biochemistry , vol.38 , pp. 11734-11740
    • Borchers, C.1    Tomer, K.B.2
  • 29
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., and Whitehouse, C. M. (1989) Electrospray ionization for mass spectrometry of large biomolecules. Science 246, 64-71. (Pubitemid 19252085)
    • (1989) Science , vol.246 , Issue.4926 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 30
    • 0034716184 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry: A technology for studying noncovalent macromolecular complexes
    • DOI 10.1016/S1387-3806(00)00298-0, PII S1387380600002980
    • Loo, J. A. (2000) Electrospray ionization mass spectrometry: a technology for studying noncovalent macromolecular complexes. Int. J. Mass Spectrom. 200, 175-186. (Pubitemid 32015921)
    • (2000) International Journal of Mass Spectrometry , vol.200 , Issue.1-3 , pp. 175-186
    • Loo, J.A.1
  • 31
    • 0036913741 scopus 로고    scopus 로고
    • Protein complexes gain momentum
    • DOI 10.1016/S0959-440X(02)00400-1
    • Sobott, F., and Robinson, C. V. (2002) Protein complexes gain momentum. Curr. Opin. Struct. Biol. 12, 729-734. (Pubitemid 36009488)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.6 , pp. 729-734
    • Sobott, F.1    Robinson, C.V.2
  • 32
    • 0042318496 scopus 로고    scopus 로고
    • The origin of macromolecule ionization by laser irradiation
    • Tanaka, K. (2003) The origin of macromolecule ionization by laser irradiation. Angew. Chem. Int. Edit. 42, 3860-3870.
    • (2003) Angew. Chem. Int. Edit. , vol.42 , pp. 3860-3870
    • Tanaka, K.1
  • 34
    • 3543072396 scopus 로고    scopus 로고
    • "Affinity-proteomics": Direct protein identification from biological material using mass spectrometric epitope mapping
    • DOI 10.1007/s00216-003-2159-8
    • Macht, M., Marquardt, A., Deininger, S. O., Damoc, E., Kohlmann, M., and Przybylski, M. (2004) "Affinity-proteomics": direct protein identification from biological material using mass spectrometric epitope mapping. Anal. Bioanal. Chem. 378, 1102-1111. (Pubitemid 40890224)
    • (2004) Analytical and Bioanalytical Chemistry , vol.378 , Issue.4 , pp. 1102-1111
    • MacHt, M.1    Marquardt, A.2    Deininger, S.-O.3    Damoc, E.4    Kohlmann, M.5    Przybylski, M.6
  • 35
    • 0026625689 scopus 로고
    • Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping
    • Suckau, D., Mak, M., and Przybylski, M. (1992) Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping. Proc. Natl. Acad. Sci. USA 89, 5630-5634.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5630-5634
    • Suckau, D.1    Mak, M.2    Przybylski, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.