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Volumn 15, Issue 16, 2015, Pages 2756-2765

Lysine conjugation properties in human IgGs studied by integrating high-resolution native mass spectrometry and bottom-up proteomics

Author keywords

Antibody drug conjugates; Covalent chemical labeling; IgGs; Lysine conjugation; Native mass spectrometry; Technology

Indexed keywords

IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1; LYSINE; N HYDROXYSUCCINIMIDE; ANTIBODY CONJUGATE;

EID: 84938750181     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400462     Document Type: Article
Times cited : (40)

References (39)
  • 1
    • 84877310777 scopus 로고    scopus 로고
    • Maturing antibody-drug conjugate pipeline hits 30
    • Mullard, A., Maturing antibody-drug conjugate pipeline hits 30. Nat. Rev. Drug Discov. 2013, 12, 329-332.
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 329-332
    • Mullard, A.1
  • 2
    • 84892621213 scopus 로고    scopus 로고
    • Antibody-drug conjugates: present and future
    • Beck, A., Reichert, J. M., Antibody-drug conjugates: present and future. MAbs 2014, 6, 15-17.
    • (2014) MAbs , vol.6 , pp. 15-17
    • Beck, A.1    Reichert, J.M.2
  • 3
    • 84862690092 scopus 로고    scopus 로고
    • Antibody-drug conjugates: basic concepts, examples and future perspectives
    • Casi, G., Neri, D., Antibody-drug conjugates: basic concepts, examples and future perspectives. J. Control Release. 2012, 161, 422-428.
    • (2012) J. Control Release. , vol.161 , pp. 422-428
    • Casi, G.1    Neri, D.2
  • 4
    • 80054098573 scopus 로고    scopus 로고
    • Antibody conjugate therapeutics: challenges and potential
    • Teicher, B. A., Chari, R. V., Antibody conjugate therapeutics: challenges and potential. Clin. Cancer Res. 2011, 17, 6389-6397.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 6389-6397
    • Teicher, B.A.1    Chari, R.V.2
  • 5
    • 85136070741 scopus 로고    scopus 로고
    • Antibody drug conjugates as cancer therapeutics
    • Trail, P., Antibody drug conjugates as cancer therapeutics. Antibodies 2013, 2, 113-129.
    • (2013) Antibodies , vol.2 , pp. 113-129
    • Trail, P.1
  • 6
    • 34548694517 scopus 로고    scopus 로고
    • Anti-inflammatory activity of human IgG4 antibodies by dynamic Fab arm exchange
    • van der Neut Kolfschoten, M., Schuurman, J., Losen, M., Bleeker, W. K. et al., Anti-inflammatory activity of human IgG4 antibodies by dynamic Fab arm exchange. Science 2007, 317, 1554-1557.
    • (2007) Science , vol.317 , pp. 1554-1557
    • van der Neut Kolfschoten, M.1    Schuurman, J.2    Losen, M.3    Bleeker, W.K.4
  • 7
    • 80052460847 scopus 로고    scopus 로고
    • Quantitative analysis of the interaction strength and dynamics of human IgG4 half molecules by native mass spectrometry
    • Rose, R. J., Labrijn, A. F., van den Bremer, E. T. J., Loverix, S. et al., Quantitative analysis of the interaction strength and dynamics of human IgG4 half molecules by native mass spectrometry. Structure 2011, 19, 1274-1282.
    • (2011) Structure , vol.19 , pp. 1274-1282
    • Rose, R.J.1    Labrijn, A.F.2    van den Bremer, E.T.J.3    Loverix, S.4
  • 8
    • 68449083226 scopus 로고    scopus 로고
    • Therapeutic IgG4 antibodies engage in Fab-arm exchange with endogenous human IgG4 in vivo
    • Labrijn, A. F., Buijsse, A. O., van den Bremer, E. T. J., Verwilligen, A. Y. W. et al., Therapeutic IgG4 antibodies engage in Fab-arm exchange with endogenous human IgG4 in vivo. Nat. Biotechnol. 2009, 27, 767-771.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 767-771
    • Labrijn, A.F.1    Buijsse, A.O.2    van den Bremer, E.T.J.3    Verwilligen, A.Y.W.4
  • 9
    • 74949107560 scopus 로고    scopus 로고
    • Antibody-drug conjugates: linking cytotoxic payloads to monoclonal antibodies
    • Ducry, L., Stump, B., Antibody-drug conjugates: linking cytotoxic payloads to monoclonal antibodies. Bioconjug. Chem. 2010, 21, 5-13.
    • (2010) Bioconjug. Chem. , vol.21 , pp. 5-13
    • Ducry, L.1    Stump, B.2
  • 10
  • 11
    • 84892621003 scopus 로고    scopus 로고
    • Methods for site-specific drug conjugation to antibodies
    • Behrens, C. R., Liu, B., Methods for site-specific drug conjugation to antibodies. MAbs 2014, 6, 46-53.
    • (2014) MAbs , vol.6 , pp. 46-53
    • Behrens, C.R.1    Liu, B.2
  • 12
    • 0042738861 scopus 로고    scopus 로고
    • cAC10-vcMMAE, an anti-CD30-monomethyl auristatin E conjugate with potent and selective antitumor activity
    • Francisco, J. A., Cerveny, C. G., Meyer, D. L., Mixan, B. J. et al., cAC10-vcMMAE, an anti-CD30-monomethyl auristatin E conjugate with potent and selective antitumor activity. Blood 2003, 102, 1458-1465.
    • (2003) Blood , vol.102 , pp. 1458-1465
    • Francisco, J.A.1    Cerveny, C.G.2    Meyer, D.L.3    Mixan, B.J.4
  • 13
    • 56449129810 scopus 로고    scopus 로고
    • Targeting HER2-positive breast cancer with trastuzumab-DM1, an antibody-cytotoxic drug conjugate
    • Lewis, P., Gail, D., Li, G., Dugger, D. L. et al., Targeting HER2-positive breast cancer with trastuzumab-DM1, an antibody-cytotoxic drug conjugate. Cancer Res. 2008, 68, 9280-9290.
    • (2008) Cancer Res. , vol.68 , pp. 9280-9290
    • Lewis, P.1    Gail, D.2    Li, G.3    Dugger, D.L.4
  • 14
    • 84938751906 scopus 로고    scopus 로고
    • Conjugates of small molecule drugs with antibodies and other proteins
    • Feng, Y., Zhu, Z., Chen, W., Prabakaran, P. et al., Conjugates of small molecule drugs with antibodies and other proteins. Biomedicines 2014, 2, 1-13.
    • (2014) Biomedicines , vol.2 , pp. 1-13
    • Feng, Y.1    Zhu, Z.2    Chen, W.3    Prabakaran, P.4
  • 15
    • 24344456964 scopus 로고    scopus 로고
    • Structural characterization of the maytansinoid-monoclonal antibody immunoconjugate, huN901-DM1, by mass spectrometry
    • Wang, L., Amphlett, G., Blättler, W. A., Lambert, J. M., Zhang, W., Structural characterization of the maytansinoid-monoclonal antibody immunoconjugate, huN901-DM1, by mass spectrometry. Protein Sci. 2005, 14, 2436-2446.
    • (2005) Protein Sci. , vol.14 , pp. 2436-2446
    • Wang, L.1    Amphlett, G.2    Blättler, W.A.3    Lambert, J.M.4    Zhang, W.5
  • 16
    • 6044223544 scopus 로고    scopus 로고
    • Effects of drug loading on the antitumor activity of a monoclonal antibody drug conjugate
    • Hamblett, K. J., Senter, P. D., Chace, D. F., Sun, M. M. C. et al., Effects of drug loading on the antitumor activity of a monoclonal antibody drug conjugate. Clin. Cancer Res. 2004, 10, 7063-7070.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 7063-7070
    • Hamblett, K.J.1    Senter, P.D.2    Chace, D.F.3    Sun, M.M.C.4
  • 17
    • 84891780613 scopus 로고    scopus 로고
    • Mass spectrometry methods for studying structure and dynamics of biological macromolecules
    • Konermann, L., Vahidi, S., Sowole, M. A., Mass spectrometry methods for studying structure and dynamics of biological macromolecules. Anal. Chem. 2014, 86, 213-232.
    • (2014) Anal. Chem. , vol.86 , pp. 213-232
    • Konermann, L.1    Vahidi, S.2    Sowole, M.A.3
  • 18
    • 69849100869 scopus 로고    scopus 로고
    • Probing protein structure by amino acid-specific covalent labeling and mass spectrometry
    • Mendoza, V. L., Vachet, R. W., Probing protein structure by amino acid-specific covalent labeling and mass spectrometry. Mass Spectrom. Rev. 2009, 28, 785-815.
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 785-815
    • Mendoza, V.L.1    Vachet, R.W.2
  • 19
    • 84860758736 scopus 로고    scopus 로고
    • Conformational analysis of therapeutic proteins by hydroxyl radical protein footprinting
    • Watson, C., Sharp, J. S., Conformational analysis of therapeutic proteins by hydroxyl radical protein footprinting. AAPS J. 2012, 14, 206-217.
    • (2012) AAPS J. , vol.14 , pp. 206-217
    • Watson, C.1    Sharp, J.S.2
  • 20
    • 84872848394 scopus 로고    scopus 로고
    • Structural analysis of a therapeutic monoclonal antibody dimer by hydroxyl radical footprinting
    • Deperalta, G., Alvarez, M., Bechtel, C., Dong, K. et al., Structural analysis of a therapeutic monoclonal antibody dimer by hydroxyl radical footprinting. MAbs 2013, 5, 86-101.
    • (2013) MAbs , vol.5 , pp. 86-101
    • Deperalta, G.1    Alvarez, M.2    Bechtel, C.3    Dong, K.4
  • 21
    • 33745260411 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction surfaces using a combination of efficient lysine acetylation and nanoLC-MALDI-MS/MS applied to the E9:Im9 bacteriotoxin-immunity protein complex
    • Scholten, A., Visser, N. F. C., van den Heuvel, R. H. H., Heck, A. J. R., Analysis of protein-protein interaction surfaces using a combination of efficient lysine acetylation and nanoLC-MALDI-MS/MS applied to the E9:Im9 bacteriotoxin-immunity protein complex. J. Am. Soc. Mass Spectrom. 2006, 17, 983-994.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 983-994
    • Scholten, A.1    Visser, N.F.C.2    van den Heuvel, R.H.H.3    Heck, A.J.R.4
  • 22
    • 0037058982 scopus 로고    scopus 로고
    • Identification of specific HIV-1 reverse transcriptase contacts to the viral RNA:tRNA complex by mass spectrometry and a primary amine selective reagent
    • Kvaratskhelia, M., Miller, J. T., Budihas, S. R., Pannell, L. K. et al., Identification of specific HIV-1 reverse transcriptase contacts to the viral RNA:tRNA complex by mass spectrometry and a primary amine selective reagent. Proc. Natl. Acad. Sci. USA 2002, 99, 15988-15993.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15988-15993
    • Kvaratskhelia, M.1    Miller, J.T.2    Budihas, S.R.3    Pannell, L.K.4
  • 23
    • 12444345515 scopus 로고    scopus 로고
    • Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • Thompson, A., Schäfer, J., Kuhn, K., Kienle, S. et al., Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS. Anal. Chem. 2003, 75, 1895-1904.
    • (2003) Anal. Chem. , vol.75 , pp. 1895-1904
    • Thompson, A.1    Schäfer, J.2    Kuhn, K.3    Kienle, S.4
  • 24
    • 84886895063 scopus 로고    scopus 로고
    • Covalent labeling with isotopically encoded reagents for faster structural analysis of proteins by mass spectrometry
    • Zhou, Y., Vachet, R. W., Covalent labeling with isotopically encoded reagents for faster structural analysis of proteins by mass spectrometry. Anal. Chem. 2013, 85, 9664-9670.
    • (2013) Anal. Chem. , vol.85 , pp. 9664-9670
    • Zhou, Y.1    Vachet, R.W.2
  • 25
    • 84906949596 scopus 로고    scopus 로고
    • Simultaneous assessment of kinetic, site-specific, and structural aspects of enzymatic protein phosphorylation
    • van de Waterbeemd, M., Lössl, P., Gautier, V., Marino, F. et al., Simultaneous assessment of kinetic, site-specific, and structural aspects of enzymatic protein phosphorylation. Angew. Chem. Int. Ed. Engl. 2014, 53, 9660-9664.
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , pp. 9660-9664
    • van de Waterbeemd, M.1    Lössl, P.2    Gautier, V.3    Marino, F.4
  • 26
    • 84869033783 scopus 로고    scopus 로고
    • High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies
    • Rose, R. J., Damoc, E., Denisov, E., Makarov, A., Heck, A. J. R., High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies. Nat. Methods 2012, 9, 1084-1086.
    • (2012) Nat. Methods , vol.9 , pp. 1084-1086
    • Rose, R.J.1    Damoc, E.2    Denisov, E.3    Makarov, A.4    Heck, A.J.R.5
  • 27
    • 84876584375 scopus 로고    scopus 로고
    • Mutation of Y407 in the CH3 domain dramatically alters glycosylation and structure of human IgG
    • Rose, R. J., van Berkel, P. H., van den Bremer, E. T., Labrijn, A. F. et al., Mutation of Y407 in the CH3 domain dramatically alters glycosylation and structure of human IgG. MAbs 2013, 5, 219-228.
    • (2013) MAbs , vol.5 , pp. 219-228
    • Rose, R.J.1    van Berkel, P.H.2    van den Bremer, E.T.3    Labrijn, A.F.4
  • 28
    • 84905376058 scopus 로고    scopus 로고
    • Proteome adaptation of Saccharomyces cerevisiae to severe calorie restriction in Retentostat cultures
    • Binai, N. A., Bisschops, M. M., van Breukelen, B., Mohammed, S. et al., Proteome adaptation of Saccharomyces cerevisiae to severe calorie restriction in Retentostat cultures. J. Proteome Res. 2014, 13, 3542-3553.
    • (2014) J. Proteome Res. , vol.13 , pp. 3542-3553
    • Binai, N.A.1    Bisschops, M.M.2    van Breukelen, B.3    Mohammed, S.4
  • 29
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers, F., Wilm, A., Dineen, D., Gibson, T. J. et al., Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol. Syst. Biol. 2011, 7, 539.
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 539
    • Sievers, F.1    Wilm, A.2    Dineen, D.3    Gibson, T.J.4
  • 30
    • 84879371161 scopus 로고    scopus 로고
    • Small-molecule ligand docking into comparative models with Rosetta
    • Combs, S. A., Deluca, S. L., Deluca, S. H., Lemmon, G. H. et al., Small-molecule ligand docking into comparative models with Rosetta. Nat. Protoc. 2013, 8, 1277-1298.
    • (2013) Nat. Protoc. , vol.8 , pp. 1277-1298
    • Combs, S.A.1    Deluca, S.L.2    Deluca, S.H.3    Lemmon, G.H.4
  • 32
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold, J. N., Wormald, M. R., Sim, R. B., Rudd, P. M., Dwek, R. A., The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 2007, 25, 21-50.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 33
    • 84871270725 scopus 로고    scopus 로고
    • Exploring an Orbitrap analyzer for the characterization of intact antibodies by native mass spectrometry
    • Rosati, S., Rose, R. J., Thompson, N. J., van Duijn, E. et al., Exploring an Orbitrap analyzer for the characterization of intact antibodies by native mass spectrometry. Angew. Chem. Int. Ed. Engl. 2012, 51, 12992-12996.
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 12992-12996
    • Rosati, S.1    Rose, R.J.2    Thompson, N.J.3    van Duijn, E.4
  • 34
    • 34748837881 scopus 로고    scopus 로고
    • Analysis of N-glycans from recombi-nant immunoglobulin G by on-line reversed-phase high-performance liquid chromatography/mass spectrometry
    • Chen, X., Flynn, G. C., Analysis of N-glycans from recombi-nant immunoglobulin G by on-line reversed-phase high-performance liquid chromatography/mass spectrometry. Anal. Biochem. 2007, 370, 147-161.
    • (2007) Anal. Biochem. , vol.370 , pp. 147-161
    • Chen, X.1    Flynn, G.C.2
  • 35
    • 84867836578 scopus 로고    scopus 로고
    • Revisiting the role of glycosylation in the structure of human IgG Fc
    • Borrok, M. J., Jung, S. T., Kang, T. H., Monzingo, A. F., Georgiou, G., Revisiting the role of glycosylation in the structure of human IgG Fc. ACS Chem. Biol. 2012, 7, 1596-1602.
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1596-1602
    • Borrok, M.J.1    Jung, S.T.2    Kang, T.H.3    Monzingo, A.F.4    Georgiou, G.5
  • 36
    • 17944380435 scopus 로고    scopus 로고
    • Crystal structure of a neutralizing human IgG against HIV-1: a template for vaccine design
    • Saphire, E. O., Parren, P. W., Pantophlet, R., Zwick, M. B. et al., Crystal structure of a neutralizing human IgG against HIV-1: a template for vaccine design. Science 2001, 293, 1155-1159.
    • (2001) Science , vol.293 , pp. 1155-1159
    • Saphire, E.O.1    Parren, P.W.2    Pantophlet, R.3    Zwick, M.B.4
  • 37
    • 39449112129 scopus 로고    scopus 로고
    • Partial acetylation of lysine residues improves intraprotein cross-linking
    • Guo, X., Bandyopadhyay, P., Schilling, B., Young, M. M. et al., Partial acetylation of lysine residues improves intraprotein cross-linking. Anal. Chem. 2008, 80, 951-960.
    • (2008) Anal. Chem. , vol.80 , pp. 951-960
    • Guo, X.1    Bandyopadhyay, P.2    Schilling, B.3    Young, M.M.4
  • 38
    • 84887975602 scopus 로고    scopus 로고
    • Small-angle neutron scattering study of a monoclonal antibody using free-energy constraints
    • Clark, N. J., Zhang, H., Krueger, S., Lee, H. J. et al., Small-angle neutron scattering study of a monoclonal antibody using free-energy constraints. J. Phys. Chem. B. 2013, 117, 14029-14038.
    • (2013) J. Phys. Chem. B. , vol.117 , pp. 14029-14038
    • Clark, N.J.1    Zhang, H.2    Krueger, S.3    Lee, H.J.4
  • 39
    • 84865130275 scopus 로고    scopus 로고
    • Influence of the cosolute environment on IgG solution structure analyzed by small-angle X-ray scattering
    • Lilyestrom, W. G., Shire, S. J., Scherer, T. M., Influence of the cosolute environment on IgG solution structure analyzed by small-angle X-ray scattering. J. Phys. Chem. B. 2012, 116, 9611-9618.
    • (2012) J. Phys. Chem. B. , vol.116 , pp. 9611-9618
    • Lilyestrom, W.G.1    Shire, S.J.2    Scherer, T.M.3


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