메뉴 건너뛰기




Volumn 14, Issue 9, 2015, Pages 4019-4028

Glycoforms of immunoglobulin g based biopharmaceuticals are differentially cleaved by trypsin due to the glycoform influence on higher-order structure

Author keywords

biopharmaceuticals; glycoproteomics; glycosylation; higher order structure; immunoglobulin G; method development; monoclonal antibodies; proteolytic biases; trypsin substrate specificity; tryptic cleavage

Indexed keywords

GLYCAN; IMMUNOGLOBULIN G; MANNOSE; MONOCLONAL ANTIBODY; POLYCLONAL ANTIBODY; TRYPSIN; GLYCOPEPTIDE;

EID: 84941057683     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/acs.jproteome.5b00573     Document Type: Article
Times cited : (36)

References (30)
  • 2
    • 84894069343 scopus 로고    scopus 로고
    • Database construction and peptide identification strategies for proteogenomic studies on sequenced genomes
    • Hernandez, C.; Waridel, P.; Quadroni, M. Database construction and peptide identification strategies for proteogenomic studies on sequenced genomes Curr. Top. Med. Chem. 2014, 14, 425-434 10.2174/1568026613666131204105652
    • (2014) Curr. Top. Med. Chem. , vol.14 , pp. 425-434
    • Hernandez, C.1    Waridel, P.2    Quadroni, M.3
  • 3
    • 84930067094 scopus 로고    scopus 로고
    • Clinical protein mass spectrometry
    • Scherl, A. Clinical protein mass spectrometry Methods 2015, 81, 3 10.1016/j.ymeth.2015.02.015
    • (2015) Methods , vol.81 , pp. 3
    • Scherl, A.1
  • 5
    • 84874616206 scopus 로고    scopus 로고
    • Protein digestion: An overview of the available techniques and recent developments
    • Switzar, L.; Giera, M.; Niessen, W. M. Protein digestion: an overview of the available techniques and recent developments J. Proteome Res. 2013, 12, 1067-1077 10.1021/pr301201x
    • (2013) J. Proteome Res. , vol.12 , pp. 1067-1077
    • Switzar, L.1    Giera, M.2    Niessen, W.M.3
  • 6
    • 84906940191 scopus 로고    scopus 로고
    • A Critical Review of Trypsin Digestion for LC-MS Based Proteomics
    • Leung, H. InTech: Rijeka, Croatia
    • Hustoft, H. K.; Malerod, H.; Wilson, S. R.; Reubsaet, L.; Lundanes, E.; Greibrokk, T. A Critical Review of Trypsin Digestion for LC-MS Based Proteomics. In Integrative Proteomics; Leung, H., Ed.; InTech: Rijeka, Croatia, 2012; Vol. 1, pp 73-82.
    • (2012) Integrative Proteomics , vol.1 , pp. 73-82
    • Hustoft, H.K.1    Malerod, H.2    Wilson, S.R.3    Reubsaet, L.4    Lundanes, E.5    Greibrokk, T.6
  • 7
    • 80054732682 scopus 로고    scopus 로고
    • Quantitative proteomics of complex mixtures
    • Coombs, K. M. Quantitative proteomics of complex mixtures Expert Rev. Proteomics 2011, 8, 659-677 10.1586/epr.11.55
    • (2011) Expert Rev. Proteomics , vol.8 , pp. 659-677
    • Coombs, K.M.1
  • 8
    • 0142135856 scopus 로고    scopus 로고
    • Determination of N-glycosylation sites and site heterogeneity in glycoproteins
    • An, H. J.; Peavy, T. R.; Hedrick, J. L.; Lebrilla, C. B. Determination of N-glycosylation sites and site heterogeneity in glycoproteins Anal. Chem. 2003, 75, 5628-5637 10.1021/ac034414x
    • (2003) Anal. Chem. , vol.75 , pp. 5628-5637
    • An, H.J.1    Peavy, T.R.2    Hedrick, J.L.3    Lebrilla, C.B.4
  • 9
    • 83055168517 scopus 로고    scopus 로고
    • Targeted mass spectrometric approach for biomarker discovery and validation with nonglycosylated tryptic peptides from N-linked glycoproteins in human plasma
    • Lee, J. Y.; Kim, J. Y.; Park, G. W.; Cheon, M. H.; Kwon, K. H.; Ahn, Y. H.; Moon, M. H.; Lee, H. J.; Paik, Y. K.; Yoo, J. S. Targeted mass spectrometric approach for biomarker discovery and validation with nonglycosylated tryptic peptides from N-linked glycoproteins in human plasma Mol. Cell. Proteomics 2011, 10, 1-12 10.1074/mcp.M111.009290
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. 1-12
    • Lee, J.Y.1    Kim, J.Y.2    Park, G.W.3    Cheon, M.H.4    Kwon, K.H.5    Ahn, Y.H.6    Moon, M.H.7    Lee, H.J.8    Paik, Y.K.9    Yoo, J.S.10
  • 10
    • 0000108345 scopus 로고    scopus 로고
    • The utility of nonspecific proteases in the characterization of glycoproteins by high-resolution time-of-flight mass spectrometry
    • Juhasz, P.; Martin, S. A. The utility of nonspecific proteases in the characterization of glycoproteins by high-resolution time-of-flight mass spectrometry Int. J. Mass Spectrom. Ion Processes 1997, 169-170, 217-230 10.1016/S0168-1176(97)00219-X
    • (1997) Int. J. Mass Spectrom. Ion Processes , vol.169-170 , pp. 217-230
    • Juhasz, P.1    Martin, S.A.2
  • 11
    • 84867404382 scopus 로고    scopus 로고
    • LC-MS analysis of glycopeptides of recombinant monoclonal antibodies by a rapid digestion procedure
    • Du, Y.; Wang, F.; May, K.; Xu, W.; Liu, H. LC-MS analysis of glycopeptides of recombinant monoclonal antibodies by a rapid digestion procedure J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. 2012, 907, 87-93 10.1016/j.jchromb.2012.09.004
    • (2012) J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. , vol.907 , pp. 87-93
    • Du, Y.1    Wang, F.2    May, K.3    Xu, W.4    Liu, H.5
  • 12
    • 76149084829 scopus 로고    scopus 로고
    • GlycoSpectrumScan: Fishing glycopeptides from MS spectra of protease digests of human colostrum sIgA
    • Deshpande, N.; Jensen, P. H.; Packer, N. H.; Kolarich, D. GlycoSpectrumScan: fishing glycopeptides from MS spectra of protease digests of human colostrum sIgA J. Proteome Res. 2010, 9, 1063-1075 10.1021/pr900956x
    • (2010) J. Proteome Res. , vol.9 , pp. 1063-1075
    • Deshpande, N.1    Jensen, P.H.2    Packer, N.H.3    Kolarich, D.4
  • 13
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp, S.; Mimura, Y.; Jefferis, R.; Huber, R.; Sondermann, P. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity J. Mol. Biol. 2003, 325, 979-989 10.1016/S0022-2836(02)01250-0
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 14
    • 84889811290 scopus 로고    scopus 로고
    • Consequences of glycan truncation on Fc structural integrity
    • Buck, P. M.; Kumar, S.; Singh, S. K. Consequences of glycan truncation on Fc structural integrity MAbs 2013, 5, 904-916 10.4161/mabs.26453
    • (2013) MAbs , vol.5 , pp. 904-916
    • Buck, P.M.1    Kumar, S.2    Singh, S.K.3
  • 15
    • 2142714017 scopus 로고    scopus 로고
    • Monoclonal antibodies as therapeutic agents for cancer
    • Harris, M. Monoclonal antibodies as therapeutic agents for cancer Lancet Oncol. 2004, 5, 292-302 10.1016/S1470-2045(04)01467-6
    • (2004) Lancet Oncol. , vol.5 , pp. 292-302
    • Harris, M.1
  • 16
    • 31044432797 scopus 로고    scopus 로고
    • Use of intravenous immunoglobulin G (IVIG)
    • John Looney, R.; Huggins, J. Use of intravenous immunoglobulin G (IVIG) Best Pract Res. Clin Haematol 2006, 19, 3-25 10.1016/j.beha.2005.01.032
    • (2006) Best Pract Res. Clin Haematol , vol.19 , pp. 3-25
    • John Looney, R.1    Huggins, J.2
  • 17
    • 70349762761 scopus 로고    scopus 로고
    • Electrospray ionization quadrupole ion-mobility time-of-flight mass spectrometry as a tool to distinguish the lot-to-lot heterogeneity in N-glycosylation profile of the therapeutic monoclonal antibody trastuzumab
    • Damen, C. W.; Chen, W.; Chakraborty, A. B.; Oosterhout, M.; Mazzeo, J. R.; Gebler, J. C.; Schellens, J. H.; Rosing, H.; Beijnen, J. H. Electrospray ionization quadrupole ion-mobility time-of-flight mass spectrometry as a tool to distinguish the lot-to-lot heterogeneity in N-glycosylation profile of the therapeutic monoclonal antibody trastuzumab J. Am. Soc. Mass Spectrom. 2009, 20, 2021-2033 10.1016/j.jasms.2009.07.017
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 2021-2033
    • Damen, C.W.1    Chen, W.2    Chakraborty, A.B.3    Oosterhout, M.4    Mazzeo, J.R.5    Gebler, J.C.6    Schellens, J.H.7    Rosing, H.8    Beijnen, J.H.9
  • 20
    • 77954772536 scopus 로고    scopus 로고
    • MZmine 2: Modular framework for processing, visualizing, and analyzing mass spectrometry-based molecular profile data
    • Pluskal, T.; Castillo, S.; Villar-Briones, A.; Oresic, M. MZmine 2: modular framework for processing, visualizing, and analyzing mass spectrometry-based molecular profile data BMC Bioinf. 2010, 11, 395 10.1186/1471-2105-11-395
    • (2010) BMC Bioinf. , vol.11 , pp. 395
    • Pluskal, T.1    Castillo, S.2    Villar-Briones, A.3    Oresic, M.4
  • 21
    • 0013153953 scopus 로고
    • Centrum voor Wiskunde en Informatica Amsterdam: Amsterdam, The Netherlands, Technical Report CS-R9526.
    • Van Rossum, G.; Drake, Jr., F. L. Python Reference Manual; Centrum voor Wiskunde en Informatica Amsterdam: Amsterdam, The Netherlands, 1995; Technical Report CS-R9526.
    • (1995) Python Reference Manual
    • Van Rossum, G.1    Drake, F.L.2
  • 22
    • 84863304598 scopus 로고    scopus 로고
    • R Foundation for Statistical Computing: Vienna, Austria
    • R Core Team. R: A Language and Environment for Statistical Computing; R Foundation for Statistical Computing: Vienna, Austria, 2012. http://www.R-project.org/.
    • (2012) R: A Language and Environment for Statistical Computing
  • 23
    • 84910647104 scopus 로고    scopus 로고
    • Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes
    • Bondt, A.; Rombouts, Y.; Selman, M. H.; Hensbergen, P. J.; Reiding, K. R.; Hazes, J. M.; Dolhain, R. J.; Wuhrer, M. Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes Mol. Cell. Proteomics 2014, 13, 3029-3039 10.1074/mcp.M114.039537
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 3029-3039
    • Bondt, A.1    Rombouts, Y.2    Selman, M.H.3    Hensbergen, P.J.4    Reiding, K.R.5    Hazes, J.M.6    Dolhain, R.J.7    Wuhrer, M.8
  • 24
    • 84983656017 scopus 로고    scopus 로고
    • Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles-Part 2: Mass spectrometric methods
    • Reusch, D.; Haberger, M.; Falck, D.; Peter, B.; Maier, B.; Gassner, J.; Hook, M.; Wagner, K.; Bonnington, L.; Bulau, P.; Wuhrer, M. Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles-Part 2: mass spectrometric methods MAbs 2015, 7, 732 10.1080/19420862.2015.1045173
    • (2015) MAbs , vol.7 , pp. 732
    • Reusch, D.1    Haberger, M.2    Falck, D.3    Peter, B.4    Maier, B.5    Gassner, J.6    Hook, M.7    Wagner, K.8    Bonnington, L.9    Bulau, P.10    Wuhrer, M.11
  • 26
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • Bailey, J. E.; Umana, P.; Jean-Mairet, J.; Moudry, R.; Amstutz, H. Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity Nat. Biotechnol. 1999, 17, 176-180 10.1038/6179
    • (1999) Nat. Biotechnol. , vol.17 , pp. 176-180
    • Bailey, J.E.1    Umana, P.2    Jean-Mairet, J.3    Moudry, R.4    Amstutz, H.5
  • 27
    • 0035081693 scopus 로고    scopus 로고
    • The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: Properties of a series of truncated glycoforms
    • Mimura, Y.; Church, S.; Ghirlando, R.; Ashton, P. R.; Dong, S.; Goodall, M.; Lund, J.; Jefferis, R. The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms Mol. Immunol. 2000, 37, 697-706 10.1016/S0161-5890(00)00105-X
    • (2000) Mol. Immunol. , vol.37 , pp. 697-706
    • Mimura, Y.1    Church, S.2    Ghirlando, R.3    Ashton, P.R.4    Dong, S.5    Goodall, M.6    Lund, J.7    Jefferis, R.8
  • 28
    • 84918825382 scopus 로고    scopus 로고
    • IgG subclasses and allotypes: From structure to effector functions
    • Vidarsson, G.; Dekkers, G.; Rispens, T. IgG subclasses and allotypes: from structure to effector functions Front. Immunol. 2014, 5, 520 10.3389/fimmu.2014.00520
    • (2014) Front. Immunol. , vol.5 , pp. 520
    • Vidarsson, G.1    Dekkers, G.2    Rispens, T.3
  • 29
    • 84904253899 scopus 로고    scopus 로고
    • Diversity in structure and functions of antibody sialylation in the Fc
    • Raju, T. S.; Lang, S. E. Diversity in structure and functions of antibody sialylation in the Fc Curr. Opin. Biotechnol. 2014, 30, 147-152 10.1016/j.copbio.2014.06.014
    • (2014) Curr. Opin. Biotechnol. , vol.30 , pp. 147-152
    • Raju, T.S.1    Lang, S.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.