NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods

Maria Lorna A. De Leoz; David L. Duewer; Adam Fung; Lily Liu; Hoi Kei Yau; Oscar Potter; Gregory O. Staples; Kenichiro Furuki; Ruth Frenkel; Yunli Hu; Zoran Sosic; Peiqing Zhang; Friedrich Altmann; Clemens Gru Nwald-Grube; Chun Shao; Joseph Zaia; Waltraud Evers; Stuart Pengelley; Detlev Suckau; Anja Wiechmann; Anja Resemann; Wolfgang Jabs; Alain Beck; John W. Froehlich; Chuncui Huang; Yan Li; Yaming Liu; Shiwei Sun; Yaojun Wang; Youngsuk Seo; Hyun Joo An; Niels Christian Reichardt; Juan Echevarria Ruiz; Stephanie Archer-Hartmann; Parastoo Azadi; Len Bell; Zsuzsanna Lakos; Yanming An; John F. Cipollo; Maja Pucic-Bakovic; Jerko Štambuk; Gordan Lauc; Xu Li; Peng George Wang; Andreas Bock; René Hennig; Erdmann Rapp; Marybeth Creskey; Terry D. Cyr; Miyako Nakano; Taiki Sugiyama; Pui King Amy Leung; Paweł Link-Lenczowski; Jolanta Jaworek; Shuang Yang; Hui Zhang; Tim Kelly; Song Klapoetke; Rui Cao; Jin Young Kim; Hyun Kyoung Lee; Ju Yeon Lee; Jong Shin Yoo; Sa Rang Kim; Soo Kyung Suh; Noortje de Haan; David Falck; Guinevere S.M. Lageveen-Kammeijer; Manfred Wuhrer; Robert J. Emery; Radoslaw P. Kozak; Li Phing Liew; Louise Royle; Paulina A. Urbanowicz; Nicolle H. Packer; Xiaomin Song; Arun Everest-Dass; Erika Lattová; Samanta Cajic; Kathirvel Alagesan; Daniel Kolarich; Toyin Kasali; Viv Lindo; Yuetian Chen; Kudrat Goswami; Brian Gau; Ravi Amunugama; Richard Jones; Corné J.M. Stroop; Koichi Kato; Hirokazu Yagi; Sachiko Kondo; C. T. Yuen; Akira Harazono; Xiaofeng Shi; Paula E. Magnelli; Brian T. Kasper; Lara Mahal; David J. Harvey; Roisin O'Flaherty; Pauline M. Rudd; Radka Saldova; Elizabeth S. Hecht; David C. Muddiman; Jichao Kang; Prachi Bhoskar; Daniele Menard; Andrew Saati; Christine Merle; Steven Mast; Sam Tep; Jennie Truong; Takashi Nishikaze; Sadanori Sekiya; Aaron Shafer; Sohei Funaoka; Masaaki Toyoda; Peter de Vreugd; Cassie Caron; Pralima Pradhan; Niclas Chiang Tan; Yehia Mechref; Sachin Patil; Jeffrey S. Rohrer; Ranjan Chakrabarti; Disha Dadke; Mohammedazam Lahori; Chunxia Zou; Christopher Cairo; Béla Reiz; Randy M. Whittal; Carlito B. Lebrilla; Lauren Wu; Andras Guttman; Marton Szigeti; Benjamin G. Kremkow; Kelvin H. Lee; Carina Sihlbom; Barbara Adamczyk; Chunsheng Jin; Niclas G. Karlsson; Jessica Örnros; Göran Larson; Jonas Nilsson; Bernd Meyer; Alena Wiegandt; Emy Komatsu; Helene Perreault; Edward D. Bodnar; Nassur Said; Yannis Nicolas Francois; Emmanuelle Leize-Wagner; Sandra Maier; Anne Zeck; Albert J.R. Heck; Yang Yang; Rob Haselberg; Ying Qing Yu; William Alley; Joseph W. Leone; Hua Yuan; Stephen E. Stein

doi:10.1074/mcp.RA119.001677

NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods

Maria Lorna A. De Leoz, David L. Duewer, Adam Fung, Lily Liu, Hoi Kei Yau, Oscar Potter, Gregory O. Staples, Kenichiro Furuki, Ruth Frenkel, Yunli Hu, Zoran Sosic, Peiqing Zhang, Friedrich Altmann, Clemens Gru Nwald-Grube, Chun Shao, Joseph Zaia, Waltraud Evers, Stuart Pengelley, Detlev Suckau, Anja WiechmannAnja Resemann, Wolfgang Jabs, Alain Beck, John W. Froehlich, Chuncui Huang, Yan Li, Yaming Liu, Shiwei Sun, Yaojun Wang, Youngsuk Seo, Hyun Joo An, Niels Christian Reichardt, Juan Echevarria Ruiz, Stephanie Archer-Hartmann, Parastoo Azadi, Len Bell, Zsuzsanna Lakos, Yanming An, John F. Cipollo, Maja Pucic-Bakovic, Jerko Štambuk, Gordan Lauc, Xu Li, Peng George Wang, Andreas Bock, René Hennig, Erdmann Rapp, Marybeth Creskey, Terry D. Cyr, Miyako Nakano, Taiki Sugiyama, Pui King Amy Leung, Paweł Link-Lenczowski, Jolanta Jaworek, Shuang Yang, Hui Zhang, Tim Kelly, Song Klapoetke, Rui Cao, Jin Young Kim, Hyun Kyoung Lee, Ju Yeon Lee, Jong Shin Yoo, Sa Rang Kim, Soo Kyung Suh, Noortje de Haan, David Falck, Guinevere S.M. Lageveen-Kammeijer, Manfred Wuhrer, Robert J. Emery, Radoslaw P. Kozak, Li Phing Liew, Louise Royle, Paulina A. Urbanowicz, Nicolle H. Packer, Xiaomin Song, Arun Everest-Dass, Erika Lattová, Samanta Cajic, Kathirvel Alagesan, Daniel Kolarich, Toyin Kasali, Viv Lindo, Yuetian Chen, Kudrat Goswami, Brian Gau, Ravi Amunugama, Richard Jones, Corné J.M. Stroop, Koichi Kato, Hirokazu Yagi, Sachiko Kondo, C. T. Yuen, Akira Harazono, Xiaofeng Shi, Paula E. Magnelli, Brian T. Kasper, Lara Mahal, David J. Harvey, Roisin O'Flaherty, Pauline M. Rudd, Radka Saldova, Elizabeth S. Hecht, David C. Muddiman, Jichao Kang, Prachi Bhoskar, Daniele Menard, Andrew Saati, Christine Merle, Steven Mast, Sam Tep, Jennie Truong, Takashi Nishikaze, Sadanori Sekiya, Aaron Shafer, Sohei Funaoka, Masaaki Toyoda, Peter de Vreugd, Cassie Caron, Pralima Pradhan, Niclas Chiang Tan, Yehia Mechref, Sachin Patil, Jeffrey S. Rohrer, Ranjan Chakrabarti, Disha Dadke, Mohammedazam Lahori, Chunxia Zou, Christopher Cairo, Béla Reiz, Randy M. Whittal, Carlito B. Lebrilla, Lauren Wu, Andras Guttman, Marton Szigeti, Benjamin G. Kremkow, Kelvin H. Lee, Carina Sihlbom, Barbara Adamczyk, Chunsheng Jin, Niclas G. Karlsson, Jessica Örnros, Göran Larson, Jonas Nilsson, Bernd Meyer, Alena Wiegandt, Emy Komatsu, Helene Perreault, Edward D. Bodnar, Nassur Said, Yannis Nicolas Francois, Emmanuelle Leize-Wagner, Sandra Maier, Anne Zeck, Albert J.R. Heck, Yang Yang, Rob Haselberg, Ying Qing Yu, William Alley, Joseph W. Leone, Hua Yuan, Stephen E. Stein

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods.

Original language	English
Pages (from-to)	11-30
Number of pages	20
Journal	MCP : Molecular & cellular proteomics
Volume	19
Issue number	1
Early online date	7 Oct 2019
DOIs	https://doi.org/10.1074/mcp.RA119.001677
Publication status	Published - 1 Jan 2020

Funding

This work was supported by: 1. Science Foundation Ireland Starting Investigator Research under Grant 13/SIRG/2164 to R.S.; 2. Swedish Research Council under Grant 8266 to G.L. and J.N.; 3. Alberta Glycomics Centre to C.C.; 4. National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK) under Grant K01- DK101632 to J.W.F.; 5. Australian Research Council Centre of Excellence for Nanoscale BioPhotonics (CNBP) under Grant CE1401000003 to N.H.P. and A.E.-D.; 6. European Union (EU) FP7 program HighGlycan under Grant 278535 to R.O.F. and P.M.R.; 7. National Institutes of Health (NIH) Research Resource for Biomedical Glycomics under Grant P41GM10349010 and Grant 1S10OD018530 to P.A.; 8. Austrian Research Promotion Agency Laura Bassi Center of Expertise under Grant 822757 to C.G.-G.; 9. National Natural Science Foundation of China under Grant 31600650, 31671369, and 31770775D to D.B., S.S., C.H. and Y.L.; 10. Deutsche Forschungs- gemeinschaft (DFG, German Research Foundation) "The concert of dolichol-based glycosylation: from molecules to disease models" under Grant FOR2509 to E.R.; 11. European Union (EC) "IMforFuture" under Grant 721815 to E.R.; 12. German Federal Ministry of Education and Research (BMBF) "Die Golgi Glykan Fabrik 2.0" under Grant 031A557 to S.C. and E.R.; 13. Health Canada, Government of Canada to T.D.C. and M.C.; 14. European Union FP7 GastricGlycoExplorer ITN under Grant 316929 and the Swedish Research Council under Grant 621-2013-5895 to N.G.K.; 15. National Research Council of Science and Technology Creative Allied Project (CAP) under Grant NTM2371511 to J.S.Y.; 16. Hungarian Government project under Grant NKFIH-K 116263 and BIONANO GINOP-2.3.2- 15-2016-00017 to A.G.; and 17. National Research Foundation of Korea under Grant NRF-2013M3A9B6075933 to H.J.A. * This work was supported by: 1. Science Foundation Ireland Starting Investigator Research under Grant 13/SIRG/2164 to R.S.; 2. Swedish Research Council under Grant 8266 to G.L. and J.N.; 3. Alberta Glycomics Centre to C.C.; 4. National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK) under Grant K01-DK101632 to J.W.F.; 5. Australian Research Council Centre of Excellence for Nanoscale BioPhotonics (CNBP) under Grant CE1401000003 to N.H.P. and A.E.-D.; 6. European Union (EU) FP7 program HighGlycan under Grant 278535 to R.O.F. and P.M.R.; 7. National Institutes of Health (NIH) Research Resource for Biomedical Glycomics under Grant P41GM10349010 and Grant 1S10OD018530 to P.A.; 8. Austrian Research Promotion Agency Laura Bassi Center of Expertise under Grant 822757 to C.G.-G.; 9. National Natural Science Foundation of China under Grant 31600650, 31671369, and 31770775D to D.B., S.S., C.H. and Y.L.; 10. Deutsche Forschungs- gemeinschaft (DFG, German Research Foundation) “The concert of dolichol-based glycosylation: from molecules to disease models” under Grant FOR2509 to E.R.; 11. European Union (EC) “IMforFuture” under Grant 721815 to E.R.; 12. German Federal Ministry of Education and Research (BMBF) “Die Golgi Glykan Fabrik 2.0” under Grant 031A557 to S.C. and E.R.; 13. Health Canada, Government of Canada to T.D.C. and M.C.; 14. European Union FP7 GastricGlycoExplorer ITN under Grant 316929 and the Swedish Research Council under Grant 621–2013-5895 to N.G.K.; 15. National Research Council of Science and Technology Creative Allied Project (CAP) under Grant NTM2371511 to J.S.Y.; 16. Hungarian Government project under Grant NKFIH-K 116263 and BIONANO GINOP-2.3.2-15–2016-00017 to A.G.; and 17. National Research Foundation of Korea under Grant NRF-2013M3A9B6075933 to H.J.A. □S This article contains supplemental Figures, Tables, and Discussion.

Funders	Funder number
FP7 GastricGlycoExplorer	621–2013-5895
National Research Council of Science and Technology Creative Allied Project
National Institutes of Health	822757, P41GM10349010
NIH Office of the Director	S10OD018530
National Institute of Diabetes and Digestive and Kidney Diseases	K01- DK101632
California Department of Fish and Game
Canadian Association of Palynologists	NTM2371511
Seventh Framework Programme	721815, 278535, 316929
ARC Centre for Nanoscale BioPhotonics	CE1401000003
Health Canada
Government of Canada
European Commission
Deutsche Forschungsgemeinschaft	FOR2509
National Natural Science Foundation of China	31671369, 31600650, 31770775D
Bundesministerium für Bildung und Forschung	031A557
Alberta Glycomics Centre
National Research Foundation of Korea	NRF-2013M3A9B6075933
Vetenskapsrådet	8266

Keywords

fluorescence
glycan
Glycomics
glycopeptide
glycoproteins
glycosylation
interlaboratory study
mass spectrometry
NISTmAb
reference antibody

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1074/mcp.RA119.001677

Persistent URL (handle)

Persistent link

Cite this

De Leoz, M. L. A., Duewer, D. L., Fung, A., Liu, L., Yau, H. K., Potter, O., Staples, G. O., Furuki, K., Frenkel, R., Hu, Y., Sosic, Z., Zhang, P., Altmann, F., Gru Nwald-Grube, C., Shao, C., Zaia, J., Evers, W., Pengelley, S., Suckau, D., ... Stein, S. E. (2020). NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods. MCP : Molecular & cellular proteomics, 19(1), 11-30. https://doi.org/10.1074/mcp.RA119.001677

@article{17701a3d41014ca58542afe13d8b1957,

title = "NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods",

abstract = "Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods.",

keywords = "fluorescence, glycan, Glycomics, glycopeptide, glycoproteins, glycosylation, interlaboratory study, mass spectrometry, NISTmAb, reference antibody",

author = "{De Leoz}, {Maria Lorna A.} and Duewer, {David L.} and Adam Fung and Lily Liu and Yau, {Hoi Kei} and Oscar Potter and Staples, {Gregory O.} and Kenichiro Furuki and Ruth Frenkel and Yunli Hu and Zoran Sosic and Peiqing Zhang and Friedrich Altmann and {Gru Nwald-Grube}, Clemens and Chun Shao and Joseph Zaia and Waltraud Evers and Stuart Pengelley and Detlev Suckau and Anja Wiechmann and Anja Resemann and Wolfgang Jabs and Alain Beck and Froehlich, {John W.} and Chuncui Huang and Yan Li and Yaming Liu and Shiwei Sun and Yaojun Wang and Youngsuk Seo and An, {Hyun Joo} and Reichardt, {Niels Christian} and Ruiz, {Juan Echevarria} and Stephanie Archer-Hartmann and Parastoo Azadi and Len Bell and Zsuzsanna Lakos and Yanming An and Cipollo, {John F.} and Maja Pucic-Bakovic and Jerko {\v S}tambuk and Gordan Lauc and Xu Li and Wang, {Peng George} and Andreas Bock and Ren{\'e} Hennig and Erdmann Rapp and Marybeth Creskey and Cyr, {Terry D.} and Miyako Nakano and Taiki Sugiyama and Leung, {Pui King Amy} and Pawe{\l} Link-Lenczowski and Jolanta Jaworek and Shuang Yang and Hui Zhang and Tim Kelly and Song Klapoetke and Rui Cao and Kim, {Jin Young} and Lee, {Hyun Kyoung} and Lee, {Ju Yeon} and Yoo, {Jong Shin} and Kim, {Sa Rang} and Suh, {Soo Kyung} and {de Haan}, Noortje and David Falck and Lageveen-Kammeijer, {Guinevere S.M.} and Manfred Wuhrer and Emery, {Robert J.} and Kozak, {Radoslaw P.} and Liew, {Li Phing} and Louise Royle and Urbanowicz, {Paulina A.} and Packer, {Nicolle H.} and Xiaomin Song and Arun Everest-Dass and Erika Lattov{\'a} and Samanta Cajic and Kathirvel Alagesan and Daniel Kolarich and Toyin Kasali and Viv Lindo and Yuetian Chen and Kudrat Goswami and Brian Gau and Ravi Amunugama and Richard Jones and Stroop, {Corn{\'e} J.M.} and Koichi Kato and Hirokazu Yagi and Sachiko Kondo and Yuen, {C. T.} and Akira Harazono and Xiaofeng Shi and Magnelli, {Paula E.} and Kasper, {Brian T.} and Lara Mahal and Harvey, {David J.} and Roisin O'Flaherty and Rudd, {Pauline M.} and Radka Saldova and Hecht, {Elizabeth S.} and Muddiman, {David C.} and Jichao Kang and Prachi Bhoskar and Daniele Menard and Andrew Saati and Christine Merle and Steven Mast and Sam Tep and Jennie Truong and Takashi Nishikaze and Sadanori Sekiya and Aaron Shafer and Sohei Funaoka and Masaaki Toyoda and {de Vreugd}, Peter and Cassie Caron and Pralima Pradhan and Tan, {Niclas Chiang} and Yehia Mechref and Sachin Patil and Rohrer, {Jeffrey S.} and Ranjan Chakrabarti and Disha Dadke and Mohammedazam Lahori and Chunxia Zou and Christopher Cairo and B{\'e}la Reiz and Whittal, {Randy M.} and Lebrilla, {Carlito B.} and Lauren Wu and Andras Guttman and Marton Szigeti and Kremkow, {Benjamin G.} and Lee, {Kelvin H.} and Carina Sihlbom and Barbara Adamczyk and Chunsheng Jin and Karlsson, {Niclas G.} and Jessica {\"O}rnros and G{\"o}ran Larson and Jonas Nilsson and Bernd Meyer and Alena Wiegandt and Emy Komatsu and Helene Perreault and Bodnar, {Edward D.} and Nassur Said and Francois, {Yannis Nicolas} and Emmanuelle Leize-Wagner and Sandra Maier and Anne Zeck and Heck, {Albert J.R.} and Yang Yang and Rob Haselberg and Yu, {Ying Qing} and William Alley and Leone, {Joseph W.} and Hua Yuan and Stein, {Stephen E.}",

year = "2020",

month = jan,

day = "1",

doi = "10.1074/mcp.RA119.001677",

language = "English",

volume = "19",

pages = "11--30",

journal = "MCP : Molecular & cellular proteomics",

issn = "1535-9484",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "1",

}

De Leoz, MLA, Duewer, DL, Fung, A, Liu, L, Yau, HK, Potter, O, Staples, GO, Furuki, K, Frenkel, R, Hu, Y, Sosic, Z, Zhang, P, Altmann, F, Gru Nwald-Grube, C, Shao, C, Zaia, J, Evers, W, Pengelley, S, Suckau, D, Wiechmann, A, Resemann, A, Jabs, W, Beck, A, Froehlich, JW, Huang, C, Li, Y, Liu, Y, Sun, S, Wang, Y, Seo, Y, An, HJ, Reichardt, NC, Ruiz, JE, Archer-Hartmann, S, Azadi, P, Bell, L, Lakos, Z, An, Y, Cipollo, JF, Pucic-Bakovic, M, Štambuk, J, Lauc, G, Li, X, Wang, PG, Bock, A, Hennig, R, Rapp, E, Creskey, M, Cyr, TD, Nakano, M, Sugiyama, T, Leung, PKA, Link-Lenczowski, P, Jaworek, J, Yang, S, Zhang, H, Kelly, T, Klapoetke, S, Cao, R, Kim, JY, Lee, HK, Lee, JY, Yoo, JS, Kim, SR, Suh, SK, de Haan, N, Falck, D, Lageveen-Kammeijer, GSM, Wuhrer, M, Emery, RJ, Kozak, RP, Liew, LP, Royle, L, Urbanowicz, PA, Packer, NH, Song, X, Everest-Dass, A, Lattová, E, Cajic, S, Alagesan, K, Kolarich, D, Kasali, T, Lindo, V, Chen, Y, Goswami, K, Gau, B, Amunugama, R, Jones, R, Stroop, CJM, Kato, K, Yagi, H, Kondo, S, Yuen, CT, Harazono, A, Shi, X, Magnelli, PE, Kasper, BT, Mahal, L, Harvey, DJ, O'Flaherty, R, Rudd, PM, Saldova, R, Hecht, ES, Muddiman, DC, Kang, J, Bhoskar, P, Menard, D, Saati, A, Merle, C, Mast, S, Tep, S, Truong, J, Nishikaze, T, Sekiya, S, Shafer, A, Funaoka, S, Toyoda, M, de Vreugd, P, Caron, C, Pradhan, P, Tan, NC, Mechref, Y, Patil, S, Rohrer, JS, Chakrabarti, R, Dadke, D, Lahori, M, Zou, C, Cairo, C, Reiz, B, Whittal, RM, Lebrilla, CB, Wu, L, Guttman, A, Szigeti, M, Kremkow, BG, Lee, KH, Sihlbom, C, Adamczyk, B, Jin, C, Karlsson, NG, Örnros, J, Larson, G, Nilsson, J, Meyer, B, Wiegandt, A, Komatsu, E, Perreault, H, Bodnar, ED, Said, N, Francois, YN, Leize-Wagner, E, Maier, S, Zeck, A, Heck, AJR, Yang, Y, Haselberg, R, Yu, YQ, Alley, W, Leone, JW, Yuan, H & Stein, SE 2020, 'NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods', MCP : Molecular & cellular proteomics, vol. 19, no. 1, pp. 11-30. https://doi.org/10.1074/mcp.RA119.001677

TY - JOUR

T1 - NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies

T2 - Comparison of Results from Diverse Analytical Methods

AU - De Leoz, Maria Lorna A.

AU - Duewer, David L.

AU - Fung, Adam

AU - Liu, Lily

AU - Yau, Hoi Kei

AU - Potter, Oscar

AU - Staples, Gregory O.

AU - Furuki, Kenichiro

AU - Frenkel, Ruth

AU - Hu, Yunli

AU - Sosic, Zoran

AU - Zhang, Peiqing

AU - Altmann, Friedrich

AU - Gru Nwald-Grube, Clemens

AU - Shao, Chun

AU - Zaia, Joseph

AU - Evers, Waltraud

AU - Pengelley, Stuart

AU - Suckau, Detlev

AU - Wiechmann, Anja

AU - Resemann, Anja

AU - Jabs, Wolfgang

AU - Beck, Alain

AU - Froehlich, John W.

AU - Huang, Chuncui

AU - Li, Yan

AU - Liu, Yaming

AU - Sun, Shiwei

AU - Wang, Yaojun

AU - Seo, Youngsuk

AU - An, Hyun Joo

AU - Reichardt, Niels Christian

AU - Ruiz, Juan Echevarria

AU - Archer-Hartmann, Stephanie

AU - Azadi, Parastoo

AU - Bell, Len

AU - Lakos, Zsuzsanna

AU - An, Yanming

AU - Cipollo, John F.

AU - Pucic-Bakovic, Maja

AU - Štambuk, Jerko

AU - Lauc, Gordan

AU - Li, Xu

AU - Wang, Peng George

AU - Bock, Andreas

AU - Hennig, René

AU - Rapp, Erdmann

AU - Creskey, Marybeth

AU - Cyr, Terry D.

AU - Nakano, Miyako

AU - Sugiyama, Taiki

AU - Leung, Pui King Amy

AU - Link-Lenczowski, Paweł

AU - Jaworek, Jolanta

AU - Yang, Shuang

AU - Zhang, Hui

AU - Kelly, Tim

AU - Klapoetke, Song

AU - Cao, Rui

AU - Kim, Jin Young

AU - Lee, Hyun Kyoung

AU - Lee, Ju Yeon

AU - Yoo, Jong Shin

AU - Kim, Sa Rang

AU - Suh, Soo Kyung

AU - de Haan, Noortje

AU - Falck, David

AU - Lageveen-Kammeijer, Guinevere S.M.

AU - Wuhrer, Manfred

AU - Emery, Robert J.

AU - Kozak, Radoslaw P.

AU - Liew, Li Phing

AU - Royle, Louise

AU - Urbanowicz, Paulina A.

AU - Packer, Nicolle H.

AU - Song, Xiaomin

AU - Everest-Dass, Arun

AU - Lattová, Erika

AU - Cajic, Samanta

AU - Alagesan, Kathirvel

AU - Kolarich, Daniel

AU - Kasali, Toyin

AU - Lindo, Viv

AU - Chen, Yuetian

AU - Goswami, Kudrat

AU - Gau, Brian

AU - Amunugama, Ravi

AU - Jones, Richard

AU - Stroop, Corné J.M.

AU - Kato, Koichi

AU - Yagi, Hirokazu

AU - Kondo, Sachiko

AU - Yuen, C. T.

AU - Harazono, Akira

AU - Shi, Xiaofeng

AU - Magnelli, Paula E.

AU - Kasper, Brian T.

AU - Mahal, Lara

AU - Harvey, David J.

AU - O'Flaherty, Roisin

AU - Rudd, Pauline M.

AU - Saldova, Radka

AU - Hecht, Elizabeth S.

AU - Muddiman, David C.

AU - Kang, Jichao

AU - Bhoskar, Prachi

AU - Menard, Daniele

AU - Saati, Andrew

AU - Merle, Christine

AU - Mast, Steven

AU - Tep, Sam

AU - Truong, Jennie

AU - Nishikaze, Takashi

AU - Sekiya, Sadanori

AU - Shafer, Aaron

AU - Funaoka, Sohei

AU - Toyoda, Masaaki

AU - de Vreugd, Peter

AU - Caron, Cassie

AU - Pradhan, Pralima

AU - Tan, Niclas Chiang

AU - Mechref, Yehia

AU - Patil, Sachin

AU - Rohrer, Jeffrey S.

AU - Chakrabarti, Ranjan

AU - Dadke, Disha

AU - Lahori, Mohammedazam

AU - Zou, Chunxia

AU - Cairo, Christopher

AU - Reiz, Béla

AU - Whittal, Randy M.

AU - Lebrilla, Carlito B.

AU - Wu, Lauren

AU - Guttman, Andras

AU - Szigeti, Marton

AU - Kremkow, Benjamin G.

AU - Lee, Kelvin H.

AU - Sihlbom, Carina

AU - Adamczyk, Barbara

AU - Jin, Chunsheng

AU - Karlsson, Niclas G.

AU - Örnros, Jessica

AU - Larson, Göran

AU - Nilsson, Jonas

AU - Meyer, Bernd

AU - Wiegandt, Alena

AU - Komatsu, Emy

AU - Perreault, Helene

AU - Bodnar, Edward D.

AU - Said, Nassur

AU - Francois, Yannis Nicolas

AU - Leize-Wagner, Emmanuelle

AU - Maier, Sandra

AU - Zeck, Anne

AU - Heck, Albert J.R.

AU - Yang, Yang

AU - Haselberg, Rob

AU - Yu, Ying Qing

AU - Alley, William

AU - Leone, Joseph W.

AU - Yuan, Hua

AU - Stein, Stephen E.

PY - 2020/1/1

Y1 - 2020/1/1

N2 - Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods.

AB - Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods.

KW - fluorescence

KW - glycan

KW - Glycomics

KW - glycopeptide

KW - glycoproteins

KW - glycosylation

KW - interlaboratory study

KW - mass spectrometry

KW - NISTmAb

KW - reference antibody

UR - http://www.scopus.com/inward/record.url?scp=85076683169&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85076683169&partnerID=8YFLogxK

U2 - 10.1074/mcp.RA119.001677

DO - 10.1074/mcp.RA119.001677

M3 - Article

C2 - 31591262

AN - SCOPUS:85076683169

SN - 1535-9484

VL - 19

SP - 11

EP - 30

JO - MCP : Molecular & cellular proteomics

JF - MCP : Molecular & cellular proteomics

IS - 1

ER -

NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods

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