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 Grunwald-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 journalArticle

6 Scopus citations

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 submit-ted 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 communityderived 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 languageEnglish (US)
Pages (from-to)11-30
Number of pages20
JournalMolecular and Cellular Proteomics
Volume19
Issue number1
DOIs
StatePublished - Jan 1 2020

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'NIST interlaboratory study on glycosylation analysis of monoclonal antibodies: Comparison of results from diverse analytical methods'. Together they form a unique fingerprint.

  • 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., Grunwald-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. Molecular and Cellular Proteomics, 19(1), 11-30. https://doi.org/10.1074/mcp.RA119.001677