De Leoz, Maria Lorna A. and Duewer, David L and Fung, Adam and Liu, Lily and Kei Yau, Hoi and Potter, Oscar and Staples, Gregory O and Furuki, Kenichiro and Frenkel, Ruth and Hu, Yunli and Socic, Zoran and Zhang, Peiqing and Altmann, Friedrich and Grunwald-Grube, Clemens and Shao, Chun and Zaia, Joseph and Evers, Waltraud and Pengelley, Stuart and Detlev, Suckau and Wiechmann, Anja and Resemann, Anja and Jabs, Wolfgang and Beck, Alain and Froehlich, John W and Huang, Chuncui and Yan, Li and Yaming, Liu and Sun, Shiwei and Wang, Yaojun and Seo, Youngsuk and An, Hyun Joo and Reichardt, Niels-Christian and Ruiz, Juan Echevarria and Archer-Hartmann, Stephanie and Azadi, Parastoo and Bell, Len and Lakos, Zsuzsanna and An, Yanming and Cipollo, John F and Pucic-Bakovic, Maja and Stambuk, Jerko and Lauc, Gordan and Li, Xu and Wang, Peng George and Bock, Andreas and Hennig, Rene and Rapp, Erdmann and Creskey, Marybeth and Cyr, Terry D and Nakano, Miyako and Sugiyama, Taiki and Leung, Pui-King Amy and Link-Lenczowski, Pawel and Jaworek, Jolanta and Yoo, Jong Shin and Kim, Sa-Rang and Suh, Soo-Kyung and de Haan, Noortje and Falck, David and Lageveen-Kammeijer, Guinevere S. M. and Wuhrer, Manfred and Emery, Robert J and Liew, Li Phing and Royle, Louise and Urbanowicz, Paulina A and Packer, Nicolle H and Song, Xiaomin and Everest-Dass, Arun and Lattova, Erika and Cajic, Samanta and Alagesan, Kathirvel and Kolarich, Daniel and Kasali, Toyin and Lindo, Viv and Chen, Yuetian and Goswami, Kudrat and Gau, Brian and Amunugama, Ravi and Jones, Richard and Stroop, Corné J M and Kato, Koichi and Yagi, Hirokazu and Kondo, Sachiko and Yuen, C T and Harazono, Akira and Shi, Xiafeng and Magnelli, Paula and Kasper, Brian T and Mahai, Lara and Harvey, David J and O'Flaherty, Roisin and Rudd, Pauline M. and Saldova, Radka and Hecht, Elizabeth S and Muddiman, David C and Kang, Jichao and Bhoskar, Prachi and Menard, Daniele and Saati, Andrew and Merle, Christine and Mast, Steven and Tep, Sam and Truong, Jennie and Nishikaze, Takashi and Sekiya, Sadanori and Shafer, Aaron and Funaoka, Sohei and Toyoda, Masaaki and de Vreugd, Peter and Caron, Cassie and Pradhan, Pralima and Tan, Niclas Chiang and Mechref, Yehia and Patil, Sachin and Rohrer, Jeffrey S and Chakrabarti, Ranjan and Dadke, Disha and Lahori, Mohammedazam and Zou, Chunxia and Cairo, Christopher and Reiz, Béla and Whittal, Randy M and Lebrilla, Carlito B and Wu, Lauren and Guttman, Andras and Szigeti, Marton and Kremkow, Benjamin G and Lee, Kevin H and Sihlbom, Carina and Adamczyk, Barbara and Jin, Chunsheng and Karlsson, Niclas G and Omros, Jessica and Larson, Goran and Nilsson, Jonas and Meyer, Bernd and Alena, Wiegandt and Komatsu, Emy and Perreault, Helene and Bodnar, Edward D and Said, Nassur and Francois, Yannis-Nicolas and Leize-Wagner, Emmanuelle and Maier, Sandra and Zeck, Anne and Heck, Albert J R and Yang, Yang and Haselberg, Rob and Qing Yu, Ying and Alley, William and Leone, Joseph W and Yuan, Hua and Stein, Stephen E (2020) NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods. Molecular and Cellular Proteomics (MCP), 19 (1). pp. 11-30. ISSN 1535-9476

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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.

Item Type:	Article
Keywords:	Glycomics; mass spectrometry; fluorescence; glycosylation; glycoproteins; glycan; glycopeptide; interlaboratory study; NISTmAb; reference antibody;
Academic Unit:	Faculty of Science and Engineering > Chemistry
Item ID:	15028
Identification Number:	https://doi.org/10.1074/mcp.RA119.001677
Depositing User:	Roisin O'Flaherty
Date Deposited:	16 Nov 2021 14:43
Journal or Publication Title:	Molecular and Cellular Proteomics (MCP)
Publisher:	Elsevier
Refereed:	Yes
URI:	Publisher
Use Licence:	This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

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