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


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    De Leoz, Maria Lorna A., Duewer, David L, Fung, Adam, Liu, Lily, Kei Yau, Hoi, Potter, Oscar, Staples, Gregory O, Furuki, Kenichiro, Frenkel, Ruth, Hu, Yunli, Socic, Zoran, Zhang, Peiqing, Altmann, Friedrich, Grunwald-Grube, Clemens, Shao, Chun, Zaia, Joseph, Evers, Waltraud, Pengelley, Stuart, Detlev, Suckau, Wiechmann, Anja, Resemann, Anja, Jabs, Wolfgang, Beck, Alain, Froehlich, John W, Huang, Chuncui, Yan, Li, Yaming, Liu, Sun, Shiwei, Wang, Yaojun, Seo, Youngsuk, An, Hyun Joo, Reichardt, Niels-Christian, Ruiz, Juan Echevarria, Archer-Hartmann, Stephanie, Azadi, Parastoo, Bell, Len, Lakos, Zsuzsanna, An, Yanming, Cipollo, John F, Pucic-Bakovic, Maja, Stambuk, Jerko, Lauc, Gordan, Li, Xu, Wang, Peng George, Bock, Andreas, Hennig, Rene, Rapp, Erdmann, Creskey, Marybeth, Cyr, Terry D, Nakano, Miyako, Sugiyama, Taiki, Leung, Pui-King Amy, Link-Lenczowski, Pawel, Jaworek, Jolanta, Yoo, Jong Shin, Kim, Sa-Rang, Suh, Soo-Kyung, de Haan, Noortje, Falck, David, Lageveen-Kammeijer, Guinevere S. M., Wuhrer, Manfred, Emery, Robert J, Liew, Li Phing, Royle, Louise, Urbanowicz, Paulina A, Packer, Nicolle H, Song, Xiaomin, Everest-Dass, Arun, Lattova, Erika, Cajic, Samanta, Alagesan, Kathirvel, Kolarich, Daniel, Kasali, Toyin, Lindo, Viv, Chen, Yuetian, Goswami, Kudrat, Gau, Brian, Amunugama, Ravi, Jones, Richard, Stroop, Corné J M, Kato, Koichi, Yagi, Hirokazu, Kondo, Sachiko, Yuen, C T, Harazono, Akira, Shi, Xiafeng, Magnelli, Paula, Kasper, Brian T, Mahai, Lara, Harvey, David J, O'Flaherty, Roisin, Rudd, Pauline M., Saldova, Radka, Hecht, Elizabeth S, Muddiman, David C, Kang, Jichao, Bhoskar, Prachi, Menard, Daniele, Saati, Andrew, Merle, Christine, Mast, Steven, Tep, Sam, Truong, Jennie, Nishikaze, Takashi, Sekiya, Sadanori, Shafer, Aaron, Funaoka, Sohei, Toyoda, Masaaki, de Vreugd, Peter, Caron, Cassie, Pradhan, Pralima, Tan, Niclas Chiang, Mechref, Yehia, Patil, Sachin, Rohrer, Jeffrey S, Chakrabarti, Ranjan, Dadke, Disha, Lahori, Mohammedazam, Zou, Chunxia, Cairo, Christopher, Reiz, Béla, Whittal, Randy M, Lebrilla, Carlito B, Wu, Lauren, Guttman, Andras, Szigeti, Marton, Kremkow, Benjamin G, Lee, Kevin H, Sihlbom, Carina, Adamczyk, Barbara, Jin, Chunsheng, Karlsson, Niclas G, Omros, Jessica, Larson, Goran, Nilsson, Jonas, Meyer, Bernd, Alena, Wiegandt, Komatsu, Emy, Perreault, Helene, Bodnar, Edward D, Said, Nassur, Francois, Yannis-Nicolas, Leize-Wagner, Emmanuelle, Maier, Sandra, Zeck, Anne, Heck, Albert J R, Yang, Yang, Haselberg, Rob, Qing Yu, Ying, Alley, William, Leone, Joseph W, 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: 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
    Related URLs:
    URI: https://mural.maynoothuniversity.ie/id/eprint/15028
    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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