1. NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies
- Author
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Miyako Nakano, Alena Wiegandt, Yunli Hu, Viv Lindo, Paulina A. Urbanowicz, Zsuzsanna Lakos, Cassie Caron, Song Klapoetke, Niels Christian Reichardt, Niclas Chiang Tan, Sandra Maier, Rene Hennig, Marton Szigeti, Ju Yeon Lee, Ying Qing Yu, Gregory O. Staples, Sachin Patil, Jolanta Jaworek, Waltraud Evers, Benjamin G. Kremkow, Youngsuk Seo, Kathirvel Alagesan, Yuetian Chen, Gordan Lauc, David L. Duewer, Yang Yang, Daniele Menard, Hyun Joo An, Tim Kelly, Stephen E. Stein, Joseph W. Leone, Anja Wiechmann, Ravi Amunugama, Peng George Wang, Clemens Grunwald-Grube, Maria Lorna A. De Leoz, Göran Larson, Rob Haselberg, Samanta Cajic, Stephanie A. Archer-Hartmann, Maja Pučić-Baković, Edward D. Bodnar, Pauline M. Rudd, Anja Resemann, Daniel Kolarich, Akira Harazono, Jeffrey S. Rohrer, Juan Echevarria Ruiz, Stuart Pengelley, Jong Shin Yoo, Arun V. Everest-Dass, Nicolle H. Packer, Steven W. Mast, William R. Alley, Erika Lattová, Anne Zeck, Corné J.M. Stroop, Radoslaw P. Kozak, Chun Shao, Alain Beck, Joseph Zaia, Erdmann Rapp, Lily Liu, Jennie Truong, Yaojun Wang, Christopher W. Cairo, Roisin O'Flaherty, Radka Saldova, Kudrat Goswami, Emy Komatsu, Jessica Örnros, Taiki Sugiyama, Prachi Bhoskar, Pralima Pradhan, Carlito B. Lebrilla, András Guttman, Christine Merle, Brian Kasper, Oscar G. Potter, Soo Kyung Suh, Li Phing Liew, Ranjan Chakrabarti, Terry D. Cyr, Sohei Funaoka, Masaaki Toyoda, Pui King Amy Leung, Toyin Kasali, Jerko Štambuk, Yanming An, Wolfgang Jabs, Bernd Meyer, Chunxia Zou, John F. Cipollo, Sa Rang Kim, Aaron Shafer, Randy M. Whittal, Jichao Kang, Albert J. R. Heck, Yehia Mechref, Hoi Kei Yau, Guinevere S. M. Lageveen-Kammeijer, Shiwei Sun, Kenichiro Furuki, Richard B. Jones, Béla Reiz, Niclas G. Karlsson, Mohammedazam Lahori, Xu Li, Barbara Adamczyk, Rui Cao, Lauren Wu, Koichi Kato, Detlev Suckau, Paweł Link-Lenczowski, Kelvin H. Lee, Xiaomin Song, Noortje de Haan, Ruth Frenkel, Adam Fung, Friedrich Altmann, Manfred Wuhrer, David Falck, Andreas Bock, Paula Magnelli, Brian Gau, Sachiko Kondo, Robert J. Emery, Chunsheng Jin, Louise Royle, David C. Muddiman, Hélène Perreault, John W. Froehlich, Disha Dadke, Peiqing Zhang, Lara K. Mahal, Takashi Nishikaze, Andrew Saati, Chuncui Huang, Hui Zhang, Carina Sihlbom, Parastoo Azadi, Jonas Nilsson, Yaming Liu, Yannis-Nicolas François, Nassur Said, Jin Young Kim, C. T. Yuen, Shuang Yang, Emmanuelle Leize-Wagner, David Harvey, Xiaofeng Shi, Yan Li, Hirokazu Yagi, Zoran Sosic, Elizabeth M. Hecht, Hua Yuan, Marybeth Creskey, Hyun Kyoung Lee, Sadanori Sekiya, Peter de Vreugd, Len Bell, Sam Tep, BioAnalytical Chemistry, AIMMS, Department of Plant and Microbial Biology, University of California, Laboratory of Infrared Material and Devices, Ningbo University (NBU), University of Natural Resources and Life Sciences (BOKU), Bruker Daltonik GmbH, Bruker Daltonik, Centre d'Immunologie Pierre Fabre, Xinjiang Agriculture University, Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), Instituto de Salud Carlos III [Madrid] (ISC)-ministerio de ciencia e innovacion, Complex Carbohydrate Research Center, University of Georgia [USA], GENOS, Universität Duisburg-Essen [Essen], Max Planck Institute for Dynamics of Complex Technical Systems, Max-Planck-Gesellschaft, Section de mathématiques [Genève], Université de Genève (UNIGE), Department of Computer Science [York] (CS-YORK), University of York [York, UK], State Key Laboratory of Hybrid Rice, Department of Genetics, College of Life Sciences, Wuhan University, LeidenUniversity Medical Center, University College Dublin [Dublin] (UCD), Texas A&M University System, College of Engineering and Computer Science, Australian National University (ANU), Unité de Recherche sur les Maladies Cardiovasculaires, du Métabolisme et de la Nutrition = Institute of cardiometabolism and nutrition (ICAN), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [AP-HP], Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), University of Edinburgh, University of Alberta, Department of Biological Sciences, Mass Spectrometry Facility, University of Alberta-Department of Chemistry, Volvo Car Corporation, Centre for Research in Intelligent Systems, Monash University [Clayton], Department of Chemistry [Winnipeg, MB, Canada], University of Manitoba [Winnipeg], Department of Chemistry [Winnipeg, Manitoba, Canada], Université de Strasbourg (UNISTRA), Laboratoire de synthèses métallo-induites, Dynamique et structure moléculaire par spectrométrie de masse (LDSM2), School of Mechanics and Engineering [Chengdu], Southwest Jiaotong University (SWJTU), School of Management and Economics [University of Electronic Science and Technology of China], and University of Electronic Science and Technology of China (UESTC)
- Subjects
Proteomics ,PROTEIN ,fluerescence ,Biochemistry ,reference antibody ,THERAPEUTIC ANTIBODIES ,Biopharmaceutics ,Analytical Chemistry ,chemistry.chemical_compound ,Biological sciences ,Glycomics ,NISTaAb ,Analysis method ,ComputingMilieux_MISCELLANEOUS ,glycoproteins ,mass spectrometry ,chemistry.chemical_classification ,0303 health sciences ,glycan ,interlaboratory study ,030302 biochemistry & molecular biology ,Glycopeptides ,Antibodies, Monoclonal ,3. Good health ,glycomics ,fluorescence ,glycosylation ,glycopeptide ,NISTmAb ,lipids (amino acids, peptides, and proteins) ,Protein glycosylation ,Glycan ,Glycosylation ,QUANTITATION ,medicine.drug_class ,Computational biology ,Biology ,Monoclonal antibody ,03 medical and health sciences ,GLYCOMIC ANALYSIS ,SDG 3 - Good Health and Well-being ,Polysaccharides ,[CHIM.ANAL]Chemical Sciences/Analytical chemistry ,Report ,medicine ,Humans ,LC-MS/MS ,Molecular Biology ,030304 developmental biology ,Biological Products ,IDENTIFICATION ,MASS-SPECTROMETRY ,PROFILES ,QUANTIFICATION ,carbohydrates (lipids) ,chemistry ,biology.protein ,Laboratories ,Glycoprotein ,Protein Processing, Post-Translational - Abstract
A broad-based interlaboratory study of glycosylation profiles of a reference and modified IgG antibody involving 103 reports from 76 laboratories., Graphical Abstract Highlights A broad-based interlaboratory study of the glycosylation of a reference antibody: NISTmAb. 103 reports were received from 76 diverse laboratories worldwide. Analysis involved two samples, the NISTmAb and an enzymatically modified sample, enabling within-lab separation of random and systematic errors using the “Youden two-sample” method. Consensus values were derived and similar performance across all experimental methods was noted., 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.
- Published
- 2020