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

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.

Adamczyk B, Alagesan K, Alley W, Altmann F, Amunugama R, An HJ, An Y, Archer-Hartmann S, Azadi P, Beck A, Bell L, Bhoskar P, Bock A, Bodnar ED, Cairo C, Cajic S, Cao R, Caron C, Chakrabarti R, Chen Y, Cipollo JF, Creskey M, Cyr TD, Dadke D, De Leoz MLA, Duewer DL, Emery RJ, Everest-Dass A, Evers W, Falck D, Francois YN, Frenkel R, Froehlich JW, Funaoka S, Fung A, Furuki K, Gau B, Goswami K, Grunwald-Grube C, Guttman A, Harazono A, Harvey DJ, Haselberg R, Hecht ES, Heck AJR, Hennig R, Hu Y, Huang C, Jabs W, Jaworek J, Jin C, Jones R, Kang J, Karlsson NG, Kasali T, Kasper BT, Kato K, Kelly T, Kim JY, Kim SR, Klapoetke S, Kolarich D, Komatsu E, Kondo S, Kozak RP, Kremkow BG, Lageveen-Kammeijer GSM, Lahori M, Lakos Z, Larson G, Lattová E, Lauc G, Lebrilla CB, Lee HK, Lee JY, Lee KH, Leize-Wagner E, Leone JW, Leung PA, Li X, Li Y, Liew LP, Lindo V, Link-Lenczowski P, Liu L, Liu Y, Magnelli PE, Mahal L, Maier S, Mast S, Mechref Y, Menard D, Merle C, Meyer B, Muddiman DC, Nakano M, Nilsson J, Nishikaze T, O'Flaherty R, Packer NH, Patil S, Pengelley S, Perreault H, Potter O, Pradhan P, Pucic-Bakovic M, Rapp E, Reichardt NC, Reiz B, Resemann A, Rohrer JS, Royle L, Rudd PM, Ruiz JE, Saati A, Said N, Saldova R, Sekiya S, Seo Y, Shafer A, Shao C, Shi X, Sihlbom C, Song X, Sosic Z, Staples GO, Stein SE, Stroop CJM, Suckau D, Sugiyama T, Suh SK, Sun S, Szigeti M, Tan NC, Tep S, Toyoda M, Truong J, Urbanowicz PA, Wang PG, Wang Y, Whittal RM, Wiechmann A, Wiegandt A, Wu L, Wuhrer M, Yagi H, Yang S, Yang Y, Yau HK, Yoo JS, Yu YQ, Yuan H, Yuen CT, Zaia J, Zeck A, Zhang H, Zhang P, Zou C, de Haan N, de Vreugd P, Örnros J, Štambuk J


Mol Cell Proteomics, 2020, 19 (1)

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