J 2020

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

LEOZ DE, M.L.A., D.L. DUEWER, A. FUNG, L. LIU, H.K. YAU et. al.

Základní údaje

Originální název

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

Autoři

LEOZ DE, M.L.A., D.L. DUEWER, A. FUNG, L. LIU, H.K. YAU, O. POTTER, G.O. STAPLES, K. FURUKI, R. FRENKEL, Y.L. HU, Z. SOSIC, P.Q. ZHANG, F. ALTMANN, C. GRUNWALD-GRUBE, C. SHAO, J. ZAIA, W. EVERS, S. PENGELLEY, D. SUCKAU, A. WIECHMANN, A. RESEMANN, W. JABS, A. BECK, J.W. FROEHLICH, C.C. HUANG, Y. LI, Y.M. LIU, S.W. SUN, Y.J. WANG, Y. SEO, H.J. AN, N.C. REICHARDT, J.E. RUIZ, S. ARCHER-HARTMANN, P. AZADI, L. BELL, Z. LAKOS, Y.M. AN, J.F. CIPOLLO, M. PUCIC-BAKOVIC, J. STAMBUK, G. LAUC, X. LI, X. WANG, A. BOCK, R. HENNIG, E. RAPP, M. CRESKEY, T.D. CYR, M. NAKANO, T. SUGIYAMA, P.K.A. LEUNG, P. LINK-LENCZOWSKI, J. JAWOREK, S. YANG, H. ZHANG, T. KELLY, S. KLAPOETKE, R. CAO, J.Y. KIM, H.K. LEE, J.Y. LEE, J.S. YOO, S.R. KIM, S.K. SUH, N. DE HAAN, D. FALCK, G.S.M. LAGEVEEN-KAMMEIJER, M. WUHRER, R.J. EMERY, R.P. KOZAK, L.P. LIEW, L. ROYLE, P.A. URBANOWICZ, N.H. PACKER, X.M. SONG, A. EVEREST-DASS, Erika LATTOVÁ (703 Slovensko, garant, domácí), S. CAJIC, K. ALAGESAN, D. KOLARICH, T. KASALI, V. LINDO, Y. CHEN, K. GOSWAMI, B. GAU, R. AMUNUGAMA, R. JONES, C.J.M. STROOP, K. KATO, H. YAGI, S. KONDO, C.T. YUEN, A. HARAZONO, X.F. SHI, P.E. MAGNELLI, B.T. KASPER, L. MAHAL, D.J. HARVEY, R. FLAHERTY, P.M. RUDD, R. SALDOVA, E.S. HECHT, D.C. MUDDIMAN, J.C. KANG, P. BHOSKAR, D. MENARD, A. SAATI, C. MERLE, S. MAST, S. TEP, J. TRUONG, T. NISHIKAZE, S. SEKIYA, A. SHAFER, S. FUNAOKA, M. TOYODA, P. DE VREUGD, C. CARON, P. PRADHAN, N.C. TAN, Y. MECHREF, S. PATIL, J.S. ROHRER, R. CHAKRABARTI, D. DADKE, M. LAHORI, C.X. ZOU, C. CAIRO, B. REIZ, R.M. WHITTAL, C.B. LEBRILLA, L.R. WU, A. GUTTMAN, M. SZIGETI, B.G. KREMKOW, K.H. LEE, C. SIHLBOM, B. ADAMCZYK, C.S. JIN, N.G. KARLSSON, J. ORNROS, G. LARSON, J. NILSSON, B. MEYER, A. WIEGANDT, E. KOMATSU, H. PERREAULT, E.D. BODNAR, N. SAID, Y.N. FRANCOIS, E. LEIZE-WAGNER, S. MAIER, A. ZECK, A.J.R. HECK, Y. YANG, R. HASELBERG, Y.Q. YU, W. ALLEY, J.W. LEONE, H. YUAN a S.E. STEIN

Vydání

MOLECULAR & CELLULAR PROTEOMICS, BETHESDA, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2020, 1535-9476

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Impakt faktor

Impact factor: 5.911

Kód RIV

RIV/00216224:14740/20:00118336

Organizační jednotka

Středoevropský technologický institut

UT WoS

000518794300002

Klíčová slova anglicky

Glycomics; mass spectrometry; fluorescence; glycosylation; glycoproteins; glycan; glycopeptide; interlaboratory study; NISTmAb; reference antibody

Štítky

Příznaky

Mezinárodní význam, Recenzováno
Změněno: 6. 3. 2021 11:35, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

A broad-based interlaboratory study of glycosylation profiles of a reference and modified IgG antibody involving 103 reports from 76 laboratories. 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.