Interlaboratory study for characterizing monoclonal antibodies by top-down and middle-down mass spectrometry

Autor: Sam Hughes, Nicolas L. Young, David Clarke, Frank Sobott, Anja Resemann, Kristina Srzentić, Kim F. Haselmann, Detlev Suckau, Dina L. Bai, Young Ah Goo, Christian Malosse, Mathieu Dupré, Sylvester M. Greer, Neil R. Quebbemann, Ziqing Lin, Jared B. Shaw, Alain Beck, Yury O. Tsybin, Stuart Pengelley, Timothy K. Toby, Lidong He, Paul O. Danis, Henrique S. Seckler, Robert Anthony D’Ippolito, Natalia Gasilova, Jeffrey N. Agar, Donald F. Hunt, Jennifer S. Brodbelt, Matthew V. Holt, Simone Nicolardi, Joseph A. Loo, Yuri E. M. van der Burgt, Nicholas D. Schmitt, Laure Menin, Robert J. Millikin, Ljiljana Paša-Tolić, David R. Goodlett, Mowei Zhou, Joshua D. Hinkle, Michael R. Shortreed, Christopher L. Hendrickson, Wendy Sandoval, Richa Sarin, Jeffrey Shabanowitz, Alan G. Marshall, Anton N. Kozhinov, Neil L. Kelleher, Chad R. Weisbrod, Lissa C. Anderson, Julia Chamot-Rooke, Yunqiu Chen, John R. Yates, Luca Fornelli, Konstantin O. Nagornov, Lloyd M. Smith, Sneha Chatterjee, Ying Ge, Sung Hwan Yoon, Jolene K. Diedrich, Norelle C. Wildburger
Přispěvatelé: Centre de Recherche Pierre Fabre (Centre de R&D Pierre Fabre), PIERRE FABRE, Institut Pasteur [Paris], Institut Pasteur [Paris] (IP)
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Proteomics
medicine.drug_class
[SDV]Life Sciences [q-bio]
Computational biology
010402 general chemistry
Tandem mass spectrometry
Monoclonal antibody
Mass spectrometry
01 natural sciences
Article
Antibodies
Mass Spectrometry
FTMS
Analytical Chemistry
Mice
Medicinal and Biomolecular Chemistry
Structural Biology
Monoclonal
intact mass measurement
tandem mass spectrometry
medicine
MS/MS
Animals
Humans
Biology
Spectroscopy
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]

Chemistry
010401 analytical chemistry
Therapeutic protein
Antibodies
Monoclonal

Complementarity Determining Regions
0104 chemical sciences
3. Good health
Fourier transform mass spectrometry
Ion dissociation
glycoform
Therapeutic antibody
Biotechnology
Physical Chemistry (incl. Structural)
Zdroj: Journal of The American Society for Mass Spectrometry
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), 2020, 31 (9), pp.1783-1802. ⟨10.1021/jasms.0c00036⟩
Journal of the American Society for Mass Spectrometry
Journal of the American Society for Mass Spectrometry, vol 31, iss 9
Journal of The American Society for Mass Spectrometry, 31(9), 1783-1802. AMER CHEMICAL SOC
J Am Soc Mass Spectrom
Journal of The American Society for Mass Spectrometry, 2020, 31 (9), pp.1783-1802. ⟨10.1021/jasms.0c00036⟩
ISSN: 1044-0305
1879-1123
DOI: 10.1021/jasms.0c00036⟩
Popis: International audience; The Consortium for Top-Down Proteomics (www.topdownproteomics.org) launched the present study to assess the current state of top-down mass spectrometry (TD MS) and middle-down mass spectrometry (MD MS) for characterizing monoclonal antibody (mAb) primary structures, including their modifications. To meet the needs of the rapidly growing therapeutic antibody market, it is important to develop analytical strategies to characterize the heterogeneity of a therapeutic product's primary structure accurately and reproducibly. The major objective of the present study is to determine whether current TD/MD MS technologies and protocols can add value to the more commonly employed bottom-up (BU) approaches with regard to confirming protein integrity, sequencing variable domains, avoiding artifacts, and revealing modifications and their locations. We also aim to gather information on the common TD/MD MS methods and practices in the field. A panel of three mAbs was selected and centrally provided to 20 laboratories worldwide for the analysis: Sigma mAb standard (SiLuLite), NIST mAb standard, and the therapeutic mAb Herceptin (trastuzumab). Various MS instrument platforms and ion dissociation techniques were employed. The present study confirms that TD/MD MS tools are available in laboratories worldwide and provide complementary information to the BU approach that can be crucial for comprehensive mAb characterization. The current limitations, as well as possible solutions to overcome them, are also outlined. A primary limitation revealed by the results of the present study is that the expert knowledge in both experiment and data analysis is indispensable to practice TD/MD MS.
Databáze: OpenAIRE