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Article ; Online: Integration of NMR Spectroscopy in an Analytical Workflow to Evaluate the Effects of Oxidative Stress on Abituzumab: Beyond the Fingerprint of mAbs

Cerofolini, Linda / Ravera, Enrico / Fischer, Christian / Trovato, Andrea / Sacco, Francesca / Palinsky, Wolf / Angiuoni, Gabriella / Fragai, Marco / Baroni, Fabio

Analytical Chemistry. 2023 June 06, v. 95, no. 24 p.9199-9206

2023

Abstract: The assessment of the higher-order structure (HOS) by NMR is a powerful methodology to characterize the structural features of biologics. Forced oxidative stress studies are used to investigate the stability profile, to develop pharmaceutical ... ...

Abstract	The assessment of the higher-order structure (HOS) by NMR is a powerful methodology to characterize the structural features of biologics. Forced oxidative stress studies are used to investigate the stability profile, to develop pharmaceutical formulations and analytical methods. Here, the effects of forced oxidative stress by H₂O₂ on the monoclonal antibody Abituzumab have been characterized by a multianalytical approach combining NMR spectroscopy, mass spectrometry, differential scanning calorimetry, surface plasmon resonance, computational tools, and bioassays. This integrated strategy has provided qualitative and semiquantitative characterization of the samples and information at residue level of the effects that oxidation has on the HOS of Abituzumab, correlating them to the loss of the biological activity.
Keywords	analytical chemistry ; bioactive properties ; calorimetry ; mass spectrometry ; monoclonal antibodies ; nuclear magnetic resonance spectroscopy ; oxidation ; oxidative stress ; surface plasmon resonance
Language	English
Dates of publication	2023-0606
Size	p. 9199-9206.
Publishing place	American Chemical Society
Document type	Article ; Online
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.3c00317
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Integration of NMR Spectroscopy in an Analytical Workflow to Evaluate the Effects of Oxidative Stress on Abituzumab: Beyond the Fingerprint of mAbs.

Cerofolini, Linda / Ravera, Enrico / Fischer, Christian / Trovato, Andrea / Sacco, Francesca / Palinsky, Wolf / Angiuoni, Gabriella / Fragai, Marco / Baroni, Fabio

Analytical chemistry

2023 Volume 95, Issue 24, Page(s) 9199–9206

Abstract	The assessment of the higher-order structure (HOS) by NMR is a powerful methodology to characterize the structural features of biologics. Forced oxidative stress studies are used to investigate the stability profile, to develop pharmaceutical formulations and analytical methods. Here, the effects of forced oxidative stress by H
MeSH term(s)	Hydrogen Peroxide ; Workflow ; Antibodies, Monoclonal/chemistry ; Magnetic Resonance Spectroscopy
Chemical Substances	Abituzumab (724QD330RD) ; Hydrogen Peroxide (BBX060AN9V) ; Antibodies, Monoclonal
Language	English
Publishing date	2023-06-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.3c00317
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Zs.A 4033: Show issues

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Article ; Online: Current views on N-glycolylneuraminic acid in therapeutic recombinant proteins.

Mastrangeli, Renato / Audino, Maria Concetta / Palinsky, Wolf / Broly, Hervé / Bierau, Horst

Trends in pharmacological sciences

2021 Volume 42, Issue 11, Page(s) 943–956

Abstract: The incorporation of the non-human N-glycolylneuraminic acid (Neu5Gc) in therapeutic recombinant proteins raises clinical concerns due to its immunogenic potential and the high prevalence of pre-existing anti-Neu5Gc antibodies in humans. The scientific ... ...

Abstract	The incorporation of the non-human N-glycolylneuraminic acid (Neu5Gc) in therapeutic recombinant proteins raises clinical concerns due to its immunogenic potential and the high prevalence of pre-existing anti-Neu5Gc antibodies in humans. The scientific literature is ambiguous regarding the actual impact of Neu5Gc-containing biotherapeutics as no severe adverse clinical manifestations were unequivocally attributed to Neu5Gc for currently marketed biotherapeutics. This review discusses structural and functional considerations of Neu5Gc-containing glycans regarding the potential impact on drug clearance, their recognition by pre-existing antibodies, and recent hypotheses regarding the tolerance to low Neu5Gc levels. Furthermore, it provides recommendations regarding the standardization of analysis and reporting, analytical aspects relevant for assessing risks associated with Neu5Gc-containing biotherapeutics, and approaches to minimize Neu5Gc incorporation in recombinant protein manufacturing.
MeSH term(s)	Antibodies ; Humans ; Neuraminic Acids/chemistry ; Recombinant Proteins/chemistry ; Recombinant Proteins/therapeutic use
Chemical Substances	Antibodies ; Neuraminic Acids ; Recombinant Proteins ; N-glycolylneuraminic acid (1113-83-3)
Language	English
Publishing date	2021-09-17
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	282846-7
ISSN	1873-3735 ; 0165-6147
ISSN (online)	1873-3735
ISSN	0165-6147
DOI	10.1016/j.tips.2021.08.004
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Article ; Online: How unique is interferon-β within the type I interferon family?

Mastrangeli, Renato / Palinsky, Wolf / Bierau, Horst

Cytokine

2018 Volume 111, Page(s) 206–208

Abstract: All type I interferons share structural homology and bind to a common heterodimeric receptor consisting of the IFNAR1 and IFNAR2 subunits, which are expressed on most cell types. Although binding to the same receptor pair, they evoke a broad range of ... ...

Abstract	All type I interferons share structural homology and bind to a common heterodimeric receptor consisting of the IFNAR1 and IFNAR2 subunits, which are expressed on most cell types. Although binding to the same receptor pair, they evoke a broad range of activities within the cell affecting the expression of numerous genes and resulting in profound cellular changes. Differential activation results from multiple levels of cellular and molecular events including binding affinity, receptor density, cell type-specific variations, and post-translational modification of signaling molecules downstream. Within the type I interferon family the Asn-Gly-Arg (NGR) sequence motif is unique to interferon-β and, together with its deamidated variants Asp-Gly-Arg (DGR) and iso-Asp-Gly-Arg (iso-DGR), imparts additional binding specificities that go beyond that of the canonical IFNAR1/IFNAR2. These warrant further investigations and functional studies and may eventually shed new light on differential effects observed for this molecule in oncology and autoimmune diseases.
MeSH term(s)	Humans ; Interferon Type I/metabolism ; Interferon-beta/metabolism ; Oligopeptides/metabolism ; Protein Binding/physiology ; Protein Processing, Post-Translational/physiology ; Receptor, Interferon alpha-beta/metabolism ; Signal Transduction/physiology
Chemical Substances	Interferon Type I ; NGR peptide ; Oligopeptides ; Receptor, Interferon alpha-beta (156986-95-7) ; Interferon-beta (77238-31-4)
Language	English
Publishing date	2018-08-31
Publishing country	England
Document type	Journal Article
ZDB-ID	1018055-2
ISSN	1096-0023 ; 1043-4666
ISSN (online)	1096-0023
ISSN	1043-4666
DOI	10.1016/j.cyto.2018.08.031
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Article ; Online: Glycoengineered antibodies: towards the next-generation of immunotherapeutics.

Mastrangeli, Renato / Palinsky, Wolf / Bierau, Horst

Glycobiology

2018 Volume 29, Issue 3, Page(s) 199–210

Abstract: Monoclonal antibodies (mAbs) are currently the largest and fastest growing class of biopharmaceuticals, and they address unmet medical needs, e.g., in oncology and in auto-immune diseases. Their clinical efficacy and safety is significantly affected by ... ...

Abstract	Monoclonal antibodies (mAbs) are currently the largest and fastest growing class of biopharmaceuticals, and they address unmet medical needs, e.g., in oncology and in auto-immune diseases. Their clinical efficacy and safety is significantly affected by the structure and composition of their glycosylation profile which is commonly heterogeneous, heavily dependent on the manufacturing process, and thus susceptible to variations in the cell culture conditions. Glycosylation is therefore considered a critical quality attribute for mAbs. Commonly, in currently marketed therapeutic mAbs, the glycosylation profile is suboptimal in terms of biological properties such as antibody-dependent cell-mediated cytotoxicity or may give rise to safety concerns due to the presence of non-human glycans. This article will review recent innovative developments in chemo-enzymatic glycoengineering, which allow generating mAbs carrying single, well-defined, uniform Fc glycoforms, which confers the desired biological properties for the target application. This approach offers significant benefits such as enhanced Fc effector functions, improved safety profiles, higher batch-to-batch consistency, decreased risks related to immunogenicity and manufacturing process changes, and the possibility to manufacture mAbs, in an economical manner, in non-mammalian expression systems. Overall, this approach could facilitate and reduce mAb manufacturing costs which in turn would translate into tangible benefits for both patients and manufacturers. The first glycoengineered mAbs are about to enter clinical trials and it is expected that, once glycoengineering reagents are available at affordable costs, and in-line with regulatory requirements, that targeted remodeling of antibody Fc glycosylation will become an integral part in manufacturing the next-generation of immunotherapeutics.
MeSH term(s)	Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/therapeutic use ; Antibody-Dependent Cell Cytotoxicity/drug effects ; Antibody-Dependent Cell Cytotoxicity/immunology ; Autoimmune Diseases/drug therapy ; Autoimmune Diseases/immunology ; Glycosylation ; Humans ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin Fc Fragments/immunology ; Immunoglobulin Fc Fragments/therapeutic use ; Immunotherapy/trends ; Neoplasms/drug therapy ; Neoplasms/immunology ; Polysaccharides/chemistry ; Polysaccharides/immunology ; Polysaccharides/therapeutic use
Chemical Substances	Antibodies, Monoclonal ; Immunoglobulin Fc Fragments ; Polysaccharides
Language	English
Publishing date	2018-10-04
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1067689-2
ISSN	1460-2423 ; 0959-6658
ISSN (online)	1460-2423
ISSN	0959-6658
DOI	10.1093/glycob/cwy092
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Article: The Formidable Challenge of Controlling High Mannose-Type N-Glycans in Therapeutic mAbs

Mastrangeli, Renato / Audino, Maria Concetta / Palinsky, Wolf / Broly, Hervé / Bierau, Horst

Trends in biotechnology. 2020 Oct., v. 38, no. 10

2020

Abstract: The clinical efficacy and safety of therapeutic monoclonal antibodies (mAbs) are significantly affected by their Fc-glycosylation profile. High mannose-type N-glycans (HM) affect efficacy (in terms of antibody-dependent cell cytotoxicity), ... ...

Abstract	The clinical efficacy and safety of therapeutic monoclonal antibodies (mAbs) are significantly affected by their Fc-glycosylation profile. High mannose-type N-glycans (HM) affect efficacy (in terms of antibody-dependent cell cytotoxicity), pharmacokinetics, and stability. While in endogenous IgGs the HM levels are very low, they are significantly higher in marketed therapeutic mAbs. In order to meet the demands for late-phase clinical trial and market supply, process intensification is required. Since glycosylation profiles are sensitive to process variations and changes, controlling HM levels in robust manufacturing processes presents a formidable challenge and requires a thorough understanding of the cellular processes as well as the biotechnical aspects that govern the production of HM glycans.
Keywords	biotechnology ; clinical trials ; cytotoxicity ; glycosylation ; markets ; pharmacokinetics ; polysaccharides ; therapeutics
Language	English
Dates of publication	2020-10
Size	p. 1154-1168.
Publishing place	Elsevier Ltd
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	47474-5
ISSN	1879-3096 ; 0167-7799
ISSN (online)	1879-3096
ISSN	0167-7799
DOI	10.1016/j.tibtech.2020.05.009
Database	NAL-Catalogue (AGRICOLA)

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Zs.A 2750: Show issues

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Article ; Online: The Formidable Challenge of Controlling High Mannose-Type N-Glycans in Therapeutic mAbs.

Mastrangeli, Renato / Audino, Maria Concetta / Palinsky, Wolf / Broly, Hervé / Bierau, Horst

Trends in biotechnology

2020 Volume 38, Issue 10, Page(s) 1154–1168

Abstract	The clinical efficacy and safety of therapeutic monoclonal antibodies (mAbs) are significantly affected by their Fc-glycosylation profile. High mannose-type N-glycans (HM) affect efficacy (in terms of antibody-dependent cell cytotoxicity), pharmacokinetics, and stability. While in endogenous IgGs the HM levels are very low, they are significantly higher in marketed therapeutic mAbs. In order to meet the demands for late-phase clinical trial and market supply, process intensification is required. Since glycosylation profiles are sensitive to process variations and changes, controlling HM levels in robust manufacturing processes presents a formidable challenge and requires a thorough understanding of the cellular processes as well as the biotechnical aspects that govern the production of HM glycans.
MeSH term(s)	Animals ; Antibodies, Monoclonal/analysis ; Antibodies, Monoclonal/chemistry ; Biotechnology/methods ; Biotechnology/standards ; CHO Cells ; Cell Culture Techniques ; Cricetinae ; Cricetulus ; Glycosylation ; Mannose/chemistry ; Polysaccharides/chemistry
Chemical Substances	Antibodies, Monoclonal ; Polysaccharides ; Mannose (PHA4727WTP)
Language	English
Publishing date	2020-06-29
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	47474-5
ISSN	1879-3096 ; 0167-7799
ISSN (online)	1879-3096
ISSN	0167-7799
DOI	10.1016/j.tibtech.2020.05.009
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Effect of Fc core fucosylation and light chain isotype on IgG1 flexibility.

Saporiti, Simona / Laurenzi, Tommaso / Guerrini, Uliano / Coppa, Crescenzo / Palinsky, Wolf / Benigno, Giulia / Palazzolo, Luca / Ben Mariem, Omar / Montavoci, Linda / Rossi, Mara / Centola, Fabio / Eberini, Ivano

Communications biology

2023 Volume 6, Issue 1, Page(s) 237

Abstract: N-glycosylation plays a key role in modulating the bioactivity of monoclonal antibodies (mAbs), as well as the light chain (LC) isotype can influence their physicochemical properties. However, investigating the impact of such features on mAbs ... ...

Abstract	N-glycosylation plays a key role in modulating the bioactivity of monoclonal antibodies (mAbs), as well as the light chain (LC) isotype can influence their physicochemical properties. However, investigating the impact of such features on mAbs conformational behavior is a big challenge, due to the very high flexibility of these biomolecules. In this work we investigate, by accelerated molecular dynamics (aMD), the conformational behavior of two commercial immunoglobulins G1 (IgG1), representative of κ and λ LCs antibodies, in both their fucosylated and afucosylated forms. Our results show, through the identification of a stable conformation, how the combination of fucosylation and LC isotype modulates the hinge behavior, the Fc conformation and the position of the glycan chains, all factors potentially affecting the binding to the FcγRs. This work also represents a technological enhancement in the conformational exploration of mAbs, making aMD a suitable approach to clarify experimental results.
MeSH term(s)	Glycosylation ; Immunoglobulin G ; Antibodies, Monoclonal ; Technology
Chemical Substances	Immunoglobulin G ; Antibodies, Monoclonal
Language	English
Publishing date	2023-03-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-023-04622-7
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Article ; Online: Asn25 Deamidation as an Allosteric Tool to Increase IFNβ-1a Biological Activity.

Lipari, Elisa / Saporiti, Simona / Eberini, Ivano / Massimo, Luigia / Mazzarella, Enrico / Anderloni, Giulia / Rossi, Mara / D'Amici, Fabio / Pergola, Carlo / Palinsky, Wolf / D'Acunto, Cosimo Walter / Centola, Fabio

Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research

2022 Volume 42, Issue 6, Page(s) 251–266

Abstract: Interferon beta (IFNβ) is a well-known cytokine, belonging to the type I family, that exerts antiviral, immunomodulatory, and antiproliferative activity. It has been reported that the artificially deamidated form of recombinant IFNβ-1a at Asn25 position ... ...

Abstract	Interferon beta (IFNβ) is a well-known cytokine, belonging to the type I family, that exerts antiviral, immunomodulatory, and antiproliferative activity. It has been reported that the artificially deamidated form of recombinant IFNβ-1a at Asn25 position shows an increased biological activity. As a deepening of the previous study, the molecular mechanism underlying this biological effect was investigated in this work by combining experimental and computational techniques. Specifically, the binding to IFNAR1 and IFNAR2 receptors and the canonical pathway of artificially deamidated IFNβ-1a molecule were analyzed in comparison to the native form. As a result, a change in receptor affinity of deamidated IFNβ-1a with respect to the native form was observed, and to better explore this molecular interaction, molecular dynamics simulations were carried out. Results confirmed, as previously hypothesized, that the N25D mutation can locally change the interaction network of the mutated residue but also that this effect can be propagated throughout the molecule. In fact, many residues not involved in the interaction with IFNAR1 in the native form participate to the recognition in the deamidated molecule, enhancing the binding to IFNAR1 receptor and consequently an increase of signaling cascade activation. In particular, a higher STAT1 phosphorylation and interferon-stimulated gene expression was observed under deamidated IFNβ-1a cell treatment. In conclusion, this study increases the scientific knowledge of deamidated IFNβ-1a, deciphering its molecular mechanism, and opens new perspectives to novel therapeutic strategies.
MeSH term(s)	Antiviral Agents/metabolism ; Immunologic Factors ; Interferon beta-1a ; Interferon-beta/metabolism ; Interferons ; Signal Transduction
Chemical Substances	Antiviral Agents ; Immunologic Factors ; Interferon-beta (77238-31-4) ; Interferons (9008-11-1) ; Interferon beta-1a (XRO4566Q4R)
Language	English
Publishing date	2022-05-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1226675-9
ISSN	1557-7465 ; 1079-9907
ISSN (online)	1557-7465
ISSN	1079-9907
DOI	10.1089/jir.2021.0209
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Zs.A 1748: Show issues

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Article ; Online: Site-specific N- and O-glycosylation analysis of atacicept.

Stavenhagen, Kathrin / Gahoual, Rabah / Dominguez Vega, Elena / Palmese, Angelo / Ederveen, Agnes L Hipgrave / Cutillo, Francesca / Palinsky, Wolf / Bierau, Horst / Wuhrer, Manfred

mAbs

2019 Volume 11, Issue 6, Page(s) 1053–1063

Abstract: The Fc-fusion protein atacicept is currently under clinical investigation for its biotherapeutic application in autoimmune diseases owing to its ability to bind the two cytokines B-Lymphocyte Stimulator (BLyS) and A PRoliferation-Inducing Ligand (APRIL). ...

Abstract	The Fc-fusion protein atacicept is currently under clinical investigation for its biotherapeutic application in autoimmune diseases owing to its ability to bind the two cytokines B-Lymphocyte Stimulator (BLyS) and A PRoliferation-Inducing Ligand (APRIL). Like typical recombinant IgG-based therapeutics, atacicept is a glycoprotein whose glycosylation-related heterogeneity arises from the glycosylation-site localization, site-specific occupation and structural diversity of the attached glycans. Here, we present a first comprehensive site-specific N- and O-glycosylation characterization of atacicept using mass spectrometry-based workflows. First, N- and O-glycosylation sites and their corresponding glycoforms were identified. Second, a relative quantitation of the N-glycosylation site microheterogeneity was achieved by glycopeptide analysis, which was further supported by analysis of the released N-glycans. We confirmed the presence of one N-glycosylation site, carrying 47 glycoforms covering 34 different compositions, next to two hinge region O-glycosylation sites with core 1-type glycans. The relative O-glycan distribution was analyzed based on the de-N-glycosylated intact protein species. Overall, N- and O-glycosylation were consistent between two individual production batches.
MeSH term(s)	Glycosylation ; Mass Spectrometry ; Polysaccharides/analysis ; Recombinant Fusion Proteins/chemistry
Chemical Substances	Polysaccharides ; Recombinant Fusion Proteins ; TACI receptor-IgG Fc fragment fusion protein (K3D9A0ICQ3)
Language	English
Publishing date	2019-07-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ISSN	1942-0870
ISSN (online)	1942-0870
DOI	10.1080/19420862.2019.1630218
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