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Book ; Online: The Secret of Time: Reconfiguring Wisdom in the Dead Sea Scrolls

Bakker, Arjen F

2023

Keywords	Judaism ; Dead Sea Scrolls ; Qumran
Language	English
Size	1 Online-Ressource
Publisher	Brill
Document type	Book ; Online
Note	English
HBZ-ID	HT030613460
ISBN	9789004529748 ; 9004529748
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article ; Online: Erratum to: 'Cross-genotype AR3-specific neutralizing antibodies confer long-term protection in injecting drug users after HCV clearance' (J Hepatol 2019; 71(1): 14-24).

Merat, Sabrina J / Bru, Camille / van de Berg, Dorien / Molenkamp, Richard / Tarr, Alexander W / Koekkoek, Sylvie / Kootstra, Neeltje A / Prins, Maria / Ball, Jonathan K / Bakker, Arjen Q / de Jong, Menno D / Spits, Hergen / Beaumont, Tim / Schinkel, Janke

Journal of hepatology

2020 Volume 73, Issue 4, Page(s) 999–1000

Language	English
Publishing date	2020-08-01
Publishing country	Netherlands
Document type	Journal Article ; Published Erratum
ZDB-ID	605953-3
ISSN	1600-0641 ; 0168-8278
ISSN (online)	1600-0641
ISSN	0168-8278
DOI	10.1016/j.jhep.2020.07.004
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Article ; Online: The Production of a Stable Infliximab Powder: The Evaluation of Spray and Freeze-Drying for Production.

Kanojia, Gaurav / Have, Rimko Ten / Bakker, Arjen / Wagner, Koen / Frijlink, Henderik W / Kersten, Gideon F A / Amorij, Jean-Pierre

PloS one

2016 Volume 11, Issue 10, Page(s) e0163109

Abstract: In prospect of developing an oral dosage form of Infliximab, for treatment of Crohn's disease and rheumatoid arthritis, freeze-drying (vial vs Lyoguard trays) and spray-drying were investigated as production method for stable powders. Dextran and inulin ... ...

Abstract	In prospect of developing an oral dosage form of Infliximab, for treatment of Crohn's disease and rheumatoid arthritis, freeze-drying (vial vs Lyoguard trays) and spray-drying were investigated as production method for stable powders. Dextran and inulin were used in combination with sucrose as stabilizing excipients. The drying processes did not affect Infliximab in these formulations, i.e. both the physical integrity and biological activity (TNF binding) were retained. Accelerated stability studies (1 month at 60°C) showed that the TNF binding ability of Infliximab was conserved in the freeze-dried formulations, whereas the liquid counterpart lost all TNF binding. After thermal treatment, the dried formulations showed some chemical modification of the IgG in the dextran-sucrose formulation, probably due to Maillard reaction products. This study indicates that, with the appropriate formulation, both spray-drying and freeze-drying may be useful for (bulk) powder production of Infliximab.
MeSH term(s)	Chromatography, Gel ; Dextrans/chemistry ; Drug Compounding/methods ; Drug Stability ; Electrophoresis, Polyacrylamide Gel ; Freeze Drying ; Infliximab/analysis ; Infliximab/chemistry ; Inulin/chemistry ; Maillard Reaction ; Sucrose/chemistry
Chemical Substances	Dextrans ; Sucrose (57-50-1) ; Inulin (9005-80-5) ; Infliximab (B72HH48FLU)
Language	English
Publishing date	2016
Publishing country	United States
Document type	Evaluation Studies ; Journal Article
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0163109
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Establishment of Systems to Enable Isolation of Porcine Monoclonal Antibodies Broadly Neutralizing the Porcine Reproductive and Respiratory Syndrome Virus.

Goldeck, David / Perry, Dana M / Hayes, Jack W P / Johnson, Luke P M / Young, Jordan E / Roychoudhury, Parimal / McLuskey, Elle L / Moffat, Katy / Bakker, Arjen Q / Kwakkenbos, Mark J / Frossard, Jean-Pierre / Rowland, Raymond R R / Murtaugh, Michael P / Graham, Simon P

Frontiers in immunology

2019 Volume 10, Page(s) 572

Abstract: The rapid evolution of porcine reproductive and respiratory syndrome viruses (PRRSV) poses a major challenge to effective disease control since available vaccines show variable efficacy against divergent strains. Knowledge of the antigenic targets of ... ...

Abstract	The rapid evolution of porcine reproductive and respiratory syndrome viruses (PRRSV) poses a major challenge to effective disease control since available vaccines show variable efficacy against divergent strains. Knowledge of the antigenic targets of virus-neutralizing antibodies that confer protection against heterologous PRRSV strains would be a catalyst for the development of next-generation vaccines. Key to discovering these epitopes is the isolation of neutralizing monoclonal antibodies (mAbs) from immune pigs. To address this need, we sought to establish systems to enable the isolation of PRRSV neutralizing porcine mAbs. We experimentally produced a cohort of immune pigs by sequential challenge infection with four heterologous PRRSV strains spanning PRRSV-1 subtypes and PRRSV species. Whilst priming with PRRSV-1 subtype 1 did not confer full protection against a subsequent infection with a PRRSV-1 subtype 3 strain, animals were protected against a subsequent PRRSV-2 infection. The infection protocol resulted in high serum neutralizing antibody titers against PRRSV-1 Olot/91 and significant neutralization of heterologous PRRSV-1/-2 strains. Enriched memory B cells isolated at the termination of the study were genetically programmed by transduction with a retroviral vector expressing the Bcl-6 transcription factor and the anti-apoptotic Bcl-xL protein, a technology we demonstrated efficiently converts porcine memory B cells into proliferating antibody-secreting cells. Pools of transduced memory B cells were cultured and supernatants containing PRRSV-specific antibodies identified by flow cytometric staining of infected MARC-145 cells and
MeSH term(s)	Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Neutralizing/blood ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/blood ; Antibodies, Viral/immunology ; B-Lymphocytes/immunology ; Cell Line ; Epitopes/genetics ; Immunologic Memory/genetics ; Immunologic Memory/immunology ; Neutralization Tests ; Porcine Reproductive and Respiratory Syndrome/immunology ; Porcine Reproductive and Respiratory Syndrome/therapy ; Porcine respiratory and reproductive syndrome virus/immunology ; Proto-Oncogene Proteins c-bcl-6/genetics ; Swine ; Viral Vaccines/immunology ; bcl-X Protein/genetics
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Proto-Oncogene Proteins c-bcl-6 ; Viral Vaccines ; bcl-X Protein
Language	English
Publishing date	2019-03-27
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2019.00572
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Article ; Online: Cross-genotype AR3-specific neutralizing antibodies confer long-term protection in injecting drug users after HCV clearance.

Journal of hepatology

2019 Volume 71, Issue 1, Page(s) 14–24

Abstract: Background & aims: In order to design an effective vaccine against hepatitis C virus (HCV) infection, it is necessary to understand immune protection. A number of broadly reactive neutralizing antibodies have been isolated from B cells of HCV-infected ... ...

Abstract	Background & aims: In order to design an effective vaccine against hepatitis C virus (HCV) infection, it is necessary to understand immune protection. A number of broadly reactive neutralizing antibodies have been isolated from B cells of HCV-infected patients. However, it remains unclear whether B cells producing such antibodies contribute to HCV clearance and long-term immune protection against HCV. Methods: We analysed the B cell repertoire of 13 injecting drug users from the Amsterdam Cohort Study, who were followed up for a median of 17.5 years after primary infection. Individuals were classified into 2 groups based on the outcome of HCV infection: 5 who became chronically infected either after primary infection or after reinfection, and 8 who were HCV RNA negative following spontaneous clearance of ≥1 HCV infection(s). From each individual, 10,000 CD27+IgG+B cells, collected 0.75 year after HCV infection, were cultured to characterize the antibody repertoire. Results: Using a multiplex flow cytometry-based assay to study the antibody binding to E1E2 from genotype 1 to 6, we found that a high frequency of cross-genotype antibodies was associated with spontaneous clearance of 1 or multiple infections (p = 0.03). Epitope specificity of these cross-genotype antibodies was determined by alanine mutant scanning in 4 individuals who were HCV RNA negative following spontaneous clearance of 1 or multiple infections. Interestingly, the cross-genotype antibodies were mainly antigenic region 3 (AR3)-specific and showed cross-neutralizing activity against HCV. In addition to AR3 antibodies, 3 individuals developed antibodies recognizing antigenic region 4, of which 1 monoclonal antibody showed cross-neutralizing capacity. Conclusions: Together, these data suggest that a strong B cell response producing cross-genotype and neutralizing antibodies, especially targeting AR3, contributes to HCV clearance and long-term immune protection against HCV. Lay summary: Although effective treatments against hepatitis C virus (HCV) are available, 500,000 people die from liver disease caused by HCV each year and approximately 1.75 million people are newly infected. This could be prevented by a vaccine. To design a vaccine against HCV, more insight into the role of antibodies in the protection against HCV infection is needed. In a cohort of injecting drug users, we found that antibodies interfering with virus cell entry, and recognizing multiple HCV genotypes, conferred long-term protection against chronic HCV infection.
MeSH term(s)	Adaptive Immunity/immunology ; Adult ; Antibodies, Neutralizing/biosynthesis ; Antibodies, Neutralizing/blood ; Epitopes, B-Lymphocyte/immunology ; Female ; Hepacivirus/genetics ; Hepacivirus/immunology ; Hepacivirus/isolation & purification ; Hepatitis C Antibodies/biosynthesis ; Hepatitis C Antibodies/blood ; Hepatitis C, Chronic/etiology ; Hepatitis C, Chronic/immunology ; Humans ; Immunologic Memory ; Male ; RNA, Viral/isolation & purification ; Substance Abuse, Intravenous/complications ; Substance Abuse, Intravenous/virology ; Viral Envelope Proteins/immunology ; Viral Hepatitis Vaccines/pharmacology
Chemical Substances	Antibodies, Neutralizing ; Epitopes, B-Lymphocyte ; Hepatitis C Antibodies ; RNA, Viral ; Viral Envelope Proteins ; Viral Hepatitis Vaccines
Language	English
Publishing date	2019-02-21
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	605953-3
ISSN	1600-0641 ; 0168-8278
ISSN (online)	1600-0641
ISSN	0168-8278
DOI	10.1016/j.jhep.2019.02.013
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Article: Identification of target membrane proteins as detected by phage antibodies.

Geuijen, Cecile A W / Bakker, Arjen Q / de Kruif, John

Methods in molecular biology (Clifton, N.J.)

2009 Volume 528, Page(s) 141–158

Abstract: The discovery of novel target antigens for antibody-based immunotherapy is still a major challenge. Antibody phage display is one of the technologies that is widely applied for the identification of novel cell surface molecules on intact eukaryotic cells ...

Abstract	The discovery of novel target antigens for antibody-based immunotherapy is still a major challenge. Antibody phage display is one of the technologies that is widely applied for the identification of novel cell surface molecules on intact eukaryotic cells and many reports describe the isolation of phage-antibodies binding to restricted cell populations such as cells in a certain pathological condition. However, the transition from cell-specific phage antibodies to the identification of the target antigens is still a major hurdle. Herein a method is described for the identification of these cell surface molecules using two complementary technologies. A genomic approach based on expression cloning can be used when cDNA libraries and antigen-negative cells are available. Otherwise, a proteomic approach based on small scale immunoprecipitation followed by large scale purification and mass-spectrometry-based identification can be applied. Correct identification of the antigens is confirmed using technologies such as recombinant expression of the target antigen followed by immunoprecipitation or cDNA transfection and FACS analysis.
MeSH term(s)	Antibodies, Viral/immunology ; Biotinylation ; Cell Line ; Cloning, Molecular ; Flow Cytometry ; Gene Library ; Genomics/methods ; Immunoprecipitation ; Mass Spectrometry ; Membrane Proteins/analysis ; Membrane Proteins/immunology ; Peptide Library ; Plasmids ; Proteomics/methods ; Transfection
Chemical Substances	Antibodies, Viral ; Membrane Proteins ; Peptide Library
Language	English
Publishing date	2009
Publishing country	United States
Document type	Evaluation Studies ; Journal Article
ISSN	1064-3745
ISSN	1064-3745
DOI	10.1007/978-1-60327-310-7_11
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: A Chemo-enzymatically Linked Bispecific Antibody Retargets T Cells to a Sialylated Epitope on CD43 in Acute Myeloid Leukemia.

Bartels, Lina / de Jong, Greta / Gillissen, Marijn A / Yasuda, Etsuko / Kattler, Veronika / Bru, Camille / Fatmawati, Christien / van Hal-van Veen, Susan E / Cercel, Madalina G / Moiset, Gemma / Bakker, Arjen Q / van Helden, Pauline M / Villaudy, Julien / Hazenberg, Mette D / Spits, Hergen / Wagner, Koen

Cancer research

2019 Volume 79, Issue 13, Page(s) 3372–3382

Abstract: Acute myeloid leukemia (AML) is a high-risk disease with a poor prognosis, particularly in elderly patients. Because current AML treatment relies primarily on untargeted therapies with severe side effects that limit patient eligibility, identification of ...

Abstract	Acute myeloid leukemia (AML) is a high-risk disease with a poor prognosis, particularly in elderly patients. Because current AML treatment relies primarily on untargeted therapies with severe side effects that limit patient eligibility, identification of novel therapeutic AML targets is highly desired. We recently described AT1413, an antibody produced by donor B cells of a patient with AML cured after allogeneic hematopoietic stem cell transplantation. AT1413 binds CD43s, a unique sialylated epitope on CD43, which is weakly expressed on normal myeloid cells and overexpressed on AML cells. Because of its selectivity for AML cells, we considered CD43s as a target for a bispecific T-cell-engaging antibody (bTCE) and generated a bTCE by coupling AT1413 to two T-cell-targeting fragments using chemo-enzymatic linkage.
MeSH term(s)	Animals ; Antibodies, Bispecific/pharmacology ; Apoptosis ; Cell Proliferation ; Cytotoxicity, Immunologic ; Endothelial Cells/drug effects ; Endothelial Cells/immunology ; Endothelial Cells/metabolism ; Epitopes/drug effects ; Epitopes/immunology ; Epitopes/metabolism ; Female ; Humans ; Leukemia, Myeloid, Acute/drug therapy ; Leukemia, Myeloid, Acute/immunology ; Leukemia, Myeloid, Acute/metabolism ; Leukemia, Myeloid, Acute/pathology ; Leukocytes, Mononuclear/drug effects ; Leukocytes, Mononuclear/immunology ; Leukocytes, Mononuclear/metabolism ; Leukosialin/immunology ; Lymphocyte Activation/drug effects ; Lymphocyte Activation/immunology ; Mice ; Mice, Inbred NOD ; Mice, SCID ; N-Acetylneuraminic Acid/metabolism ; Prognosis ; T-Lymphocytes/drug effects ; T-Lymphocytes/immunology ; T-Lymphocytes/metabolism ; Tumor Cells, Cultured ; Xenograft Model Antitumor Assays
Chemical Substances	Antibodies, Bispecific ; Epitopes ; Leukosialin ; SPN protein, human ; N-Acetylneuraminic Acid (GZP2782OP0)
Language	English
Publishing date	2019-05-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-18-0189
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Article: Patient-derived antibody recognizes a unique CD43 epitope expressed on all AML and has antileukemia activity in mice.

Gillissen, Marijn A / de Jong, Greta / Kedde, Martijn / Yasuda, Etsuko / Levie, Sophie E / Moiset, Gemma / Hensbergen, Paul J / Bakker, Arjen Q / Wagner, Koen / Villaudy, Jullien / van Helden, Pauline M / Spits, Hergen / Hazenberg, Mette D

Blood advances

2017 Volume 1, Issue 19, Page(s) 1551–1564

Abstract: Immunotherapy has proven beneficial in many hematologic and nonhematologic malignancies, but immunotherapy for acute myeloid leukemia (AML) and myelodysplastic syndrome (MDS) is hampered by the lack of tumor-specific targets. We took advantage of the ... ...

Abstract	Immunotherapy has proven beneficial in many hematologic and nonhematologic malignancies, but immunotherapy for acute myeloid leukemia (AML) and myelodysplastic syndrome (MDS) is hampered by the lack of tumor-specific targets. We took advantage of the tumor-immunotherapeutic effect of allogeneic hematopoietic stem cell transplantation and searched the B-cell repertoire of a patient with a lasting and potent graft-versus-AML response for the presence of AML-specific antibodies. We identified an antibody, AT1413, that was of donor origin and that specifically recognizes a novel sialylated epitope on CD43 (CD43s). Strikingly, CD43s is expressed on all World Health Organization 2008 types of AML and MDS. AT1413 induced antibody-dependent cell-mediated cytotoxicity and complement-dependent cytotoxicity of AML cells in vitro. Of note, AT1413 was highly efficacious against AML cells in a humanized mouse model without affecting nonmalignant human myeloid cells, suggesting AT1413 has potential as a therapeutic antibody.
Language	English
Publishing date	2017-08-22
Publishing country	United States
Document type	Journal Article
ZDB-ID	2876449-3
ISSN	2473-9537 ; 2473-9529
ISSN (online)	2473-9537
ISSN	2473-9529
DOI	10.1182/bloodadvances.2017008342
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Article ; Online: Genetic manipulation of B cells for the isolation of rare therapeutic antibodies from the human repertoire.

Kwakkenbos, Mark J / Bakker, Arjen Q / van Helden, Pauline M / Wagner, Koen / Yasuda, Etsuko / Spits, Hergen / Beaumont, Tim

Methods (San Diego, Calif.)

2014 Volume 65, Issue 1, Page(s) 38–43

Abstract: Antibody based therapies are increasingly applied to prevent and treat human disease. While the majority of antibodies currently on the market are chimeric or humanized antibodies from rodents, the focus has now shifted to the isolation and development ... ...

Abstract	Antibody based therapies are increasingly applied to prevent and treat human disease. While the majority of antibodies currently on the market are chimeric or humanized antibodies from rodents, the focus has now shifted to the isolation and development of fully human antibodies. By retroviral transduction of B cell lymphoma-6 (BCL-6), which prevents terminal differentiation of B cells and, the anti-apoptotic gene B-cell lymphoma-extra large (Bcl-xL) into primary human B cells we efficiently immortalize antibody-producing B cells allowing the isolation of therapeutic antibodies. Selection of antigen-specific B cell clones was greatly facilitated because the transduced B cells retain surface immunoglobulin expression and secrete immunoglobulin into the culture supernatant. Surface immunoglobulin expression can be utilized to stain and isolate antigen specific B cell clones with labeled antigen. Immunoglobulins secreted in culture supernatant can directly be tested in functional assays to identify unique B cell clones. Here we describe the key features of our Bcl-6/Bcl-xL culture platform (AIMSelect).
MeSH term(s)	Animals ; Antibodies, Monoclonal/biosynthesis ; Antibodies, Monoclonal/isolation & purification ; B-Lymphocytes/physiology ; Cell Culture Techniques ; Cell Separation ; Cells, Cultured ; DNA-Binding Proteins/genetics ; Drug Discovery ; Genetic Engineering ; Humans ; Proto-Oncogene Proteins c-bcl-6 ; Receptors, Antigen, B-Cell/genetics ; Receptors, Antigen, B-Cell/metabolism ; bcl-X Protein/genetics
Chemical Substances	Antibodies, Monoclonal ; BCL2L1 protein, human ; BCL6 protein, human ; DNA-Binding Proteins ; Proto-Oncogene Proteins c-bcl-6 ; Receptors, Antigen, B-Cell ; bcl-X Protein
Language	English
Publishing date	2014-01-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2013.07.002
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Article ; Online: Multiplex flow cytometry-based assay to study the breadth of antibody responses against E1E2 glycoproteins of hepatitis C virus.

Merat, Sabrina J / van de Berg, Dorien / Bru, Camille / Yasuda, Etsuko / Breij, Esther / Kootstra, Neeltje / Prins, Maria / Molenkamp, Richard / Bakker, Arjen Q / de Jong, Menno D / Spits, Hergen / Schinkel, Janke / Beaumont, Tim

Journal of immunological methods

2017 Volume 454, Page(s) 15–26

Abstract: Hepatitis C virus (HCV) infection is a major global public health problem. Early induction of cross-reactive neutralizing antibodies during acute infection correlates with the spontaneous clearance of HCV. Understanding the antibody response in multiple ... ...

Abstract	Hepatitis C virus (HCV) infection is a major global public health problem. Early induction of cross-reactive neutralizing antibodies during acute infection correlates with the spontaneous clearance of HCV. Understanding the antibody response in multiple subjects in large-scale studies would greatly benefit vaccine development. To determine the breadth of a polyclonal-serum antibody response, and or, the monoclonal antibodies against the different HCV E1E2 genotypes, we developed a quick and high throughput flow cytometry assay using fluorescent cell barcoding to distinguish cells transfected with different E1E2 sequences in a single measurement. HCV-specific antibodies recognizing conformational epitopes were tested for binding to cells transfected with E1E2 from six genotypes. In this assay, 1500 samples can be analyzed for specific binding to 6 different HCV E1E2 sequences within 8h. Plasma of HCV infected subjects were tested in our assay allowing us to determine the breadth of their antibody response. In summary, we developed a quick and high throughput assay to study the specificity of an antibody response against multiple HCV E1E2 sequences simultaneously. This assay can also be used to facilitate the discovery of novel antibodies, and because other flavi- and picornaviruses have similar intracellular assembly mechanisms, this approach can be used to study the antibody response against such viruses.
MeSH term(s)	Antibodies, Neutralizing/metabolism ; Antibody Formation ; Cell Separation ; Cross Reactions ; Epitopes, B-Lymphocyte/genetics ; Epitopes, B-Lymphocyte/immunology ; Flow Cytometry/methods ; Fluorescence ; HEK293 Cells ; Hepacivirus/immunology ; Hepatitis C Antibodies/metabolism ; Hepatitis C, Chronic/immunology ; Hepatitis C, Chronic/metabolism ; High-Throughput Screening Assays ; Humans ; Neutralization Tests ; Transgenes/genetics ; Viral Envelope Proteins/genetics ; Viral Envelope Proteins/immunology
Chemical Substances	Antibodies, Neutralizing ; E1 protein, Hepatitis C virus ; Epitopes, B-Lymphocyte ; Hepatitis C Antibodies ; Viral Envelope Proteins ; glycoprotein E2, Hepatitis C virus (157184-61-7)
Language	English
Publishing date	2017-08-30
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120142-6
ISSN	1872-7905 ; 0022-1759
ISSN (online)	1872-7905
ISSN	0022-1759
DOI	10.1016/j.jim.2017.07.015
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