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Article ; Online: In vivo

Man, Francis / Koers, Alexander / Karagiannis, Panagiotis / Josephs, Debra H / Bax, Heather J / Gilbert, Amy E / Dodev, Tihomir S / Mele, Silvia / Chiarruttini, Giulia / Crescioli, Silvia / Chauhan, Jitesh / Blower, Julia E / Cooper, Margaret S / Spicer, James / Karagiannis, Sophia N / Blower, Philip J

Oncoimmunology

2021 Volume 10, Issue 1, Page(s) 1966970

Abstract: IgE antibodies elicit powerful immune responses, recruiting effector cells to tumors more efficiently and with greater cytotoxicity than IgG antibodies. Consequently, IgE antibodies are a promising alternative to conventional IgG-based therapies in ... ...

Abstract	IgE antibodies elicit powerful immune responses, recruiting effector cells to tumors more efficiently and with greater cytotoxicity than IgG antibodies. Consequently, IgE antibodies are a promising alternative to conventional IgG-based therapies in oncology (AllergoOncology). As the pharmacokinetics of IgE antibodies are less well understood, we used molecular imaging in mice to compare the distribution and elimination of IgE and IgG antibodies targeting the human tumor-associated antigen chondroitin sulfate proteoglycan 4 (CSPG4). Anti-CSPG4 IgE and IgG1 antibodies with human Fc domains were radiolabeled with
MeSH term(s)	Animals ; Antigens, Neoplasm ; Immunoglobulin E ; Immunoglobulin G ; Melanoma ; Mice ; Mice, Inbred NOD ; Molecular Imaging
Chemical Substances	Antigens, Neoplasm ; Immunoglobulin G ; Immunoglobulin E (37341-29-0)
Language	English
Publishing date	2021-09-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2645309-5
ISSN	2162-402X ; 2162-402X
ISSN (online)	2162-402X
ISSN	2162-402X
DOI	10.1080/2162402X.2021.1966970
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Article ; Online: Mechanism of the antigen-independent cytokinergic SPE-7 IgE activation of human mast cells in vitro.

Bax, Heather J / Bowen, Holly / Dodev, Tihomir S / Sutton, Brian J / Gould, Hannah J

Scientific reports

2015 Volume 5, Page(s) 9538

Abstract: Release of pro-inflammatory mediators by mast cells is a key feature of allergic disease. The 'dogma' is that IgE molecules merely sensitise mast cells by binding FcεRI prior to cross-linking by multivalent allergen, receptor aggregation and mast cell ... ...

Abstract	Release of pro-inflammatory mediators by mast cells is a key feature of allergic disease. The 'dogma' is that IgE molecules merely sensitise mast cells by binding FcεRI prior to cross-linking by multivalent allergen, receptor aggregation and mast cell activation. However, certain monoclonal IgE antibodies have been shown to elicit mast cell activation in an antigen-independent cytokinergic manner, and DNP-specific murine SPE-7 IgE is the most highly cytokinergic antibody known. We show that both monovalent hapten and recombinant SPE-7 IgE Fab inhibit its cytokinergic activity as measured by mast cell degranulation and TNF-α release. Using SPE-7 IgE, a non-cytokinergic human IgE and a poorly cytokinergic murine IgE, we reveal that interaction of the Fab region of 'free' SPE-7 IgE with the Fab of FcεRI-bound SPE-7 IgE is the basis of its cytokinergic activity. We rule out involvement of IgE Fc, Cε1 and Cλ/κ domains, and propose that 'free' SPE-7 IgE binds to FcεRI-bound SPE-7 IgE by an Fv-Fv interaction. Initial formation of a tri-molecular complex (one 'free' IgE molecule cross-linking two receptor-bound IgE molecules) leads to capture of further 'free' and receptor-bound IgEs to form larger clusters that trigger mast cell activation.
MeSH term(s)	Amino Acid Sequence ; Animals ; Antigens/immunology ; Cell Degranulation/drug effects ; Cell Line ; HEK293 Cells ; Haptens/chemistry ; Humans ; Hypersensitivity/immunology ; Hypersensitivity/pathology ; Immunoglobulin E/genetics ; Immunoglobulin E/metabolism ; Immunoglobulin E/pharmacology ; Immunoglobulin Fab Fragments/genetics ; Immunoglobulin Fab Fragments/metabolism ; Immunoglobulin Fab Fragments/pharmacology ; Mast Cells/cytology ; Mast Cells/drug effects ; Mast Cells/physiology ; Molecular Sequence Data ; Protein Binding ; Rats ; Receptors, IgE/chemistry ; Receptors, IgE/genetics ; Receptors, IgE/metabolism ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; Recombinant Proteins/pharmacology ; Tumor Necrosis Factor-alpha/metabolism
Chemical Substances	Antigens ; Haptens ; Immunoglobulin Fab Fragments ; Receptors, IgE ; Recombinant Proteins ; Tumor Necrosis Factor-alpha ; Immunoglobulin E (37341-29-0)
Language	English
Publishing date	2015-04-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/srep09538
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Article ; Online: Promiscuous antibodies characterised by their physico-chemical properties: From sequence to structure and back.

Laffy, Julie M J / Dodev, Tihomir / Macpherson, Jamie A / Townsend, Catherine / Lu, Hui Chun / Dunn-Walters, Deborah / Fraternali, Franca

Progress in biophysics and molecular biology

2016 Volume 128, Page(s) 47–56

Abstract: Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, ... ...

Abstract	Human B cells produce antibodies, which bind to their cognate antigen based on distinct molecular properties of the antibody CDR loop. We have analysed a set of 10 antibodies showing a clear difference in their binding properties to a panel of antigens, resulting in two subsets of antibodies with a distinct binding phenotype. We call the observed binding multiplicity 'promiscuous' and selected physico-chemical CDRH3 characteristics and conformational preferences may characterise these promiscuous antibodies. To classify CDRH3 physico-chemical properties playing a role in their binding properties, we used statistical analyses of the sequences annotated by Kidera factors. To characterise structure-function requirements for antigen binding multiplicity we employed Molecular Modelling and Monte Carlo based coarse-grained simulations. The ability to predict the molecular causes of promiscuous, multi-binding behaviour would greatly improve the efficiency of the therapeutic antibody discovery process.
MeSH term(s)	Antibodies/chemistry ; Antibodies/immunology ; Antibody Specificity ; Antigens/immunology ; Chemical Phenomena ; Complementarity Determining Regions/chemistry ; Humans ; Models, Molecular ; Monte Carlo Method ; Phenotype ; Protein Conformation, beta-Strand
Chemical Substances	Antibodies ; Antigens ; Complementarity Determining Regions
Language	English
Publishing date	2016-09-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209302-9
ISSN	1873-1732 ; 0079-6107
ISSN (online)	1873-1732
ISSN	0079-6107
DOI	10.1016/j.pbiomolbio.2016.09.002
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Article ; Online: Structure of a patient-derived antibody in complex with allergen reveals simultaneous conventional and superantigen-like recognition.

Mitropoulou, Alkistis N / Bowen, Holly / Dodev, Tihomir S / Davies, Anna M / Bax, Heather J / Beavil, Rebecca L / Beavil, Andrew J / Gould, Hannah J / James, Louisa K / Sutton, Brian J

Proceedings of the National Academy of Sciences of the United States of America

2018 Volume 115, Issue 37, Page(s) E8707–E8716

Abstract: Antibodies classically bind antigens via their complementarity-determining regions, but an alternative mode of interaction involving V-domain framework regions has been observed for some B cell "superantigens." We report the crystal structure of an ... ...

Abstract	Antibodies classically bind antigens via their complementarity-determining regions, but an alternative mode of interaction involving V-domain framework regions has been observed for some B cell "superantigens." We report the crystal structure of an antibody employing both modes of interaction simultaneously and binding two antigen molecules. This human antibody from an allergic individual binds to the grass pollen allergen
MeSH term(s)	Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/metabolism ; Antibody Specificity/immunology ; Antigens, Plant/chemistry ; Antigens, Plant/immunology ; Antigens, Plant/metabolism ; Basophils/immunology ; Basophils/physiology ; Calcium-Binding Proteins/chemistry ; Calcium-Binding Proteins/immunology ; Calcium-Binding Proteins/metabolism ; Cell Degranulation/immunology ; Cross Reactions/immunology ; Crystallography, X-Ray ; Epitopes/chemistry ; Epitopes/immunology ; Epitopes/metabolism ; Humans ; Immunoglobulin E/chemistry ; Immunoglobulin E/immunology ; Immunoglobulin E/metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation ; Superantigens/chemistry ; Superantigens/immunology ; Superantigens/metabolism
Chemical Substances	Antibodies, Monoclonal ; Antigens, Plant ; Calcium-Binding Proteins ; Epitopes ; Phl p 7 allergen ; Superantigens ; Immunoglobulin E (37341-29-0)
Language	English
Publishing date	2018-08-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1806840115
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Article ; Online: IgE Trimers Drive SPE-7 Cytokinergic Activity.

Bax, Heather J / Bowen, Holly / Beavil, Rebecca L / Chung, Raymond / Ward, Malcolm / Davies, Anna M / Dodev, Tihomir S / McDonnell, James M / Beavil, Andrew J / Sutton, Brian J / Gould, Hannah J

Scientific reports

2017 Volume 7, Issue 1, Page(s) 8164

Abstract: Degranulation of mast cells and basophils, with release of agents of the allergic response, ensues when multivalent antigens bind to and cross-link the cells' receptor-bound IgE antibodies. A widely used commercial monoclonal IgE antibody, SPE-7 IgE from ...

Abstract	Degranulation of mast cells and basophils, with release of agents of the allergic response, ensues when multivalent antigens bind to and cross-link the cells' receptor-bound IgE antibodies. A widely used commercial monoclonal IgE antibody, SPE-7 IgE from Sigma, was found to possess the radically anomalous property, termed "cytokinergic", of inducing basophil degranulation without the intervention of an antigen. We show here that the IgE monomer, freed of protein contaminants, is devoid of this activity, and that the source of the anomaly is a trace impurity, identified as a dissociation-resistant IgE trimer. Possible models for the formation of IgE trimers and the manner in which they cross-link cell surface receptors are suggested herein.
MeSH term(s)	Animals ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/isolation & purification ; Antibodies, Monoclonal/metabolism ; Basophils/immunology ; Basophils/metabolism ; Cell Degranulation/immunology ; Cell Line ; Humans ; Immunoglobulin E/chemistry ; Immunoglobulin E/immunology ; Immunoglobulin E/isolation & purification ; Immunoglobulin E/metabolism ; Mice ; Protein Binding ; Protein Multimerization ; Receptors, IgE/metabolism
Chemical Substances	Antibodies, Monoclonal ; Receptors, IgE ; Immunoglobulin E (37341-29-0)
Language	English
Publishing date	2017-08-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-017-08212-6
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Article ; Online: Anti-cancer pro-inflammatory effects of an IgE antibody targeting the melanoma-associated antigen chondroitin sulfate proteoglycan 4.

Chauhan, Jitesh / Grandits, Melanie / Palhares, Lais C G F / Mele, Silvia / Nakamura, Mano / López-Abente, Jacobo / Crescioli, Silvia / Laddach, Roman / Romero-Clavijo, Pablo / Cheung, Anthony / Stavraka, Chara / Chenoweth, Alicia M / Sow, Heng Sheng / Chiaruttini, Giulia / Gilbert, Amy E / Dodev, Tihomir / Koers, Alexander / Pellizzari, Giulia / Ilieva, Kristina M /

Nature communications

2023 Volume 14, Issue 1, Page(s) 2192

Abstract: Outcomes for half of patients with melanoma remain poor despite standard-of-care checkpoint inhibitor therapies. The prevalence of the melanoma-associated antigen chondroitin sulfate proteoglycan 4 (CSPG4) expression is ~70%, therefore effective ... ...

Abstract	Outcomes for half of patients with melanoma remain poor despite standard-of-care checkpoint inhibitor therapies. The prevalence of the melanoma-associated antigen chondroitin sulfate proteoglycan 4 (CSPG4) expression is ~70%, therefore effective immunotherapies directed at CSPG4 could benefit many patients. Since IgE exerts potent immune-activating functions in tissues, we engineer a monoclonal IgE antibody with human constant domains recognizing CSPG4 to target melanoma. CSPG4 IgE binds to human melanomas including metastases, mediates tumoricidal antibody-dependent cellular cytotoxicity and stimulates human IgE Fc-receptor-expressing monocytes towards pro-inflammatory phenotypes. IgE demonstrates anti-tumor activity in human melanoma xenograft models engrafted with human effector cells and is associated with enhanced macrophage infiltration, enriched monocyte and macrophage gene signatures and pro-inflammatory signaling pathways in the tumor microenvironment. IgE prolongs the survival of patient-derived xenograft-bearing mice reconstituted with autologous immune cells. No ex vivo activation of basophils in patient blood is measured in the presence of CSPG4 IgE. Our findings support a promising IgE-based immunotherapy for melanoma.
MeSH term(s)	Humans ; Mice ; Animals ; Proteoglycans/metabolism ; Antigens ; Chondroitin Sulfate Proteoglycans ; Melanoma/metabolism ; Antibodies, Monoclonal/pharmacology ; Immunoglobulin E ; Tumor Microenvironment
Chemical Substances	chondroitin sulfate proteoglycan 4 ; Proteoglycans ; Antigens ; Chondroitin Sulfate Proteoglycans ; Antibodies, Monoclonal ; Immunoglobulin E (37341-29-0)
Language	English
Publishing date	2023-04-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-37811-3
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Article ; Online: A tool kit for rapid cloning and expression of recombinant antibodies.

Dodev, Tihomir S / Karagiannis, Panagiotis / Gilbert, Amy E / Josephs, Debra H / Bowen, Holly / James, Louisa K / Bax, Heather J / Beavil, Rebecca / Pang, Marie O / Gould, Hannah J / Karagiannis, Sophia N / Beavil, Andrew J

Scientific reports

2014 Volume 4, Page(s) 5885

Abstract: Over the last four decades, molecular cloning has evolved tremendously. Efficient products allowing assembly of multiple DNA fragments have become available. However, cost-effective tools for engineering antibodies of different specificities, isotypes ... ...

Abstract	Over the last four decades, molecular cloning has evolved tremendously. Efficient products allowing assembly of multiple DNA fragments have become available. However, cost-effective tools for engineering antibodies of different specificities, isotypes and species are still needed for many research and clinical applications in academia. Here, we report a method for one-step assembly of antibody heavy- and light-chain DNAs into a single mammalian expression vector, starting from DNAs encoding the desired variable and constant regions, which allows antibodies of different isotypes and specificity to be rapidly generated. As a proof of principle we have cloned, expressed and characterized functional recombinant tumor-associated antigen-specific chimeric IgE/κ and IgG1/κ, as well as recombinant grass pollen allergen Phl p 7 specific fully human IgE/λ and IgG4/λ antibodies. This method utilizing the antibody expression vectors, available at Addgene, has many applications, including the potential to support simultaneous processing of antibody panels, to facilitate mechanistic studies of antigen-antibody interactions and to conduct early evaluations of antibody functions.
MeSH term(s)	Animals ; Antigens, Plant/biosynthesis ; Antigens, Plant/genetics ; Base Sequence ; Calcium-Binding Proteins/biosynthesis ; Calcium-Binding Proteins/genetics ; Cloning, Molecular/methods ; DNA Primers/chemical synthesis ; Epitopes/chemistry ; Epitopes/immunology ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Humans ; Immunoglobulin E/biosynthesis ; Immunoglobulin E/genetics ; Immunoglobulin G/biosynthesis ; Immunoglobulin G/genetics ; Immunoglobulin kappa-Chains/biosynthesis ; Immunoglobulin kappa-Chains/genetics ; Immunoglobulin lambda-Chains/biosynthesis ; Immunoglobulin lambda-Chains/genetics ; Molecular Sequence Data ; Plant Proteins/biosynthesis ; Plant Proteins/genetics ; Polymerase Chain Reaction ; Reagent Kits, Diagnostic ; Recombinant Fusion Proteins/biosynthesis ; Recombinant Fusion Proteins/genetics
Chemical Substances	Antigens, Plant ; Calcium-Binding Proteins ; DNA Primers ; Epitopes ; Immunoglobulin G ; Immunoglobulin kappa-Chains ; Immunoglobulin lambda-Chains ; Phl p 7 allergen ; Plant Proteins ; Reagent Kits, Diagnostic ; Recombinant Fusion Proteins ; Immunoglobulin E (37341-29-0)
Language	English
Publishing date	2014-07-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/srep05885
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Article ; Online: "Auto-anti-IgE": naturally occurring IgG anti-IgE antibodies may inhibit allergen-induced basophil activation.

Chan, Yih-Chih / Ramadani, Faruk / Santos, Alexandra F / Pillai, Prathap / Ohm-Laursen, Line / Harper, Clare E / Fang, Cailong / Dodev, Tihomir S / Wu, Shih-Ying / Ying, Sun / Corrigan, Christopher J / Gould, Hannah J

The Journal of allergy and clinical immunology

2014 Volume 134, Issue 6, Page(s) 1394–1401.e4

Abstract: Background: Naturally occurring IgE-specific IgG autoantibodies have been identified in patients with asthma and other diseases, but their spectrum of functions is poorly understood.: Objective: Address the hypothesis that: (i) IgG anti-IgE ... ...

Abstract	Background: Naturally occurring IgE-specific IgG autoantibodies have been identified in patients with asthma and other diseases, but their spectrum of functions is poorly understood. Objective: Address the hypothesis that: (i) IgG anti-IgE autoantibodies are detectable in the serum of all subjects but elevated in asthmatic patients regardless of atopic status as compared with controls; (ii) some activate IgE-sensitized basophils; and (iii) some inhibit allergen-induced basophil activation. Methods: IgE-specific IgG autoantibodies were detected and quantified in sera using ELISA. Sera were examined for their ability to activate IgE-sensitized human blood basophils in the presence and absence of allergen using a basophil activation test, and to inhibit allergen binding to specific IgE on a rat basophilic cell line stably expressing human FcεRI. Results: IgG autoantibodies binding to both free and FcεRI-bound IgE were detected in patients with atopic and non-atopic asthma, as well as controls. While some were able to activate IgE-sensitised basophils, others inhibited allergen-induced basophil activation, at least partly by inhibiting binding of IgE to specific allergen. Conclusion: Naturally occurring IgG anti-IgE autoantibodies may inhibit, as well as induce, basophil activation. They act in a manner distinct from therapeutic IgG anti-IgE antibodies such as omalizumab. They may at least partly explain why atopic subjects who make allergen-specific IgE never develop clinical symptoms, and why omalizumab therapy is of variable clinical benefit in severe atopic asthma.
MeSH term(s)	Allergens/immunology ; Animals ; Antibodies, Anti-Idiotypic/blood ; Antibodies, Anti-Idiotypic/immunology ; Antigens, Plant/immunology ; Asthma/blood ; Asthma/immunology ; Autoantibodies/blood ; Autoantibodies/immunology ; Basophils/immunology ; Calcium-Binding Proteins/immunology ; Cell Line ; Humans ; Immunoglobulin E/immunology ; Immunoglobulin G/blood ; Immunoglobulin G/immunology ; Phleum/immunology ; Rats ; Receptors, IgE/immunology
Chemical Substances	Allergens ; Antibodies, Anti-Idiotypic ; Antigens, Plant ; Autoantibodies ; Calcium-Binding Proteins ; Immunoglobulin G ; Phl p 7 allergen ; Receptors, IgE ; anti-IgE antibodies ; Immunoglobulin E (37341-29-0)
Language	English
Publishing date	2014-08-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	121011-7
ISSN	1097-6825 ; 1085-8725 ; 0091-6749
ISSN (online)	1097-6825 ; 1085-8725
ISSN	0091-6749
DOI	10.1016/j.jaci.2014.06.029
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Article: Recruitment of coregulator complexes to the β-globin gene locus by TFII-I and upstream stimulatory factor

Crusselle-Davis, Valerie J / Zhou, Zhuo / Anantharaman, Archana / Moghimi, Babak / Dodev, Tihomir / Huang, Suming / Bungert, Jörg

FEBS journal. 2007 Dec., v. 274, no. 23

2007

Abstract: Upstream stimulatory factor and TFII-I are ubiquitously expressed helix-loop-helix transcription factors that interact with E-box sequences and or initiator elements. We previously demonstrated that upstream stimulatory factor is an activator of β-globin ...

Abstract	Upstream stimulatory factor and TFII-I are ubiquitously expressed helix-loop-helix transcription factors that interact with E-box sequences and or initiator elements. We previously demonstrated that upstream stimulatory factor is an activator of β-globin gene expression whereas TFII-I is a repressor. In the present study, we demonstrate that upstream stimulatory factor interacts with the coactivator p300 and that this interaction is restricted to erythroid cells expressing the adult β-globin gene. Furthermore, we demonstrate that Suz12, a component of the polycomb repressor complex 2, is recruited to the β-globin gene. Reducing expression of Suz12 significantly activates β-globin gene expression in an erythroid cell line with an embryonic phenotype. Suz12 also interacts with the adult β-globin gene during early stages of erythroid differentiation of mouse embryonic stem cells. Our data suggest that TFII-I contributes to the recruitment of the polycomb repressor complex 2 complex to the β-globin gene. Together, these data demonstrate that the antagonistic activities of upstream stimulatory factor and TFII-I on β-globin gene expression are mediated at least in part by protein complexes that render the promoter associated chromatin accessible or inaccessible for the transcription complex.
Language	English
Dates of publication	2007-12
Size	p. 6065-6073.
Publisher	Blackwell Publishing Ltd
Publishing place	Oxford, UK
Document type	Article
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/j.1742-4658.2007.06128.x
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Article: Functionally Active Fc Mutant Antibodies Recognizing Cancer Antigens Generated Rapidly at High Yields.

Ilieva, Kristina M / Fazekas-Singer, Judit / Achkova, Daniela Y / Dodev, Tihomir S / Mele, Silvia / Crescioli, Silvia / Bax, Heather J / Cheung, Anthony / Karagiannis, Panagiotis / Correa, Isabel / Figini, Mariangela / Marlow, Rebecca / Josephs, Debra H / Beavil, Andrew J / Maher, John / Spicer, James F / Jensen-Jarolim, Erika / Tutt, Andrew N / Karagiannis, Sophia N

Frontiers in immunology

2017 Volume 8, Page(s) 1112

Abstract: Monoclonal antibodies find broad application as therapy for various types of cancer by employing multiple mechanisms of action against tumors. Manipulating the Fc-mediated functions of antibodies that engage immune effector cells, such as NK cells, ... ...

Abstract	Monoclonal antibodies find broad application as therapy for various types of cancer by employing multiple mechanisms of action against tumors. Manipulating the Fc-mediated functions of antibodies that engage immune effector cells, such as NK cells, represents a strategy to influence effector cell activation and to enhance antibody potency and potentially efficacy. We developed a novel approach to generate and ascertain the functional attributes of Fc mutant monoclonal antibodies. This entailed coupling single expression vector (pVitro1) antibody cloning, using polymerase incomplete primer extension (PIPE) polymerase chain reaction, together with simultaneous Fc region point mutagenesis and high yield transient expression in human mammalian cells. Employing this, we engineered wild type, low (N297Q, NQ), and high (S239D/I332E, DE) FcR-binding Fc mutant monoclonal antibody panels recognizing two cancer antigens, HER2/
Language	English
Publishing date	2017-09-11
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2606827-8
ISSN	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2017.01112
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