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Article ; Online: In Vivo Human Single-Chain Fragment Variable Phage Display-Assisted Identification of Galectin-3 as a New Biomarker of Atherosclerosis.

Hemadou, Audrey / Fontayne, Alexandre / Laroche-Traineau, Jeanny / Ottones, Florence / Mondon, Philippe / Claverol, Stéphane / Ducasse, Éric / Sanchez, Stéphane / Mohamad, Sarah / Lorenzato, Cyril / Duonor-Cerutti, Martine / Clofent-Sanchez, Gisèle / Jacobin-Valat, Marie-Josée

Journal of the American Heart Association

2021 Volume 10, Issue 19, Page(s) e016287

Abstract: Background Atherosclerosis is a complex pathology in which dysfunctional endothelium, activated leucocytes, macrophages, and lipid-laden foam cells are implicated, and in which plaque disruption is driven by many putative actors. This study aimed to ... ...

Abstract	Background Atherosclerosis is a complex pathology in which dysfunctional endothelium, activated leucocytes, macrophages, and lipid-laden foam cells are implicated, and in which plaque disruption is driven by many putative actors. This study aimed to identify accurate targetable biomarkers using new in vivo approaches to propose tools for improved diagnosis and treatment. Methods and Results Human scFv (single-chain fragment variable) selected by in vivo phage display in a rabbit model of atherosclerosis was reformatted as scFv fused to the scFv-Fc (single-chain fragment variable fused to the crystallizable fragment of immunoglobulin G format) antibodies. Their reactivity was tested using flow cytometry and immunoassays, and aorta sections from animal models and human carotid and coronary artery specimens. A pool of atherosclerotic proteins from human endarterectomies was co-immunoprecipitated with the selected scFv-Fc followed by mass spectrometry for target identification. Near-infrared fluorescence imaging was performed in
MeSH term(s)	Animals ; Apolipoproteins E ; Atherosclerosis/diagnosis ; Atherosclerosis/genetics ; Bacteriophages ; Biomarkers ; Galectin 3/genetics ; Humans ; Mice ; Plaque, Atherosclerotic ; Rabbits ; Single-Chain Antibodies/genetics
Chemical Substances	Apolipoproteins E ; Biomarkers ; Galectin 3 ; Single-Chain Antibodies
Language	English
Publishing date	2021-09-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2653953-6
ISSN	2047-9980 ; 2047-9980
ISSN (online)	2047-9980
ISSN	2047-9980
DOI	10.1161/JAHA.120.016287
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Article ; Online: A mutated factor X activatable by thrombin corrects bleedings in vivo in a rabbit model of antibody-induced hemophilia A.

Abache, Toufik / Fontayne, Alexandre / Grenier, Dominique / Jacque, Emilie / Longue, Alain / Dezetter, Anne-Sophie / Souilliart, Béatrice / Chevreux, Guillaume / Bataille, Damien / Chtourou, Sami / Plantier, Jean-Luc

Haematologica

2020 Volume 105, Issue 9, Page(s) 2335–2340

Abstract: Rendering coagulation factor X sensitive to thrombin was proposed as a strategy that can bypass the need for factor VIII. In this paper, this non-replacement strategy was evaluated in vitro and in vivo in its ability to correct factor VIII but also ... ...

Abstract	Rendering coagulation factor X sensitive to thrombin was proposed as a strategy that can bypass the need for factor VIII. In this paper, this non-replacement strategy was evaluated in vitro and in vivo in its ability to correct factor VIII but also factor IX, X and XI deficiencies. A novel modified factor X, named Actiten, was generated and produced in the HEK293F cell line. The molecule possesses the required post-translational modifications, partially keeps its ability to be activated by RVV-X, factor VIIa/tissue factor, factor VIIIa/factor IXa and acquires the ability to be activated by thrombin. The potency of the molecule was evaluated in respective deficient plasmas or hemophilia A plasmas, for some with inhibitors. Actiten corrects dose dependently all the assayed deficient plasmas. It is able to normalize the thrombin generation at 20 μg/mL showing however an increased lagtime. It was then assayed in a rabbit antibody-induced model of hemophilia A where, in contrast to recombinant factor X wild-type, it normalized the bleeding time and the loss of hemoglobin. No sign of thrombogenicity was observed and the generation of activated factor X was controlled by the anticoagulation pathway in all performed coagulation assays. This data indicates that Actiten may be considered as a possible non replacement factor to treat hemophilia's with the advantage of being a zymogen correcting bleedings only when needed.
MeSH term(s)	Animals ; Factor IX ; Factor VIII/genetics ; Factor VIIa ; Factor X/genetics ; Hemophilia A/drug therapy ; Hemophilia A/genetics ; Rabbits ; Thrombin
Chemical Substances	Factor VIII (9001-27-8) ; Factor IX (9001-28-9) ; Factor X (9001-29-0) ; Factor VIIa (EC 3.4.21.21) ; Thrombin (EC 3.4.21.5)
Language	English
Publishing date	2020-09-01
Publishing country	Italy
Document type	Journal Article
ZDB-ID	2333-4
ISSN	1592-8721 ; 0017-6567 ; 0390-6078
ISSN (online)	1592-8721
ISSN	0017-6567 ; 0390-6078
DOI	10.3324/haematol.2019.219865
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Article ; Online: Characterization of monoclonal antibodies by a fast and easy liquid chromatography-mass spectrometry time-of-flight analysis on culture supernatant.

Henninot, Antoine / Terrier, Aurelie / Charton, Julie / Urbain, Rémi / Fontayne, Alexandre / Deprez, Benoit / Beghyn, Terence

Analytical biochemistry

2015 Volume 491, Page(s) 52–54

Abstract: Rapid and efficient structural analysis is key to the development of new monoclonal antibodies. We have developed a fast and easy process to obtain mass spectrometry profiles of antibodies from culture supernatant. Treatment of the supernatant with IdeS ... ...

Abstract	Rapid and efficient structural analysis is key to the development of new monoclonal antibodies. We have developed a fast and easy process to obtain mass spectrometry profiles of antibodies from culture supernatant. Treatment of the supernatant with IdeS generates three fragments of 25 kDa that can be analyzed by liquid chromatography-mass spectrometry time-of-flight (LC-MS TOF) in one run: LC, Fd, and Fc/2. This process gives rapid access to isoform and glycoform profiles. To specifically measure the fucosylation yield, we included a one-pot treatment with EndoS that removes the distal glycan heterogeneity. Our process was successfully compared with high-performance capillary electrophoresis with laser-induced fluorescence detection (HPCE-LIF), currently considered as the "gold standard" method.
MeSH term(s)	Antibodies, Monoclonal/analysis ; Chromatography, High Pressure Liquid ; Electrophoresis, Capillary ; Glycosylation ; Protein Isoforms/analysis ; Spectrometry, Fluorescence ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical Substances	Antibodies, Monoclonal ; Protein Isoforms
Language	English
Publishing date	2015-12-15
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2015.08.006
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Article ; Online: Inactivated antithombin as anticoagulant reversal in a rat model of cardiopulmonary bypass: a potent and potentially safer alternative to protamine.

Bianchini, Elsa P / Sebestyen, Alexandre / Abache, Toufik / Bourti, Yasmine / Fontayne, Alexandre / Richard, Vincent / Tamion, Fabienne / Plantier, Jean-Luc / Doguet, Fabien / Borgel, Delphine

British journal of haematology

2018 Volume 180, Issue 5, Page(s) 715–720

Abstract: Heparin anticoagulation followed by protamine reversal is commonly used in cardiopulmonary bypass (CPB). As an alternative to protamine, a recombinant inactive antithrombin (riAT) was designed as an antidote to heparin and was previously shown to be as ... ...

Abstract	Heparin anticoagulation followed by protamine reversal is commonly used in cardiopulmonary bypass (CPB). As an alternative to protamine, a recombinant inactive antithrombin (riAT) was designed as an antidote to heparin and was previously shown to be as potent as protamine in-vitro. In the present study, riAT was assessed for its ability to neutralize heparin after CPB in a rat model. After 60 min of CPB under heparin, rats received 5 mg/kg protamine, 37.5 mg/kg riAT or phosphate buffered saline (PBS) as placebo. Residual anticoagulant activity was assessed using the activated partial thromboplastin time assay before, and 10-30 min after reversion. Haemodynamic monitoring was performed and plasma histamine concentration was also measured. In this model, riAT appeared to be as efficient as protamine in neutralizing heparin. Ten minutes after injection, riAT and protamine both decreased heparin activity, to 1.8 ± 1.3 and 4.5 ± 1.4 u/ml, respectively (23.1 ± 5.1 u/ml in placebo group). Furthermore, evolution of mean carotid arterial pressure, heart rate and plasma histamine levels was comparable in rats treated with PBS or riAT, while protamine exhibited haemodynamic side effects and increased histamine plasma concentration. Thus, riAT could represent an advantage over protamine in CPB because it efficiently reverses heparin activity without negative effects on haemodynamic parameters and plasma histamine level.
MeSH term(s)	Animals ; Anticoagulants/pharmacology ; Antithrombins/pharmacology ; Cardiopulmonary Bypass ; Hemodynamics/drug effects ; Heparin/pharmacology ; Heparin Antagonists/pharmacology ; Histamine/metabolism ; Male ; Protamines/pharmacology ; Rats, Wistar
Chemical Substances	Anticoagulants ; Antithrombins ; Heparin Antagonists ; Protamines ; Histamine (820484N8I3) ; Heparin (9005-49-6)
Language	English
Publishing date	2018-01-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80077-6
ISSN	1365-2141 ; 0007-1048
ISSN (online)	1365-2141
ISSN	0007-1048
DOI	10.1111/bjh.15091
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Article ; Online: Fc Sialylation Prolongs Serum Half-Life of Therapeutic Antibodies.

Bas, Mathilde / Terrier, Aurélie / Jacque, Emilie / Dehenne, Aurélie / Pochet-Béghin, Virginie / Beghin, Cécile / Dezetter, Anne-Sophie / Dupont, Gilles / Engrand, Anaïs / Beaufils, Benjamin / Mondon, Philippe / Fournier, Nathalie / de Romeuf, Christophe / Jorieux, Sylvie / Fontayne, Alexandre / Mars, Lennart T / Monnet, Céline

Journal of immunology (Baltimore, Md. : 1950)

2019 Volume 202, Issue 5, Page(s) 1582–1594

Abstract: ... The long ... ...

Abstract	The long serum
MeSH term(s)	Animals ; Antibodies/blood ; Antibodies/chemistry ; Antibodies/therapeutic use ; HEK293 Cells ; Half-Life ; Humans ; Immunoglobulin Fc Fragments/blood ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin G/blood ; Immunoglobulin G/chemistry ; Immunoglobulin G/therapeutic use ; Mice ; Mice, Knockout
Chemical Substances	Antibodies ; Immunoglobulin Fc Fragments ; Immunoglobulin G
Language	English
Publishing date	2019-01-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.1800896
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Article ; Online: The Dual Targeting of FcRn and FcγRs

Monnet, Céline / Jacque, Emilie / de Romeuf, Christophe / Fontayne, Alexandre / Abache, Toufik / Fournier, Nathalie / Dupont, Gilles / Derache, Delphine / Engrand, Anais / Bauduin, Aurélie / Terrier, Aurélie / Seifert, Alexander / Beghin, Cécile / Longue, Alain / Masiello, Nicholas / Danino, Laetitia / Nogre, Michel / Raia, Anais / Dhainaut, Frederic /

Fauconnier, Louis / Togbe, Dieudonnée / Reitinger, Carmen / Nimmerjahn, Falk / Stevens, Wil / Chtourou, Sami / Mondon, Philippe

Frontiers in immunology

2021 Volume 12, Page(s) 728322

Abstract: Novel molecules that directly target the neonatal Fc receptor (FcRn) and/or Fc gamma receptors (FcγRs) are emerging as promising treatments for immunoglobulin G (IgG)-dependent autoimmune pathologies. Mutated Fc regions and monoclonal antibodies that ... ...

Abstract	Novel molecules that directly target the neonatal Fc receptor (FcRn) and/or Fc gamma receptors (FcγRs) are emerging as promising treatments for immunoglobulin G (IgG)-dependent autoimmune pathologies. Mutated Fc regions and monoclonal antibodies that target FcRn are currently in clinical development and hold promise for reducing the levels of circulating IgG. Additionally, engineered structures containing multimeric Fc regions allow the dual targeting of FcRn and FcγRs; however, their tolerance needs to first be validated in phase I clinical studies. Here, for the first time, we have developed a modified monomeric recombinant Fc optimized for binding to all FcRns and FcγRs without the drawback of possible tolerance associated with FcγR cross-linking. A rational approach using Fc engineering allowed the selection of LFBD192, an Fc with a combination of six mutations that exhibits improved binding to human FcRn and FcγR as well as mouse FcRn and FcγRIV. The potency of LFBD192 was compared with that of intravenous immunoglobulin (IVIg), an FcRn blocker (Fc-MST-HN), and a trimeric Fc that blocks FcRn and/or immune complex-mediated cell activation through FcγR without triggering an immune reaction in several
MeSH term(s)	Animals ; Antirheumatic Agents/metabolism ; Antirheumatic Agents/pharmacology ; Arthritis, Experimental/genetics ; Arthritis, Experimental/immunology ; Arthritis, Experimental/metabolism ; Arthritis, Experimental/prevention & control ; Autoimmunity/drug effects ; Binding, Competitive ; Complement C5a/metabolism ; Female ; Histocompatibility Antigens Class I/genetics ; Histocompatibility Antigens Class I/immunology ; Histocompatibility Antigens Class I/metabolism ; Humans ; Immunoglobulin Fc Fragments/genetics ; Immunoglobulin Fc Fragments/immunology ; Immunoglobulin Fc Fragments/metabolism ; Immunoglobulin Fc Fragments/pharmacology ; Interleukin-2/metabolism ; Jurkat Cells ; Kinetics ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation ; Phagocytosis/drug effects ; Platelet Aggregation/drug effects ; Protein Binding ; Protein Engineering ; Receptors, Fc/antagonists & inhibitors ; Receptors, Fc/genetics ; Receptors, Fc/immunology ; Receptors, Fc/metabolism ; Receptors, IgG/antagonists & inhibitors ; Receptors, IgG/genetics ; Receptors, IgG/immunology ; Receptors, IgG/metabolism ; Secretory Pathway ; Signal Transduction ; THP-1 Cells ; Mice
Chemical Substances	Antirheumatic Agents ; Histocompatibility Antigens Class I ; IL2 protein, human ; Immunoglobulin Fc Fragments ; Interleukin-2 ; Receptors, Fc ; Receptors, IgG ; Complement C5a (80295-54-1) ; Fc receptor, neonatal (TW3XAW0RCY)
Language	English
Publishing date	2021-08-26
Publishing country	Switzerland
Document type	Comparative Study ; 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.2021.728322
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Article ; Online: An innovative flow cytometry method to screen human scFv-phages selected by in vivo phage-display in an animal model of atherosclerosis.

Hemadou, Audrey / Laroche-Traineau, Jeanny / Antoine, Ségolène / Mondon, Philippe / Fontayne, Alexandre / Le Priol, Yannick / Claverol, Stéphane / Sanchez, Stéphane / Cerutti, Martine / Ottones, Florence / Clofent-Sanchez, Gisèle / Jacobin-Valat, Marie-Josée

Scientific reports

2018 Volume 8, Issue 1, Page(s) 15016

Abstract: Atherosclerosis is a chronic, progressive inflammatory disease that may develop into vulnerable lesions leading to thrombosis. This pathology is characterized by the deposition of lipids within the arterial wall and infiltration of immune cells leading ... ...

Abstract	Atherosclerosis is a chronic, progressive inflammatory disease that may develop into vulnerable lesions leading to thrombosis. This pathology is characterized by the deposition of lipids within the arterial wall and infiltration of immune cells leading to amplification of inflammation. Nowadays there is a rising interest to assess directly the molecular and cellular components that underlie the clinical condition of stroke and myocardial infarction. Single chain fragment variable (scFv)-phages issuing from a human combinatorial library were selected on the lesions induced in a rabbit model of atherosclerosis after three rounds of in vivo phage display. We further implemented a high-throughput flow cytometry method on rabbit protein extracts to individually test one thousand of scFv-phages. Two hundred and nine clones were retrieved on the basis of their specificity for atherosclerotic proteins. Immunohistochemistry assays confirmed the robustness of the designed cytometry protocol. Sequencing of candidates demonstrated their high diversity in VH and VL germline usage. The large number of candidates and their diversity open the way in the discovery of new biomarkers. Here, we successfully showed the capacity of combining in vivo phage display and high-throughput cytometry strategies to give new insights in in vivo targetable up-regulated biomarkers in atherosclerosis.
MeSH term(s)	Animals ; Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/immunology ; Atherosclerosis/genetics ; Atherosclerosis/immunology ; Atherosclerosis/pathology ; Cell Surface Display Techniques ; Disease Models, Animal ; Flow Cytometry ; Humans ; Immunohistochemistry/methods ; Rabbits ; Single-Chain Antibodies/immunology ; Single-Chain Antibodies/isolation & purification
Chemical Substances	Antibodies, Monoclonal ; Single-Chain Antibodies
Language	English
Publishing date	2018-10-09
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/s41598-018-33382-2
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Article: Characterization of monoclonal antibodies by a fast and easy liquid chromatography–mass spectrometry time-of-flight analysis on culture supernatant

Henninot, Antoine / Alexandre Fontayne / Aurelie Terrier / Benoit Deprez / Julie Charton / Rémi Urbain / Terence Beghyn

Analytical biochemistry. 2015 Dec. 15, v. 491

2015

Abstract	Rapid and efficient structural analysis is key to the development of new monoclonal antibodies. We have developed a fast and easy process to obtain mass spectrometry profiles of antibodies from culture supernatant. Treatment of the supernatant with IdeS generates three fragments of 25 kDa that can be analyzed by liquid chromatography–mass spectrometry time-of-flight (LC–MS TOF) in one run: LC, Fd, and Fc/2. This process gives rapid access to isoform and glycoform profiles. To specifically measure the fucosylation yield, we included a one-pot treatment with EndoS that removes the distal glycan heterogeneity. Our process was successfully compared with high-performance capillary electrophoresis with laser-induced fluorescence detection (HPCE–LIF), currently considered as the “gold standard” method.
Keywords	capillary electrophoresis ; fluorescence ; liquid chromatography ; mass spectrometry ; monoclonal antibodies
Language	English
Dates of publication	2015-1215
Size	p. 52-54.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2015.08.006
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Article: Selection of IgG Variants with Increased FcRn Binding Using Random and Directed Mutagenesis: Impact on Effector Functions.

Monnet, Céline / Jorieux, Sylvie / Urbain, Rémi / Fournier, Nathalie / Bouayadi, Khalil / De Romeuf, Christophe / Behrens, Christian K / Fontayne, Alexandre / Mondon, Philippe

Frontiers in immunology

2015 Volume 6, Page(s) 39

Abstract: Despite the reasonably long half-life of immunoglogulin G (IgGs), market pressure for higher patient convenience while conserving efficacy continues to drive IgG half-life improvement. IgG half-life is dependent on the neonatal Fc receptor (FcRn), which ... ...

Abstract	Despite the reasonably long half-life of immunoglogulin G (IgGs), market pressure for higher patient convenience while conserving efficacy continues to drive IgG half-life improvement. IgG half-life is dependent on the neonatal Fc receptor (FcRn), which among other functions, protects IgG from catabolism. FcRn binds the Fc domain of IgG at an acidic pH ensuring that endocytosed IgG will not be degraded in lysosomal compartments and will then be released into the bloodstream. Consistent with this mechanism of action, several Fc-engineered IgG with increased FcRn affinity and conserved pH dependency were designed and resulted in longer half-life in vivo in human FcRn-transgenic mice (hFcRn), cynomolgus monkeys, and recently in healthy humans. These IgG variants were usually obtained by in silico approaches or directed mutagenesis in the FcRn-binding site. Using random mutagenesis, combined with a pH-dependent phage display selection process, we isolated IgG variants with improved FcRn-binding, which exhibited longer in vivo half-life in hFcRn mice. Interestingly, many mutations enhancing Fc/FcRn interaction were located at a distance from the FcRn-binding site validating our random molecular approach. Directed mutagenesis was then applied to generate new variants to further characterize our IgG variants and the effect of the mutations selected. Since these mutations are distributed over the whole Fc sequence, binding to other Fc effectors, such as complement C1q and FcγRs, was dramatically modified, even by mutations distant from these effectors' binding sites. Hence, we obtained numerous IgG variants with increased FcRn-binding and different binding patterns to other Fc effectors, including variants without any effector function, providing distinct "fit-for-purpose" Fc molecules. We therefore provide evidence that half-life and effector functions should be optimized simultaneously as mutations can have unexpected effects on all Fc receptors that are critical for IgG therapeutic efficacy.
Language	English
Publishing date	2015
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2606827-8
ISSN	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2015.00039
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Article ; Online: The European AntibotABE Framework Program and Its Update: Development of Innovative Botulinum Antibodies.

Rasetti-Escargueil, Christine / Avril, Arnaud / Miethe, Sebastian / Mazuet, Christelle / Derman, Yagmur / Selby, Katja / Thullier, Philippe / Pelat, Thibaut / Urbain, Remi / Fontayne, Alexandre / Korkeala, Hannu / Sesardic, Dorothea / Hust, Michael / Popoff, Michel R

Toxins

2017 Volume 9, Issue 10

Abstract: The goal of the AntiBotABE Program was the development of recombinant antibodies that neutralize botulinum neurotoxins (BoNT) A, B and E. These serotypes are lethal and responsible for most human botulinum cases. To improve therapeutic efficacy, the ... ...

Abstract	The goal of the AntiBotABE Program was the development of recombinant antibodies that neutralize botulinum neurotoxins (BoNT) A, B and E. These serotypes are lethal and responsible for most human botulinum cases. To improve therapeutic efficacy, the heavy and light chains (HC and LC) of the three BoNT serotypes were targeted to achieve a synergistic effect (oligoclonal antibodies). For antibody isolation, macaques were immunized with the recombinant and non-toxic BoNT/A, B or E, HC or LC, followed by the generation of immune phage-display libraries. Antibodies were selected from these libraries against the holotoxin and further analyzed in in vitro and ex vivo assays. For each library, the best ex vivo neutralizing antibody fragments were germline-humanized and expressed as immunoglobulin G (IgGs). The IgGs were tested in vivo, in a standardized model of protection, and challenged with toxins obtained from collections of
MeSH term(s)	Animals ; Antibodies, Neutralizing/immunology ; Botulinum Toxins/immunology ; Humans ; Immunization ; Neurotoxins/immunology ; Recombinant Proteins/immunology ; Single-Chain Antibodies/immunology
Chemical Substances	Antibodies, Neutralizing ; Neurotoxins ; Recombinant Proteins ; Single-Chain Antibodies ; Botulinum Toxins (EC 3.4.24.69)
Language	English
Publishing date	2017--02
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2518395-3
ISSN	2072-6651 ; 2072-6651
ISSN (online)	2072-6651
ISSN	2072-6651
DOI	10.3390/toxins9100309
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