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  1. Article ; Online: Hyper-Enriched Anti-RSV Immunoglobulins Nasally Administered: A Promising Approach for Respiratory Syncytial Virus Prophylaxis.

    Jacque, Emilie / Chottin, Claire / Laubreton, Daphné / Nogre, Michel / Ferret, Cécile / de Marcos, Sandrine / Baptista, Linda / Drajac, Carole / Mondon, Philippe / De Romeuf, Christophe / Rameix-Welti, Marie-Anne / Eléouët, Jean-François / Chtourou, Sami / Riffault, Sabine / Perret, Gérald / Descamps, Delphyne

    Frontiers in immunology

    2021  Volume 12, Page(s) 683902

    Abstract: Respiratory syncytial virus (RSV) is a public health concern that causes acute lower respiratory tract infection. So far, no vaccine candidate under development has reached the market and the only licensed product to prevent RSV infection in at-risk ... ...

    Abstract Respiratory syncytial virus (RSV) is a public health concern that causes acute lower respiratory tract infection. So far, no vaccine candidate under development has reached the market and the only licensed product to prevent RSV infection in at-risk infants and young children is a monoclonal antibody (Synagis
    Importance: Respiratory Syncytial Virus (RSV) is the major cause of acute lower respiratory infections in children, and is also recognized as a cause of morbidity in the elderly. There are still no vaccines and no efficient antiviral therapy against this virus. Here, we described an approach of passive immunization with a new class of hyper-enriched anti-RSV immunoglobulins (Ig) manufactured from human normal plasma. This new class of immunoglobulin plasma derived product is generated by an innovative bioprocess, called Ig cracking, which requires a combination of expertise in both plasma derived products and affinity chromatography. The strong efficacy in a small volume of these hyper-enriched anti-RSV IgG to inhibit the viral infection was demonstrated using a mouse model. This new class of immunoglobulin plasma-derived products could be applied to other pathogens to address specific therapeutic needs in the field of infectious diseases or even pandemics, such as COVID-19.
    MeSH term(s) Administration, Intranasal ; Animals ; Antibodies, Viral/administration & dosage ; Antibodies, Viral/immunology ; Antibodies, Viral/isolation & purification ; Disease Models, Animal ; Humans ; Immunization, Passive ; Immunoglobulin G/administration & dosage ; Immunoglobulin G/immunology ; Immunoglobulin G/isolation & purification ; Lung/drug effects ; Lung/virology ; Neutralization Tests ; Respiratory Syncytial Virus Infections/prevention & control ; Respiratory Syncytial Virus Infections/virology ; Respiratory Syncytial Virus, Human/immunology ; Turbinates/drug effects ; Turbinates/virology ; Viral Fusion Proteins/immunology ; Virus Replication/drug effects
    Chemical Substances Antibodies, Viral ; F protein, human respiratory syncytial virus ; Immunoglobulin G ; Viral Fusion Proteins
    Language English
    Publishing date 2021-06-07
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2021.683902
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. 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
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: DNA aptamer affinity ligands for highly selective purification of human plasma-related proteins from multiple sources.

    Forier, Cynthia / Boschetti, Egisto / Ouhammouch, Mohamed / Cibiel, Agnès / Ducongé, Frédéric / Nogré, Michel / Tellier, Michel / Bataille, Damien / Bihoreau, Nicolas / Santambien, Patrick / Chtourou, Sami / Perret, Gérald

    Journal of chromatography. A

    2017  Volume 1489, Page(s) 39–50

    Abstract: Nucleic acid aptamers are promising ligands for analytical and preparative-scale affinity chromatography applications. However, a full industrial exploitation requires that aptamer-grafted chromatography media provide a number of high technical standards ...

    Abstract Nucleic acid aptamers are promising ligands for analytical and preparative-scale affinity chromatography applications. However, a full industrial exploitation requires that aptamer-grafted chromatography media provide a number of high technical standards that remained largely untested. Ideally, they should exhibit relatively high binding capacity associated to a very high degree of specificity. In addition, they must be highly resistant to harsh cleaning/sanitization conditions, as well as to prolonged and repeated exposure to biological environment. Here, we present practical examples of aptamer affinity chromatography for the purification of three human therapeutic proteins from various sources: Factor VII, Factor H and Factor IX. In a single chromatographic step, three DNA aptamer ligands enabled the efficient purification of their target protein, with an unprecedented degree of selectivity (from 0.5% to 98% of purity in one step). Furthermore, these aptamers demonstrated a high stability under harsh sanitization conditions (100h soaking in 1M NaOH). These results pave the way toward a wider adoption of aptamer-based affinity ligands in the industrial-scale purification of not only plasma-derived proteins but also of any other protein in general.
    MeSH term(s) Aptamers, Nucleotide/chemistry ; Blood Proteins/isolation & purification ; Chromatography, Affinity/methods ; DNA/chemistry ; Humans ; Ligands
    Chemical Substances Aptamers, Nucleotide ; Blood Proteins ; Ligands ; DNA (9007-49-2)
    Language English
    Publishing date 2017-03-17
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1171488-8
    ISSN 1873-3778 ; 0021-9673
    ISSN (online) 1873-3778
    ISSN 0021-9673
    DOI 10.1016/j.chroma.2017.01.031
    Database MEDical Literature Analysis and Retrieval System OnLINE

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