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  1. Article ; Online: High-resolution map of the Fc functions mediated by COVID-19-neutralizing antibodies.

    Paciello, Ida / Maccari, Giuseppe / Pantano, Elisa / Andreano, Emanuele / Rappuoli, Rino

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

    2024  Volume 121, Issue 3, Page(s) e2314730121

    Abstract: A growing body of evidence shows that fragment crystallizable (Fc)-dependent antibody effector functions play an important role in protection from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. To unravel the mechanisms that ... ...

    Abstract A growing body of evidence shows that fragment crystallizable (Fc)-dependent antibody effector functions play an important role in protection from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. To unravel the mechanisms that drive these responses, we analyzed the phagocytosis and complement deposition mediated by a panel of 482 human monoclonal antibodies (nAbs) neutralizing the original Wuhan virus, expressed as recombinant IgG1. Our study confirmed that nAbs no longer neutralizing SARS-CoV-2 Omicron variants can retain their Fc functions. Surprisingly, we found that nAbs with the most potent Fc function recognize the N-terminal domain, followed by those targeting class 3 epitopes in the receptor binding domain. Interestingly, nAbs direct against the class 1/2 epitopes in the receptor binding motif, which are the most potent in neutralizing the virus, were the weakest in Fc functions. The divergent properties of the neutralizing and Fc function-mediating antibodies were confirmed by the use of different B cell germlines and by the observation that Fc functions of polyclonal sera differ from the profile observed with nAbs, suggesting that non-neutralizing antibodies also contribute to Fc functions. These data provide a high-resolution picture of the Fc-antibody response to SARS-CoV-2 and suggest that the Fc contribution should be considered for the design of improved vaccines, the selection of therapeutic antibodies, and the evaluation of correlates of protection.
    MeSH term(s) Humans ; Antibodies, Neutralizing ; COVID-19 ; SARS-CoV-2 ; Epitopes
    Chemical Substances Antibodies, Neutralizing ; Epitopes
    Language English
    Publishing date 2024-01-10
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2314730121
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    Zs.A 1148: Show issues Location:
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  2. Article ; Online: SARS-CoV-2 escaped natural immunity, raising questions about vaccines and therapies.

    Andreano, Emanuele / Rappuoli, Rino

    Nature medicine

    2021  Volume 27, Issue 5, Page(s) 759–761

    MeSH term(s) COVID-19/prevention & control ; Humans ; Immune Evasion ; Immunity, Innate/immunology ; SARS-CoV-2/immunology ; Viral Vaccines/immunology
    Chemical Substances Viral Vaccines
    Language English
    Publishing date 2021-04-20
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1220066-9
    ISSN 1546-170X ; 1078-8956
    ISSN (online) 1546-170X
    ISSN 1078-8956
    DOI 10.1038/s41591-021-01347-0
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  3. Article ; Online: Immunodominant antibody germlines in COVID-19.

    Andreano, Emanuele / Rappuoli, Rino

    The Journal of experimental medicine

    2021  Volume 218, Issue 5

    Abstract: The neutralizing antibody response to SARS-CoV-2 is dominated by antibodies deriving from germlines IGHV3-53/IGHV3-66, which are also associated with self-reacting antibodies. Could vaccines avoid the expansion of this immunodominant response, decrease ... ...

    Abstract The neutralizing antibody response to SARS-CoV-2 is dominated by antibodies deriving from germlines IGHV3-53/IGHV3-66, which are also associated with self-reacting antibodies. Could vaccines avoid the expansion of this immunodominant response, decrease the risk of autoimmunity, and still protect against emerging SARS-CoV-2 variants?
    MeSH term(s) Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; Antigens, Viral/immunology ; COVID-19/genetics ; COVID-19/immunology ; COVID-19/virology ; Germ Cells/immunology ; Host-Pathogen Interactions/genetics ; Host-Pathogen Interactions/immunology ; Humans ; SARS-CoV-2/immunology
    Chemical Substances Antibodies, Neutralizing ; Antibodies, Viral ; Antigens, Viral
    Language English
    Publishing date 2021-03-02
    Publishing country United States
    Document type Letter ; Research Support, Non-U.S. Gov't
    ZDB-ID 218343-2
    ISSN 1540-9538 ; 0022-1007
    ISSN (online) 1540-9538
    ISSN 0022-1007
    DOI 10.1084/jem.20210281
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  4. Article ; Online: Deep-learning image analysis for high-throughput screening of opsono-phagocytosis-promoting monoclonal antibodies against Neisseria gonorrhoeae.

    Vacca, Fabiola / Cardamone, Dario / Andreano, Emanuele / Medini, Duccio / Rappuoli, Rino / Sala, Claudia

    Scientific reports

    2024  Volume 14, Issue 1, Page(s) 4807

    Abstract: Antimicrobial resistance (AMR) is nowadays a global health concern as bacterial pathogens are increasingly developing resistance to antibiotics. Monoclonal antibodies (mAbs) represent a powerful tool for addressing AMR thanks to their high specificity ... ...

    Abstract Antimicrobial resistance (AMR) is nowadays a global health concern as bacterial pathogens are increasingly developing resistance to antibiotics. Monoclonal antibodies (mAbs) represent a powerful tool for addressing AMR thanks to their high specificity for pathogenic bacteria which allows sparing the microbiota, kill bacteria through complement deposition, enhance phagocytosis or inhibit bacterial adhesion to epithelial cells. Here we describe a visual opsono-phagocytosis assay which relies on confocal microscopy to measure the impact of mAbs on phagocytosis of the bacterium Neisseria gonorrhoeae by macrophages. With respect to traditional CFU-based assays, generated images can be automatically analysed by convolutional neural networks. Our results demonstrate that confocal microscopy and deep learning-based analysis allow screening for phagocytosis-promoting mAbs against N. gonorrhoeae, even when mAbs are not purified and are expressed at low concentration. Ultimately, the flexibility of the staining protocol and of the deep-learning approach make the assay suitable for other bacterial species and cell lines where mAb activity needs to be investigated.
    MeSH term(s) Humans ; Neisseria gonorrhoeae ; Antibodies, Monoclonal ; High-Throughput Screening Assays ; Deep Learning ; Anti-Bacterial Agents/pharmacology ; Phagocytosis ; Gonorrhea
    Chemical Substances Antibodies, Monoclonal ; Anti-Bacterial Agents
    Language English
    Publishing date 2024-02-27
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-024-55606-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Epitope Mapping of Human Polyclonal Antibodies to the fHbp Antigen of a Neisseria Meningitidis Vaccine by Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS).

    Grauslund, Laura R / Ständer, Susanne / Veggi, Daniele / Andreano, Emanuele / Rand, Kasper D / Norais, Nathalie

    Molecular & cellular proteomics : MCP

    2024  Volume 23, Issue 3, Page(s) 100734

    Abstract: Antigen-antibody interactions play a key role in the immune response post vaccination and the mechanism of action of antibody-based biopharmaceuticals. 4CMenB is a multicomponent vaccine against Neisseria meningitidis serogroup B in which factor H ... ...

    Abstract Antigen-antibody interactions play a key role in the immune response post vaccination and the mechanism of action of antibody-based biopharmaceuticals. 4CMenB is a multicomponent vaccine against Neisseria meningitidis serogroup B in which factor H binding protein (fHbp) is one of the key antigens. In this study, we use hydrogen/deuterium exchange mass spectrometry (HDX-MS) to identify epitopes in fHbp recognized by polyclonal antibodies (pAb) from two human donors (HDs) vaccinated with 4CMenB. Our HDX-MS data reveal several epitopes recognized by the complex mixture of human pAb. Furthermore, we show that the pAb from the two HDs recognize the same epitope regions. Epitope mapping of total pAb and purified fHbp-specific pAb from the same HD reveals that the two antibody samples recognize the same main epitopes, showing that HDX-MS based epitope mapping can, in this case at least, be performed directly using total IgG pAb samples that have not undergone Ab-selective purification. Two monoclonal antibodies (mAb) were previously produced from B-cell repertoire sequences from one of the HDs and used for epitope mapping of fHbp with HDX-MS. The epitopes identified for the pAb from the same HD in this study, overlap with the epitopes recognized by the two individual mAbs. Overall, HDX-MS epitope mapping appears highly suitable for simultaneous identification of epitopes recognized by pAb from human donors and to thus both guide vaccine development and study basic human immunity to pathogens, including viruses.
    MeSH term(s) Humans ; Epitope Mapping/methods ; Neisseria meningitidis/metabolism ; Deuterium/metabolism ; Bacterial Proteins/metabolism ; Meningococcal Infections/prevention & control ; Carrier Proteins ; Deuterium Exchange Measurement ; Complement Factor H ; Meningococcal Vaccines ; Antigens, Bacterial ; Epitopes ; Antibodies, Monoclonal/metabolism ; Hydrogen Deuterium Exchange-Mass Spectrometry
    Chemical Substances Deuterium (AR09D82C7G) ; Bacterial Proteins ; Carrier Proteins ; Complement Factor H (80295-65-4) ; Meningococcal Vaccines ; Antigens, Bacterial ; Epitopes ; Antibodies, Monoclonal
    Language English
    Publishing date 2024-02-09
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2075924-1
    ISSN 1535-9484 ; 1535-9476
    ISSN (online) 1535-9484
    ISSN 1535-9476
    DOI 10.1016/j.mcpro.2024.100734
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    Zs.A 5599: Show issues Location:
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  6. Article: High-throughput bactericidal assays for monoclonal antibody screening against antimicrobial resistant

    Stazzoni, Samuele / Troisi, Marco / Abbiento, Valentina / Sala, Claudia / Andreano, Emanuele / Rappuoli, Rino

    Frontiers in microbiology

    2023  Volume 14, Page(s) 1243427

    Abstract: Neisseria ... ...

    Abstract Neisseria gonorrhoeae
    Language English
    Publishing date 2023-08-16
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2023.1243427
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  7. Article ; Online: Emerging roles of SARS-CoV-2 Spike-ACE2 in immune evasion and pathogenesis.

    Baldari, Cosima T / Onnis, Anna / Andreano, Emanuele / Del Giudice, Giuseppe / Rappuoli, Rino

    Trends in immunology

    2023  Volume 44, Issue 6, Page(s) 424–434

    Abstract: The COVID-19 pandemic, caused by SARS-CoV-2, has caused an estimated 5 billion infections and 20 million deaths by respiratory failure. In addition to the respiratory disease, SARS-CoV-2 infection has been associated with many extrapulmonary ... ...

    Abstract The COVID-19 pandemic, caused by SARS-CoV-2, has caused an estimated 5 billion infections and 20 million deaths by respiratory failure. In addition to the respiratory disease, SARS-CoV-2 infection has been associated with many extrapulmonary complications not easily explainable by the respiratory infection. A recent study showed that the SARS-CoV-2 spike protein, which mediates cell entry by binding to the angiotensin-converting enzyme 2 (ACE2) receptor, signals through ACE2 to change host cell behavior. In CD8
    MeSH term(s) Humans ; Angiotensin-Converting Enzyme 2/metabolism ; CD8-Positive T-Lymphocytes/metabolism ; COVID-19 ; Immune Evasion ; Pandemics ; Protein Binding ; SARS-CoV-2/metabolism
    Chemical Substances Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23)
    Language English
    Publishing date 2023-04-06
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2036831-8
    ISSN 1471-4981 ; 1471-4906
    ISSN (online) 1471-4981
    ISSN 1471-4906
    DOI 10.1016/j.it.2023.04.001
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  8. Article: 2D NMR Analysis as a Sensitive Tool for Evaluating the Higher-Order Structural Integrity of Monoclonal Antibody against COVID-19.

    Cantini, Francesca / Andreano, Emanuele / Paciello, Ida / Ghini, Veronica / Berti, Francesco / Rappuoli, Rino / Banci, Lucia

    Pharmaceutics

    2022  Volume 14, Issue 10

    Abstract: The higher-order structure (HOS) of protein therapeutics has been confirmed as a critical quality parameter. In this study, we compared ... ...

    Abstract The higher-order structure (HOS) of protein therapeutics has been confirmed as a critical quality parameter. In this study, we compared 2D
    Language English
    Publishing date 2022-09-20
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2527217-2
    ISSN 1999-4923
    ISSN 1999-4923
    DOI 10.3390/pharmaceutics14101981
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  9. Article ; Online: High-resolution map of the Fc-functions mediated by COVID-19 neutralizing antibodies

    Paciello, Ida / Maccari, Giuseppe / Pantano, Elisa / Andreano, Emanuele / Rappuoli, Rino

    bioRxiv

    Abstract: A growing body of evidence shows that Fc-dependent antibody effector functions play an important role in protection from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. To unravel the mechanisms that drive these responses, we ... ...

    Abstract A growing body of evidence shows that Fc-dependent antibody effector functions play an important role in protection from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. To unravel the mechanisms that drive these responses, we analyzed the phagocytosis and complement deposition mediated by a panel of 482 human monoclonal antibodies (nAbs) neutralizing the original Wuhan virus, expressed as recombinant IgG1. Our study confirmed that nAbs no longer neutralizing SARS-CoV-2 Omicron variants can retain their Fc-functions. Surprisingly, we found that nAbs with the most potent Fc-function recognize the N-terminal domain, followed by those targeting Class 3 epitopes in the receptor binding domain. Interestingly, nAbs direct against the Class 1/2 epitopes in the receptor binding motif, which are the most potent in neutralizing the virus, were the weakest in Fc-functions. The divergent properties of the neutralizing and Fc-function mediating antibodies were confirmed by the use of different B cell germlines and by the observation that Fc-functions of polyclonal sera differ from the profile observed with nAbs, suggesting that not-neutralizing antibodies also contribute to Fc-functions. These data provide a high-resolution picture of the Fc-antibody response to SARS-CoV-2 and suggest that the Fc contribution should be considered for the design of improved vaccines, the selection of therapeutic antibodies and the evaluation of correlates of protection.
    Keywords covid19
    Language English
    Publishing date 2023-07-10
    Publisher Cold Spring Harbor Laboratory
    Document type Article ; Online
    DOI 10.1101/2023.07.10.548360
    Database COVID19

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  10. Article ; Online: Human monoclonal antibodies for discovery, therapy, and vaccine acceleration.

    Andreano, Emanuele / Seubert, Anja / Rappuoli, Rino

    Current opinion in immunology

    2019  Volume 59, Page(s) 130–134

    Abstract: Screening of single B cells from convalescent or vaccinated people allows the discovery of novel targets for infectious diseases and rapid production of engineered human monoclonal antibodies (mAbs) that can prevent or control infections by passive ... ...

    Abstract Screening of single B cells from convalescent or vaccinated people allows the discovery of novel targets for infectious diseases and rapid production of engineered human monoclonal antibodies (mAbs) that can prevent or control infections by passive immunization. Here we propose that the development of human mAbs can also significantly accelerate vaccine development by anticipating some of the key biological and regulatory questions.
    MeSH term(s) Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/therapeutic use ; Antibodies, Neutralizing/metabolism ; Antibodies, Viral/metabolism ; Antineoplastic Agents, Immunological/therapeutic use ; B-Lymphocytes/physiology ; Bioengineering ; Communicable Disease Control ; Humans ; Immunotherapy/methods ; Neoplasms/immunology ; Neoplasms/therapy ; Single-Cell Analysis ; Vaccines/immunology ; Virus Diseases/immunology
    Chemical Substances Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Antineoplastic Agents, Immunological ; Vaccines
    Language English
    Publishing date 2019-08-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1035767-1
    ISSN 1879-0372 ; 0952-7915
    ISSN (online) 1879-0372
    ISSN 0952-7915
    DOI 10.1016/j.coi.2019.07.005
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