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  1. Article: Antibody Focusing to Conserved Sites of Vulnerability: The Immunological Pathways for 'Universal' Influenza Vaccines.

    Sangesland, Maya / Lingwood, Daniel

    Vaccines

    2021  Volume 9, Issue 2

    Abstract: Influenza virus remains a serious public health burden due to ongoing viral evolution. Vaccination remains the best measure of prophylaxis, yet current seasonal vaccines elicit strain-specific neutralizing responses that favor the hypervariable epitopes ... ...

    Abstract Influenza virus remains a serious public health burden due to ongoing viral evolution. Vaccination remains the best measure of prophylaxis, yet current seasonal vaccines elicit strain-specific neutralizing responses that favor the hypervariable epitopes on the virus. This necessitates yearly reformulations of seasonal vaccines, which can be limited in efficacy and also shortchange pandemic preparedness. Universal vaccine development aims to overcome these deficits by redirecting antibody responses to functionally conserved sites of viral vulnerability to enable broad coverage. However, this is challenging as such antibodies are largely immunologically silent, both following vaccination and infection. Defining and then overcoming the immunological basis for such subdominant or 'immuno-recessive' antibody targeting has thus become an important aspect of universal vaccine development. This, coupled with structure-guided immunogen design, has led to proof-of-concept that it is possible to rationally refocus humoral immunity upon normally 'unseen' broadly neutralizing antibody targets on influenza virus.
    Language English
    Publishing date 2021-02-05
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2703319-3
    ISSN 2076-393X
    ISSN 2076-393X
    DOI 10.3390/vaccines9020125
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Public Immunity: Evolutionary Spandrels for Pathway-Amplifying Protective Antibodies.

    Sangesland, Maya / Lingwood, Daniel

    Frontiers in immunology

    2021  Volume 12, Page(s) 708882

    Abstract: Humoral immunity is seeded by affinity between the B cell receptor (BCR) and cognate antigen. While the BCR is a chimeric display of diverse antigen engagement solutions, we discuss its functional activity as an 'innate-like' immune receptor, wherein ... ...

    Abstract Humoral immunity is seeded by affinity between the B cell receptor (BCR) and cognate antigen. While the BCR is a chimeric display of diverse antigen engagement solutions, we discuss its functional activity as an 'innate-like' immune receptor, wherein genetically hardwired antigen complementarity can serve as reproducible templates for pathway-amplifying otherwise immunologically recessive antibody responses. We propose that the capacity for germline reactivity to new antigen emerged as a set of evolutionary spandrels or coupled traits, which can now be exploited by rational vaccine design to focus humoral immunity upon conventionally immune-subdominant antibody targets. Accordingly, we suggest that evolutionary spandrels account for the necessary but unanticipated antigen reactivity of the germline antibody repertoire.
    MeSH term(s) Antibodies, Neutralizing/immunology ; Humans ; Immunity, Humoral/immunology ; Receptors, Antigen, B-Cell/immunology
    Chemical Substances Antibodies, Neutralizing ; Receptors, Antigen, B-Cell
    Language English
    Publishing date 2021-12-09
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2021.708882
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Repeated vaccination with homologous influenza hemagglutinin broadens human antibody responses to unmatched flu viruses.

    Deng, Yixiang / Tang, Melbourne / Ross, Ted M / Schmidt, Aaron G / Chakraborty, Arup K / Lingwood, Daniel

    medRxiv : the preprint server for health sciences

    2024  

    Abstract: The on-going diversification of influenza virus necessicates annual vaccine updating. The vaccine antigen, the viral spike protein hemagglutinin (HA), tends to elicit strain-specific neutralizing activity, predicting that sequential immunization with the ...

    Abstract The on-going diversification of influenza virus necessicates annual vaccine updating. The vaccine antigen, the viral spike protein hemagglutinin (HA), tends to elicit strain-specific neutralizing activity, predicting that sequential immunization with the same HA strain will boost antibodies with narrow coverage. However, repeated vaccination with homologous SARS-CoV-2 vaccine eventually elicits neutralizing activity against highly unmatched variants, questioning this immunological premise. We evaluated a longitudinal influenza vaccine cohort, where each year the subjects received the same, novel H1N1 2009 pandemic vaccine strain. Repeated vaccination gradually enhanced receptor-blocking antibodies (HAI) to highly unmatched H1N1 strains within individuals with no initial memory recall against these historical viruses. An
    Language English
    Publishing date 2024-03-29
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.03.27.24303943
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Lipocalin 2 as a membrane-reorganizing agent.

    Lingwood, Daniel

    Science signaling

    2014  Volume 7, Issue 338, Page(s) pe19

    Abstract: Lipocalins are a class of proteins that scavenge hydrophobic molecules in diverse contexts, including the immune system, the nervous system, and cancer. A recent study by Watanbe et al. identifies lipocalin 2 produced by the female mouse reproductive ... ...

    Abstract Lipocalins are a class of proteins that scavenge hydrophobic molecules in diverse contexts, including the immune system, the nervous system, and cancer. A recent study by Watanbe et al. identifies lipocalin 2 produced by the female mouse reproductive tract as a sperm-capacitating agent that alters the membrane properties of sperm in preparation for fertilization. The potential for lipocalins to act as general modulators of plasma membrane bioactivity is discussed.
    MeSH term(s) Acute-Phase Proteins/chemistry ; Acute-Phase Proteins/metabolism ; Allosteric Regulation/physiology ; Animals ; Cell Membrane/metabolism ; Female ; Gangliosidosis, GM1/metabolism ; Lipocalin-2 ; Lipocalins/chemistry ; Lipocalins/metabolism ; Male ; Membrane Microdomains/metabolism ; Mice ; Models, Biological ; Oncogene Proteins/chemistry ; Oncogene Proteins/metabolism ; Sperm Capacitation/physiology
    Chemical Substances Acute-Phase Proteins ; Lipocalin-2 ; Lipocalins ; Oncogene Proteins ; Lcn2 protein, mouse (126469-30-5)
    Language English
    Publishing date 2014-08-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2417226-1
    ISSN 1937-9145 ; 1945-0877
    ISSN (online) 1937-9145
    ISSN 1945-0877
    DOI 10.1126/scisignal.2005563
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: An Approach for Antigen-Agnostic Identification of Virus-Like Particle-Displayed Epitopes that Engage Specific Antibody V Gene Regions.

    Peabody, Julianne / Core, Susan B / Ronsard, Larance / Lingwood, Daniel / Peabody, David S / Chackerian, Bryce

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

    2023  Volume 2720, Page(s) 55–74

    Abstract: Antibody complementarity determining regions (CDRs) participate in antigen recognition, but not all participate equally in antigen binding. Here we describe a technique for discovering strong, specific binding partners to defined motifs within the CDRs ... ...

    Abstract Antibody complementarity determining regions (CDRs) participate in antigen recognition, but not all participate equally in antigen binding. Here we describe a technique for discovering strong, specific binding partners to defined motifs within the CDRs of chimeric, engineered antibodies using affinity selection and counter-selection of epitopes displayed on bacteriophage MS2-based virus-like particles (VLPs). As an example, we show how this technique can be used to identify families of VLPs that interact with antibodies displaying the CDRs encoded by the germline precursor of a broadly neutralizing monoclonal antibody against HIV-1.
    Language English
    Publishing date 2023-09-29
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3469-1_4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Lupus-associated innate receptors drive extrafollicular evolution of autoreactive B cells.

    Zhu, Danni Yi-Dan / Maurer, Daniel P / Castrillon, Carlos / Deng, Yixiang / Mohamed, Faez Amokrane Nait / Ma, Minghe / Schmidt, Aaron G / Lingwood, Daniel / Carroll, Michael C

    bioRxiv : the preprint server for biology

    2024  

    Abstract: In systemic lupus erythematosus, recent findings highlight the extrafollicular (EF) pathway as prominent origin of autoantibody-secreting cells (ASCs). ... ...

    Abstract In systemic lupus erythematosus, recent findings highlight the extrafollicular (EF) pathway as prominent origin of autoantibody-secreting cells (ASCs). CD21
    Language English
    Publishing date 2024-01-09
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.01.09.574739
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Heterologous Sarbecovirus Receptor Binding Domains as Scaffolds for SARS-CoV-2 Receptor Binding Motif Presentation.

    Hauser, Blake M / Sangesland, Maya / Lam, Evan C / St Denis, Kerri J / Sheehan, Maegan L / Vu, Mya L / Cheng, Agnes H / Sordilla, Sophia / Lamson, Dana Thornlow / Almawi, Ahmad W / Balazs, Alejandro B / Lingwood, Daniel / Schmidt, Aaron G

    ACS infectious diseases

    2024  Volume 10, Issue 2, Page(s) 553–561

    Abstract: Structure-guided rational immunogen design can generate optimized immunogens that elicit a desired humoral response. Design strategies often center on targeting conserved sites on viral glycoproteins that will ultimately confer potent neutralization. For ...

    Abstract Structure-guided rational immunogen design can generate optimized immunogens that elicit a desired humoral response. Design strategies often center on targeting conserved sites on viral glycoproteins that will ultimately confer potent neutralization. For SARS-CoV-2 (SARS-2), the surface-exposed spike glycoprotein includes a broadly conserved portion, the receptor binding motif (RBM), that is required to engage the host cellular receptor, ACE2. Expanding humoral responses to this site may result in a more potent neutralizing antibody response against diverse sarbecoviruses. Here, we used a "resurfacing" approach and iterative design cycles to graft the SARS-2 RBM onto heterologous sarbecovirus scaffolds. The scaffolds were selected to vary the antigenic distance relative to SARS-2 to potentially focus responses to RBM. Multimerized versions of these immunogens elicited broad neutralization against sarbecoviruses in the context of preexisting SARS-2 immunity. These validated engineering approaches can help inform future immunogen design efforts for sarbecoviruses and are generally applicable to other viruses.
    MeSH term(s) Humans ; SARS-CoV-2 ; Severe acute respiratory syndrome-related coronavirus ; COVID-19 ; Antibodies, Neutralizing
    Chemical Substances Antibodies, Neutralizing
    Language English
    Publishing date 2024-01-28
    Publishing country United States
    Document type Journal Article
    ISSN 2373-8227
    ISSN (online) 2373-8227
    DOI 10.1021/acsinfecdis.3c00483
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: A VRC13-like bNAb response is associated with complex escape pathways in HIV-1 envelope.

    Joshi, Vinita R / Claiborne, Daniel T / Pack, Melissa L / Power, Karen A / Newman, Ruchi M / Batorsky, Rebecca / Bean, David J / Goroff, Matthew S / Lingwood, Daniel / Seaman, Michael S / Rosenberg, Eric / Allen, Todd M

    Journal of virology

    2024  Volume 98, Issue 3, Page(s) e0172023

    Abstract: The rational design of HIV-1 immunogens to trigger the development of broadly neutralizing antibodies (bNAbs) requires understanding the viral evolutionary pathways influencing this process. An acute HIV-1-infected individual exhibiting >50% plasma ... ...

    Abstract The rational design of HIV-1 immunogens to trigger the development of broadly neutralizing antibodies (bNAbs) requires understanding the viral evolutionary pathways influencing this process. An acute HIV-1-infected individual exhibiting >50% plasma neutralization breadth developed neutralizing antibody specificities against the CD4-binding site (CD4bs) and V1V2 regions of Env gp120. Comparison of pseudoviruses derived from early and late autologous
    MeSH term(s) Humans ; Amino Acids ; Broadly Neutralizing Antibodies/immunology ; CD4 Antigens/genetics ; env Gene Products, Human Immunodeficiency Virus/genetics ; Epitopes ; HIV Antibodies ; HIV Antigens ; HIV Envelope Protein gp120/genetics ; HIV Infections ; HIV Seropositivity ; HIV-1/genetics ; AIDS Vaccines/immunology
    Chemical Substances Amino Acids ; Broadly Neutralizing Antibodies ; CD4 Antigens ; env Gene Products, Human Immunodeficiency Virus ; Epitopes ; HIV Antibodies ; HIV Antigens ; HIV Envelope Protein gp120 ; AIDS Vaccines
    Language English
    Publishing date 2024-02-27
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.01720-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Humoral responses to the SARS-CoV-2 spike and receptor binding domain in context of pre-existing immunity confer broad sarbecovirus neutralization.

    Hauser, Blake M / Sangesland, Maya / Lam, Evan C / Feldman, Jared / Balazs, Alejandro B / Lingwood, Daniel / Schmidt, Aaron G

    Frontiers in immunology

    2022  Volume 13, Page(s) 902260

    Abstract: Since the emergence of SARS-CoV-2 (SARS-2), multiple vaccine candidates were developed and studied both preclinically and clinically. Nearly all are based on the SARS-2 spike glycoprotein or its receptor binding domain (RBD). Studies of these vaccine ... ...

    Abstract Since the emergence of SARS-CoV-2 (SARS-2), multiple vaccine candidates were developed and studied both preclinically and clinically. Nearly all are based on the SARS-2 spike glycoprotein or its receptor binding domain (RBD). Studies of these vaccine candidates have largely been in a SARS-2 naïve context. However, pre-existing immunity to SARS-2 acquired through infection or vaccination continues to increase. Evaluating future vaccine candidates in context of this pre-existing immunity is necessary to understand how immune responses are subsequently influenced. Here, we evaluated the serum and IgG
    MeSH term(s) Antibodies, Viral ; COVID-19/prevention & control ; Epitopes ; Humans ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus
    Chemical Substances Antibodies, Viral ; Epitopes ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Language English
    Publishing date 2022-08-04
    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.2022.902260
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Enhancing antibody responses by multivalent antigen display on thymus-independent DNA origami scaffolds.

    Wamhoff, Eike-Christian / Ronsard, Larance / Feldman, Jared / Knappe, Grant A / Hauser, Blake M / Romanov, Anna / Case, James Brett / Sanapala, Shilpa / Lam, Evan C / Denis, Kerri J St / Boucau, Julie / Barczak, Amy K / Balazs, Alejandro B / Diamond, Michael S / Schmidt, Aaron G / Lingwood, Daniel / Bathe, Mark

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 795

    Abstract: Protein-based virus-like particles (P-VLPs) are commonly used to spatially organize antigens and enhance humoral immunity through multivalent antigen display. However, P-VLPs are thymus-dependent antigens that are themselves immunogenic and can induce B ... ...

    Abstract Protein-based virus-like particles (P-VLPs) are commonly used to spatially organize antigens and enhance humoral immunity through multivalent antigen display. However, P-VLPs are thymus-dependent antigens that are themselves immunogenic and can induce B cell responses that may neutralize the platform. Here, we investigate thymus-independent DNA origami as an alternative material for multivalent antigen display using the receptor binding domain (RBD) of the SARS-CoV-2 spike protein, the primary target of neutralizing antibody responses. Sequential immunization of mice with DNA-based VLPs (DNA-VLPs) elicits protective neutralizing antibodies to SARS-CoV-2 in a manner that depends on the valency of the antigen displayed and on T cell help. Importantly, the immune sera do not contain boosted, class-switched antibodies against the DNA scaffold, in contrast to P-VLPs that elicit strong B cell memory against both the target antigen and the scaffold. Thus, DNA-VLPs enhance target antigen immunogenicity without generating scaffold-directed immunity and thereby offer an important alternative material for particulate vaccine design.
    MeSH term(s) Humans ; Animals ; Mice ; Antibody Formation ; Antibodies, Blocking ; Vaccines, Virus-Like Particle/genetics ; Antibodies, Neutralizing ; DNA ; Antibodies, Viral ; Spike Glycoprotein, Coronavirus
    Chemical Substances spike protein, SARS-CoV-2 ; Antibodies, Blocking ; Vaccines, Virus-Like Particle ; Antibodies, Neutralizing ; DNA (9007-49-2) ; Antibodies, Viral ; Spike Glycoprotein, Coronavirus
    Language English
    Publishing date 2024-01-30
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-44869-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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