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  1. Article ; Online: Cryo-EM cools down swine fever.

    Gallagher, John R / Harris, Audray K

    The Journal of biological chemistry

    2020  Volume 295, Issue 1, Page(s) 13–14

    Abstract: African swine fever virus (ASFV) is among the most complex DNA viruses known. Outbreaks have killed millions of swine around the world, and there is currently no vaccine. Three recent papers report the cryo-EM structure of the complete ASFV virion, ... ...

    Abstract African swine fever virus (ASFV) is among the most complex DNA viruses known. Outbreaks have killed millions of swine around the world, and there is currently no vaccine. Three recent papers report the cryo-EM structure of the complete ASFV virion, comprising a viral particle of multiple layers, and resolve the major outer-capsid protein p72 to higher resolution. Progress in these reports provides a further understanding of the structure-function relationships of large viruses and should aid in ASFV vaccine development.
    MeSH term(s) African Swine Fever ; African Swine Fever Virus ; Animals ; Classical Swine Fever ; Cryoelectron Microscopy ; Swine ; Virion
    Language English
    Publishing date 2020-01-03
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Comment
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.H119.012169
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Cryo-electron microscopy of influenza vaccine nanoparticles indicates full occupancy of displayed epitopes is facilitated by particle design.

    Gallagher, John R / Harris, Audray K

    Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada

    2016  Volume 22, Issue Suppl 3, Page(s) 1112–1113

    Language English
    Publishing date 2016-07-25
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1385710-1
    ISSN 1435-8115 ; 1431-9276
    ISSN (online) 1435-8115
    ISSN 1431-9276
    DOI 10.1017/S1431927616006401
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Immunoelectron Microscopy of Viral Antigens.

    Gulati, Neetu M / Torian, Udana / Gallagher, John R / Harris, Audray K

    Current protocols in microbiology

    2019  Volume 53, Issue 1, Page(s) e86

    Abstract: Immunoelectron microscopy is a powerful technique for identifying viral antigens and determining their structural localization and organization within vaccines and viruses. While traditional negative staining transmission electron microscopy provides ... ...

    Abstract Immunoelectron microscopy is a powerful technique for identifying viral antigens and determining their structural localization and organization within vaccines and viruses. While traditional negative staining transmission electron microscopy provides structural information, identity of components within a sample may be confounding. Immunoelectron microscopy allows for identification and visualization of antigens and their relative positions within a particulate sample. This allows for simple qualitative analysis of samples including whole virus, viral components, and viral-like particles. This article describes methods for immunogold labeling of viral antigens in a liquid suspension, with examples of immunogold-labeled influenza virus glycoproteins, and also discusses the important considerations for sample preparation and determination of morphologies. Together, these methods allow for understanding the antigenic makeup of viral particulate samples, which have important implications for molecular virology and vaccine development. © 2019 The Authors. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
    MeSH term(s) Animals ; Antigens, Viral/chemistry ; Antigens, Viral/immunology ; Antigens, Viral/ultrastructure ; Cell Line ; Microscopy, Immunoelectron/methods ; Staining and Labeling/methods ; Virus Cultivation/methods ; Viruses/chemistry ; Viruses/growth & development ; Viruses/immunology ; Viruses/ultrastructure
    Chemical Substances Antigens, Viral
    Language English
    Publishing date 2019-06-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2213675-7
    ISSN 1934-8533 ; 1934-8525
    ISSN (online) 1934-8533
    ISSN 1934-8525
    DOI 10.1002/cpmc.86
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Negative-Stain Transmission Electron Microscopy of Molecular Complexes for Image Analysis by 2D Class Averaging.

    Gallagher, John R / Kim, Alexander J / Gulati, Neetu M / Harris, Audray K

    Current protocols in microbiology

    2019  Volume 54, Issue 1, Page(s) e90

    Abstract: Negative-stain transmission electron microscopy (EM) is a technique that has provided nanometer resolution images of macromolecules for about 60 years. Developments in cryo-EM image processing have maximized the information gained from averaging large ... ...

    Abstract Negative-stain transmission electron microscopy (EM) is a technique that has provided nanometer resolution images of macromolecules for about 60 years. Developments in cryo-EM image processing have maximized the information gained from averaging large numbers of particles. These developments can now be applied back to negative-stain image analysis to ascertain domain level molecular structure (10 to 20 Å) more quickly and efficiently than possible by atomic resolution cryo-EM. Using uranyl acetate stained molecular complexes of influenza hemagglutinin bound to Fab 441D6, we describe a simple and efficient means to collect several hundred micrographs with SerialEM. Using RELION, we illustrate how tens of thousands of complexes can be auto-picked and classified to accurately describe the domain level topology of this unconventional hemagglutinin head-domain epitope. By comparing to the cryo-EM density map of the same complex, we show that questions about epitope mapping and conformational heterogeneity can readily be answered by this negative-stain method. © 2019 The Authors.
    MeSH term(s) Image Processing, Computer-Assisted/methods ; Macromolecular Substances/chemistry ; Macromolecular Substances/ultrastructure ; Microscopy, Electron, Transmission/methods ; Staining and Labeling/methods
    Chemical Substances Macromolecular Substances
    Language English
    Publishing date 2019-09-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2213675-7
    ISSN 1934-8533 ; 1934-8525
    ISSN (online) 1934-8533
    ISSN 1934-8525
    DOI 10.1002/cpmc.90
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Corrigendum: Impact of adjuvant: trivalent vaccine with quadrivalent-like protection against heterologous Yamagata-lineage influenza B virus.

    Myers, Mallory L / Gallagher, John R / Woolfork, De'Marcus D / Stradtmann-Carvalho, Regan K / Maldonado-Puga, Samantha / Bock, Kevin W / Boyoglu-Barnum, Seyhan / Syeda, Hubza / Creanga, Adrian / Alves, Derron A / Kanekiyo, Masaru / Harris, Audray K

    Frontiers in immunology

    2023  Volume 14, Page(s) 1283355

    Abstract: This corrects the article DOI: 10.3389/fimmu.2022.1002286.]. ...

    Abstract [This corrects the article DOI: 10.3389/fimmu.2022.1002286.].
    Language English
    Publishing date 2023-09-12
    Publishing country Switzerland
    Document type Published Erratum
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2023.1283355
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Commercial influenza vaccines vary in HA-complex structure and in induction of cross-reactive HA antibodies.

    Myers, Mallory L / Gallagher, John R / Kim, Alexander J / Payne, Walker H / Maldonado-Puga, Samantha / Assimakopoulos, Haralabos / Bock, Kevin W / Torian, Udana / Moore, Ian N / Harris, Audray K

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 1763

    Abstract: Influenza virus infects millions of people annually and can cause global pandemics. Hemagglutinin (HA) is the primary component of commercial influenza vaccines (CIV), and antibody titer to HA is a primary correlate of protection. Continual antigenic ... ...

    Abstract Influenza virus infects millions of people annually and can cause global pandemics. Hemagglutinin (HA) is the primary component of commercial influenza vaccines (CIV), and antibody titer to HA is a primary correlate of protection. Continual antigenic variation of HA requires that CIVs are reformulated yearly. Structural organization of HA complexes have not previously been correlated with induction of broadly reactive antibodies, yet CIV formulations vary in how HA is organized. Using electron microscopy to study four current CIVs, we find structures including: individual HAs, starfish structures with up to 12 HA molecules, and novel spiked-nanodisc structures that display over 50 HA molecules along the complex's perimeter. CIV containing these spiked nanodiscs elicit the highest levels of heterosubtypic cross-reactive antibodies in female mice. Here, we report that HA structural organization can be an important CIV parameter and can be associated with the induction of cross-reactive antibodies to conserved HA epitopes.
    MeSH term(s) Female ; Animals ; Mice ; Humans ; Influenza Vaccines ; Hemagglutinins ; Antibodies, Viral ; Hemagglutinin Glycoproteins, Influenza Virus ; Orthomyxoviridae Infections ; Cross Reactions ; Influenza, Human
    Chemical Substances Influenza Vaccines ; Hemagglutinins ; Antibodies, Viral ; Hemagglutinin Glycoproteins, Influenza Virus
    Language English
    Publishing date 2023-03-30
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-37162-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Phantoms models to characterize influenza hemagglutinin-based vaccines.

    McCraw, Dustin M / Harris, Audray K

    Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada

    2017  Volume 23, Issue Suppl 1, Page(s) 1322–1323

    Language English
    Publishing date 2017-08-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1385710-1
    ISSN 1435-8115 ; 1431-9276
    ISSN (online) 1435-8115
    ISSN 1431-9276
    DOI 10.1017/S1431927617007279
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Probing the Structural Organization of Virions and Genomic Ribonucleoprotein Complexes from Type B Influenza Virus by Cryo-electron Microscopy.

    Gulati, Neetu M / Gallagher, John R / McCraw, Dustin M / Harris, Audray K

    Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada

    2019  Volume 25, Issue Suppl 2, Page(s) 1302–1303

    MeSH term(s) Cryoelectron Microscopy ; Image Processing, Computer-Assisted ; Influenza B virus/ultrastructure ; Macromolecular Substances/ultrastructure ; Ribonucleoproteins/ultrastructure ; Virion/ultrastructure
    Chemical Substances Macromolecular Substances ; Ribonucleoproteins
    Language English
    Publishing date 2019-08-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1385710-1
    ISSN 1435-8115 ; 1431-9276
    ISSN (online) 1435-8115
    ISSN 1431-9276
    DOI 10.1017/S1431927619007244
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Designed nanoparticles elicit cross-reactive antibody responses to conserved influenza virus hemagglutinin stem epitopes.

    McCraw, Dustin M / Myers, Mallory L / Gulati, Neetu M / Prabhakaran, Madhu / Brand, Joshua / Andrews, Sarah / Gallagher, John R / Maldonado-Puga, Samantha / Kim, Alexander J / Torian, Udana / Syeda, Hubza / Boyoglu-Barnum, Seyhan / Kanekiyo, Masaru / McDermott, Adrian B / Harris, Audray K

    PLoS pathogens

    2023  Volume 19, Issue 8, Page(s) e1011514

    Abstract: Despite the availability of seasonal vaccines and antiviral medications, influenza virus continues to be a major health concern and pandemic threat due to the continually changing antigenic regions of the major surface glycoprotein, hemagglutinin (HA). ... ...

    Abstract Despite the availability of seasonal vaccines and antiviral medications, influenza virus continues to be a major health concern and pandemic threat due to the continually changing antigenic regions of the major surface glycoprotein, hemagglutinin (HA). One emerging strategy for the development of more efficacious seasonal and universal influenza vaccines is structure-guided design of nanoparticles that display conserved regions of HA, such as the stem. Using the H1 HA subtype to establish proof of concept, we found that tandem copies of an alpha-helical fragment from the conserved stem region (helix-A) can be displayed on the protruding spikes structures of a capsid scaffold. The stem region of HA on these designed chimeric nanoparticles is immunogenic and the nanoparticles are biochemically robust in that heat exposure did not destroy the particles and immunogenicity was retained. Furthermore, mice vaccinated with H1-nanoparticles were protected from lethal challenge with H1N1 influenza virus. By using a nanoparticle library approach with this helix-A nanoparticle design, we show that this vaccine nanoparticle construct design could be applicable to different influenza HA subtypes. Importantly, antibodies elicited by H1, H5, and H7 nanoparticles demonstrated homosubtypic and heterosubtypic cross-reactivity binding to different HA subtypes. Also, helix-A nanoparticle immunizations were used to isolate mouse monoclonal antibodies that demonstrated heterosubtypic cross-reactivity and provided protection to mice from viral challenge via passive-transfer. This tandem helix-A nanoparticle construct represents a novel design to display several hundred copies of non-trimeric conserved HA stem epitopes on vaccine nanoparticles. This design concept provides a new approach to universal influenza vaccine development strategies and opens opportunities for the development of nanoparticles with broad coverage over many antigenically diverse influenza HA subtypes.
    MeSH term(s) Animals ; Mice ; Humans ; Hemagglutinins ; Epitopes ; Influenza, Human ; Antibody Formation ; Influenza A Virus, H1N1 Subtype ; Influenza Vaccines ; Nanoparticles
    Chemical Substances Hemagglutinins ; Epitopes ; Influenza Vaccines
    Language English
    Publishing date 2023-08-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1011514
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Impact of adjuvant: Trivalent vaccine with quadrivalent-like protection against heterologous Yamagata-lineage influenza B virus.

    Myers, Mallory L / Gallagher, John R / Woolfork, De'Marcus D / Stradtmann-Carvalho, Regan K / Maldonado-Puga, Samantha / Bock, Kevin W / Boyoglu-Barnum, Seyhan / Syeda, Hubza / Creanga, Adrian / Alves, Derron A / Kanekiyo, Masaru / Harris, Audray K

    Frontiers in immunology

    2022  Volume 13, Page(s) 1002286

    Abstract: As new vaccine technologies and platforms, such as nanoparticles and novel adjuvants, are developed to aid in the establishment of a universal influenza vaccine, studying traditional influenza split/subunit vaccines should not be overlooked. Commercially ...

    Abstract As new vaccine technologies and platforms, such as nanoparticles and novel adjuvants, are developed to aid in the establishment of a universal influenza vaccine, studying traditional influenza split/subunit vaccines should not be overlooked. Commercially available vaccines are typically studied in terms of influenza A H1 and H3 viruses but influenza B viruses need to be examined as well. Thus, there is a need to both understand the limitations of split/subunit vaccines and develop strategies to overcome those limitations, particularly their ability to elicit cross-reactive antibodies to the co-circulating Victoria (B-V) and Yamagata (B-Y) lineages of human influenza B viruses. In this study, we compared three commercial influenza hemagglutinin (HA) split/subunit vaccines, one quadrivalent (H1, H3, B-V, B-Y HAs) and two trivalent (H1, H3, B-V HAs), to characterize potential differences in their antibody responses and protection against a B-Y challenge. We found that the trivalent adjuvanted vaccine Fluad, formulated without B-Y HA, was able to produce antibodies to B-Y (cross-lineage) on a similar level to those elicited from a quadrivalent vaccine (Flucelvax) containing both B-V and B-Y HAs. Interestingly, Fluad protected mice from a lethal cross-lineage B-Y viral challenge, while another trivalent vaccine, Fluzone HD, failed to elicit antibodies or full protection following challenge. Fluad immunization also diminished viral burden in the lungs compared to Fluzone and saline groups. The success of a trivalent vaccine to provide protection from a cross-lineage influenza B challenge, similar to a quadrivalent vaccine, suggests that further analysis of different split/subunit vaccine formulations could identify mechanisms for vaccines to target antigenically different viruses. Understanding how to increase the breadth of the immune response following immunization will be needed for universal influenza vaccine development.
    MeSH term(s) Adjuvants, Immunologic ; Animals ; Antibodies, Viral ; Hemagglutinins ; Humans ; Influenza B virus ; Influenza Vaccines ; Influenza, Human/prevention & control ; Mice ; Vaccines, Combined ; Vaccines, Subunit
    Chemical Substances Adjuvants, Immunologic ; Antibodies, Viral ; Hemagglutinins ; Influenza Vaccines ; Vaccines, Combined ; Vaccines, Subunit
    Language English
    Publishing date 2022-09-30
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2022.1002286
    Database MEDical Literature Analysis and Retrieval System OnLINE

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