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      Protein nanoparticle vaccines induce potent neutralizing antibody responses against MERS-CoV

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          Abstract

          Middle East respiratory syndrome coronavirus (MERS-CoV) is a zoonotic betacoronavirus that causes severe and often lethal respiratory illness in humans. The MERS-CoV spike (S) protein is the viral fusogen and the target of neutralizing antibodies, and has therefore been the focus of vaccine design efforts. Currently there are no licensed vaccines against MERS-CoV and only a few candidates have advanced to Phase I clinical trials. Here we developed MERS-CoV vaccines utilizing a computationally designed protein nanoparticle platform that has generated safe and immunogenic vaccines against various enveloped viruses, including a licensed vaccine for SARS-CoV-2. Two-component protein nanoparticles displaying MERS-CoV S-derived antigens induced robust neutralizing antibody responses and protected mice against challenge with mouse-adapted MERS-CoV. Electron microscopy polyclonal epitope mapping and serum competition assays revealed the specificities of the dominant antibody responses elicited by immunogens displaying the prefusion-stabilized S-2P trimer, receptor binding domain (RBD), or N-terminal domain (NTD). An RBD nanoparticle vaccine elicited antibodies targeting multiple non-overlapping epitopes in the RBD, whereas anti-NTD antibodies elicited by the S-2P- and NTD-based immunogens converged on a single antigenic site. Our findings demonstrate the potential of two-component nanoparticle vaccine candidates for MERS-CoV and suggest that this platform technology could be broadly applicable to betacoronavirus vaccine development.

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          Most cited references125

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          A pneumonia outbreak associated with a new coronavirus of probable bat origin

          Since the outbreak of severe acute respiratory syndrome (SARS) 18 years ago, a large number of SARS-related coronaviruses (SARSr-CoVs) have been discovered in their natural reservoir host, bats 1–4 . Previous studies have shown that some bat SARSr-CoVs have the potential to infect humans 5–7 . Here we report the identification and characterization of a new coronavirus (2019-nCoV), which caused an epidemic of acute respiratory syndrome in humans in Wuhan, China. The epidemic, which started on 12 December 2019, had caused 2,794 laboratory-confirmed infections including 80 deaths by 26 January 2020. Full-length genome sequences were obtained from five patients at an early stage of the outbreak. The sequences are almost identical and share 79.6% sequence identity to SARS-CoV. Furthermore, we show that 2019-nCoV is 96% identical at the whole-genome level to a bat coronavirus. Pairwise protein sequence analysis of seven conserved non-structural proteins domains show that this virus belongs to the species of SARSr-CoV. In addition, 2019-nCoV virus isolated from the bronchoalveolar lavage fluid of a critically ill patient could be neutralized by sera from several patients. Notably, we confirmed that 2019-nCoV uses the same cell entry receptor—angiotensin converting enzyme II (ACE2)—as SARS-CoV.
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            UCSF Chimera--a visualization system for exploratory research and analysis.

            The design, implementation, and capabilities of an extensible visualization system, UCSF Chimera, are discussed. Chimera is segmented into a core that provides basic services and visualization, and extensions that provide most higher level functionality. This architecture ensures that the extension mechanism satisfies the demands of outside developers who wish to incorporate new features. Two unusual extensions are presented: Multiscale, which adds the ability to visualize large-scale molecular assemblies such as viral coats, and Collaboratory, which allows researchers to share a Chimera session interactively despite being at separate locales. Other extensions include Multalign Viewer, for showing multiple sequence alignments and associated structures; ViewDock, for screening docked ligand orientations; Movie, for replaying molecular dynamics trajectories; and Volume Viewer, for display and analysis of volumetric data. A discussion of the usage of Chimera in real-world situations is given, along with anticipated future directions. Chimera includes full user documentation, is free to academic and nonprofit users, and is available for Microsoft Windows, Linux, Apple Mac OS X, SGI IRIX, and HP Tru64 Unix from http://www.cgl.ucsf.edu/chimera/. Copyright 2004 Wiley Periodicals, Inc.
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              cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination

              A software tool, cryoSPARC, addresses the speed bottleneck in cryo-EM image processing, enabling automated macromolecular structure determination in hours on a desktop computer without requiring a starting model.
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                Author and article information

                Contributors
                Role: designed the studyRole: designed and characterized immunogensRole: performed in vitro experimentsRole: produced proteins and provided reagentsRole: analyzed the dataRole: wrote the manuscript with input from all authors
                Role: performed in vitro experimentsRole: analyzed the dataRole: wrote the manuscript with input from all authors
                Role: designed the studyRole: designed and characterized immunogensRole: produced proteins and provided reagents
                Role: performed challenge experiments
                Role: conducted and performed animal immunizations
                Role: produced proteins and provided reagents
                Role: produced proteins and provided reagents
                Role: produced proteins and provided reagents
                Role: produced proteins and provided reagents
                Role: produced proteins and provided reagents
                Role: produced proteins and provided reagents
                Role: produced proteins and provided reagents
                Role: provided and maintained cells
                Role: provided and maintained cells
                Role: provided and maintained cells
                Role: conducted and performed animal immunizations
                Role: conducted and performed animal immunizations
                Role: designed the studyRole: designed and characterized immunogens
                Role: provided oversight of immunization and challenge studies
                Role: conducted and performed animal immunizationsRole: wrote the manuscript with input from all authors
                Role: provided oversight of immunization and challenge studies
                Role: provided oversight of immunization and challenge studiesRole: wrote the manuscript with input from all authors
                Role: designed the studyRole: wrote the manuscript with input from all authors
                Role: designed the studyRole: wrote the manuscript with input from all authors
                Journal
                bioRxiv
                BIORXIV
                bioRxiv
                Cold Spring Harbor Laboratory
                14 March 2024
                : 2024.03.13.584735
                Affiliations
                [1 ]Institute for Protein Design, University of Washington, Seattle, WA 98195, USA
                [2 ]Department of Biochemistry, University of Washington, Seattle, WA 98195, USA
                [3 ]Graduate Program in Molecular and Cellular Biology, University of Washington, Seattle, WA 98195, USA
                [4 ]Department of Epidemiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27514, USA
                [5 ]Howard Hughes Medical Institute, Seattle, WA 98195, USA
                [6 ]Vaccine and Infectious Disease Division, Fred Hutchinson Cancer Research Center, Seattle WA 98109, USA
                [7 ]Department of Global Health, University of Washington, Seattle, WA 98195, USA
                [8 ]Department of Laboratory Medicine and Pathology, University of Washington, Seattle WA 98115, USA
                Author information
                http://orcid.org/0009-0004-4824-6445
                http://orcid.org/0009-0008-5844-1403
                Article
                10.1101/2024.03.13.584735
                10979991
                38558973
                dcf30fa3-cfec-4a03-9334-31c09f12f2ca

                This work is licensed under a Creative Commons Attribution 4.0 International License, which allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use.

                History
                Funding
                Funded by: National Institute of Allergy and Infectious Diseases, R.S.B., D.V., N.P.K., D.V., Investigators in the Pathogenesis of Infectious Disease Awards from the Burroughs Wellcome Fund, D.V., National Science Foundation Graduate Research Fellowships Program Award, C.W.C., University of Washington Arnold and Mabel Beckman cryoEM center and the National Institute of Health, D.V., Audacious Project at the Institute for Protein Design, N.P.K.
                Award ID: P01AI167966, 75N93022C00036, DGE-2140004, S10OD032290
                Funded by: D.V., Investigator of the Howard Hughes Medical Institute and the Hans Neurath Endowed Chair in Biochemistry t the University of Washington
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