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      Is Open Access

      Integrative illustration for coronavirus outreach

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          Abstract

          Two illustrations integrate current knowledge about severe acute respiratory syndrome (SARS) coronaviruses and their life cycle. They have been widely used in education and outreach through free distribution as part of a coronavirus-related resource at Protein Data Bank (PDB)-101, the education portal of the RCSB PDB. Scientific sources for creation of the illustrations and examples of dissemination and response are presented.

          Abstract

          This Community Page article describes how visually striking illustrations of SARS coronaviruses can capture the state of knowledge of the field and provide a touchstone for outreach and education about these pathogens.

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          Most cited references10

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          Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy.

          Coronavirus particles are enveloped and pleomorphic and are thus refractory to crystallization and symmetry-assisted reconstruction. A novel methodology of single-particle image analysis was applied to selected virus features to obtain a detailed model of the oligomeric state and spatial relationships among viral structural proteins. Two-dimensional images of the S, M, and N structural proteins of severe acute respiratory syndrome coronavirus and two other coronaviruses were refined to a resolution of approximately 4 nm. Proteins near the viral membrane were arranged in overlapping lattices surrounding a disordered core. Trimeric glycoprotein spikes were in register with four underlying ribonucleoprotein densities. However, the spikes were dispensable for ribonucleoprotein lattice formation. The ribonucleoprotein particles displayed coiled shapes when released from the viral membrane. Our results contribute to the understanding of the assembly pathway used by coronaviruses and other pleomorphic viruses and provide the first detailed view of coronavirus ultrastructure.
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            Atlas of coronavirus replicase structure

            Highlights • Complete and up to date coverage of replicase protein structures for SARS-CoV. • Discusses SARS-CoV structure in the context of other coronavirus structures. • Summarizes data from a variety of structural methods to illuminate protein function. • Uses models and predictions to fill gaps in the SARS-CoV structure. • Discusses the high percentage of novel protein folds among SARS-CoV proteins.
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              Coronavirus

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                Author and article information

                Journal
                PLoS Biol
                PLoS Biol
                plos
                plosbiol
                PLoS Biology
                Public Library of Science (San Francisco, CA USA )
                1544-9173
                1545-7885
                6 August 2020
                August 2020
                6 August 2020
                : 18
                : 8
                : e3000815
                Affiliations
                [1 ] RCSB Protein Data Bank, Rutgers, The State University of New Jersey, Piscataway, New Jersey, United States of America
                [2 ] Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America
                [3 ] Institute for Quantitative Biomedicine, Rutgers, The State University of New Jersey, Piscataway, New Jersey, United States of America
                [4 ] Research Collaboratory for Structural Bioinformatics Protein Data Bank, San Diego Supercomputer Center, University of California, San Diego, California, United States of America
                [5 ] Rutgers Cancer Institute of New Jersey, Rutgers, The State University of New Jersey, New Brunswick, New Jersey, United States of America
                Author notes

                The authors have declared that no competing interests exist.

                Author information
                http://orcid.org/0000-0002-5932-2130
                http://orcid.org/0000-0003-3103-7781
                http://orcid.org/0000-0002-4149-1745
                http://orcid.org/0000-0002-2487-9713
                Article
                PBIOLOGY-D-20-01284
                10.1371/journal.pbio.3000815
                7433897
                32760062
                6cba10f7-7f68-44de-a6e0-bc4cba9cf236
                © 2020 Goodsell et al

                This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

                History
                Page count
                Figures: 4, Tables: 0, Pages: 7
                Funding
                This work is supported by (DSG) grant GM120604 from the National Institutes of Health ( www.nih.gov) and (DSG, MV, CZ, SKB) the RCSB Protein Data Bank (National Science Foundation (DBI-1832184, www.nsf.gov), the US Department of Energy (DE-SC0019749, www.energy.gov), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health grant R01GM133198). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
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                2020-08-18
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