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are a diverse group of non-enveloped, positive-sense RNA viruses with a wide range of hosts and transmission routes. Norovirus is the most well-known member of the Caliciviridae; the acute gastroenteritis caused by human norovirus (HuNoV), for example, frequently results in closures of hospital wards and schools during the winter months. One area of calicivirus biology that has gained increasing attention over the past decade is the conformational flexibility exhibited by the protruding (P) domains of the major capsid protein VP1. This was observed in structure analyses of capsids encoded by many species and is often a consequence of environmental cues such as metal ions, changes to pH, or receptor\/co-factor engagement. This review summarises the current understanding of P-domain flexibility, discussing the role this region plays in caliciviral infection and immune evasion, and highlighting potential avenues for further investigation.<\/jats:p>","DOI":"10.3390\/v16121835","type":"journal-article","created":{"date-parts":[[2024,11,27]],"date-time":"2024-11-27T04:20:12Z","timestamp":1732681212000},"page":"1835","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Conformational Flexibility in Capsids Encoded by the Caliciviridae"],"prefix":"10.3390","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0918-9201","authenticated-orcid":false,"given":"Charlotte B.","family":"Lewis","sequence":"first","affiliation":[{"name":"MRC\u2014University of Glasgow Centre for Virus Research, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4367-772X","authenticated-orcid":false,"given":"Lee","family":"Sherry","sequence":"additional","affiliation":[{"name":"MRC\u2014University of Glasgow Centre for Virus Research, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michaela J.","family":"Conley","sequence":"additional","affiliation":[{"name":"MRC\u2014University of Glasgow Centre for Virus Research, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masaaki","family":"Nakashima","sequence":"additional","affiliation":[{"name":"MRC\u2014University of Glasgow Centre for Virus Research, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shirin","family":"Akbar","sequence":"additional","affiliation":[{"name":"MRC\u2014University of Glasgow Centre for Virus Research, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nithya","family":"Govindan","sequence":"additional","affiliation":[{"name":"MRC\u2014University of Glasgow Centre for Virus Research, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4313-5023","authenticated-orcid":false,"given":"Margaret J.","family":"Hosie","sequence":"additional","affiliation":[{"name":"MRC\u2014University of Glasgow Centre for Virus Research, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Bhella","sequence":"additional","affiliation":[{"name":"MRC\u2014University of Glasgow Centre for Virus Research, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,11,26]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1099\/jgv.0.001332","article-title":"ICTV Virus Taxonomy Profile: Caliciviridae","volume":"100","author":"Estes","year":"2019","journal-title":"J. Gen. Virol."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Desselberger, U. (2019). Caliciviridae Other Than Noroviruses. Viruses, 11.","DOI":"10.3390\/v11030286"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"S309","DOI":"10.1086\/315575","article-title":"Organization and Expression of Calicivirus Genes","volume":"181","author":"Clarke","year":"2000","journal-title":"J. Infect. Dis."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.virusres.2015.02.002","article-title":"Functions of the 5\u2032 and 3\u2032 Ends of Calicivirus Genomes","volume":"206","author":"Alhatlani","year":"2015","journal-title":"Virus Res."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"6487","DOI":"10.1128\/jvi.68.10.6487-6495.1994","article-title":"Identification and Characterization of a 3C-like Protease from Rabbit Hemorrhagic Disease Virus, a Calicivirus","volume":"68","author":"Boniotti","year":"1994","journal-title":"J. Virol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/0168-1702(93)90034-K","article-title":"The Amino Terminal Sequence of VP60 from Rabbit Hemorrhagic Disease Virus Supports Its Putative Subgenomic Origin","volume":"27","author":"Parra","year":"1993","journal-title":"Virus Res."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"e00280-20","DOI":"10.1128\/JVI.00280-20","article-title":"Major Capsid Protein Synthesis from the Genomic RNA of Feline Calicivirus","volume":"94","author":"Urban","year":"2020","journal-title":"J. Virol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"34051","DOI":"10.1074\/jbc.M304874200","article-title":"Translation of the Minor Capsid Protein of a Calicivirus Is Initiated by a Novel Termination-Dependent Reinitiation Mechanism","volume":"278","author":"Meyers","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"4012","DOI":"10.1128\/JVI.79.7.4012-4024.2005","article-title":"Feline Calicivirus VP2 Is Essential for the Production of Infectious Virions","volume":"79","author":"Sosnovtsev","year":"2005","journal-title":"J. Virol."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Hofmann-Lehmann, R., Hosie, M.J., Hartmann, K., Egberink, H., Truyen, U., Tasker, S., Bel\u00e1k, S., Boucraut-Baralon, C., Frymus, T., and Lloret, A. (2022). Calicivirus Infection in Cats. Viruses, 14.","DOI":"10.3390\/v14050937"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Domanico, M., Cavadini, P., Nardini, R., Cecca, D., Mastrandrea, G., Eleni, C., Galietta, V., Attili, L., Pizzarelli, A., and Onorati, R. (2023). Pathological and Virological Insights from an Outbreak of European Brown Hare Syndrome in the Italian Hare (Lepus Corsicanus). Front. Microbiol., 14.","DOI":"10.3389\/fmicb.2023.1250787"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1186\/1297-9716-43-12","article-title":"Rabbit Haemorrhagic Disease (RHD) and Rabbit Haemorrhagic Disease Virus (RHDV): A Review","volume":"43","author":"Abrantes","year":"2012","journal-title":"Vet. Res."},{"key":"ref_13","unstructured":"Peter, R.D. (2021). Vesicular Exanthema of Swine, Merck & Co., Inc.. MSD Veterinary Manual."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1016\/j.vaccine.2017.01.009","article-title":"Re-Assessing the Total Burden of Norovirus Circulating in the United Kingdom Population","volume":"35","author":"Harris","year":"2017","journal-title":"Vaccine"},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Bartsch, S.M., Lopman, B.A., Ozawa, S., Hall, A.J., and Lee, B.Y. (2016). Global Economic Burden of Norovirus Gastroenteritis. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0151219"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Sattar, S.A., Ali, M., and Tetro, J.A. (2011). In Vivo Comparison of Two Human Norovirus Surrogates for Testing Ethanol-Based Handrubs: The Mouse Chasing the Cat!. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0017340"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"5743","DOI":"10.1128\/AEM.01532-14","article-title":"Comprehensive Comparison of Cultivable Norovirus Surrogates in Response to Different Inactivation and Disinfection Treatments","volume":"80","author":"Cromeans","year":"2014","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"868","DOI":"10.1111\/jam.12878","article-title":"Physicochemical Stability Profile of Tulane Virus: A Human Norovirus Surrogate","volume":"119","author":"Arthur","year":"2015","journal-title":"J. Appl. Microbiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1086\/499315","article-title":"Molecular and Epidemiologic Trends of Caliciviruses Associated with Outbreaks of Acute Gastroenteritis in the United States, 2000\u20132004","volume":"193","author":"Blanton","year":"2006","journal-title":"J. Infect. Dis."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"144","DOI":"10.3201\/eid1301.060800","article-title":"Gastroenteritis Caused by Norovirus GGII.4, The Netherlands, 1994\u20132005","volume":"13","author":"Siebenga","year":"2007","journal-title":"Emerg. Infect. Dis."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.3201\/eid1908.130465","article-title":"Norovirus Disease in the United States","volume":"19","author":"Hall","year":"2013","journal-title":"Emerg. Infect. Dis."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1038\/s41586-018-0852-1","article-title":"Calicivirus VP2 Forms a Portal-like Assembly Following Receptor Engagement","volume":"565","author":"Conley","year":"2019","journal-title":"Nature"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"e0035024","DOI":"10.1128\/jvi.00350-24","article-title":"VP2 Mediates the Release of the Feline Calicivirus RNA Genome by Puncturing the Endosome Membrane of Infected Cells","volume":"98","author":"Sun","year":"2024","journal-title":"J. Virol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.jsb.2012.09.006","article-title":"RELION: Implementation of a Bayesian Approach to Cryo-EM Structure Determination","volume":"180","author":"Scheres","year":"2012","journal-title":"J. Struct. Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1107\/S205225251801463X","article-title":"A Bayesian Approach to Beam-Induced Motion Correction in Cryo-EM Single-Particle Analysis","volume":"6","author":"Zivanov","year":"2019","journal-title":"IUCrJ"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"e00282-21","DOI":"10.1128\/JVI.00282-21","article-title":"The Cryo-EM Structure of Vesivirus 2117 Highlights Functional Variations in Entry Pathways for Viruses in Different Clades of the Vesivirus Genus","volume":"95","author":"Sutherland","year":"2021","journal-title":"J. Virol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1038\/s41586-024-07215-4","article-title":"Automated Model Building and Protein Identification in Cryo-EM Maps","volume":"628","author":"Jamali","year":"2024","journal-title":"Nature"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and Development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1107\/S2059798319011471","article-title":"Macromolecular Structure Determination Using X-rays, Neutrons and Electrons: Recent Developments in Phenix","volume":"75","author":"Liebschner","year":"2019","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1107\/S2059798318002425","article-title":"ISOLDE: A Physically Realistic Environment for Model Building into Low-Resolution Electron-Density Maps","volume":"74","author":"Croll","year":"2018","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"McElwee, M., Vijayakrishnan, S., Rixon, F., and Bhella, D. (2018). Structure of the Herpes Simplex Virus Portal-Vertex. PLoS Biol., 16.","DOI":"10.1101\/290544"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Sanchez-Garcia, R., Gomez-Blanco, J., Cuervo, A., Carazo, J.M., Sorzano, C.O.S., and Vargas, J. (2021). DeepEMhancer: A Deep Learning Solution for Cryo-EM Volume Post-Processing. Commun. Biol., 4.","DOI":"10.1038\/s42003-021-02399-1"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera--a Visualization System for Exploratory Research and Analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1002\/pro.3943","article-title":"UCSF ChimeraX: Structure Visualization for Researchers, Educators, and Developers","volume":"30","author":"Pettersen","year":"2021","journal-title":"Protein Sci."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"6527","DOI":"10.1128\/jvi.66.11.6527-6532.1992","article-title":"Expression, Self-Assembly, and Antigenicity of the Norwalk Virus Capsid Protein","volume":"66","author":"Jiang","year":"1992","journal-title":"J. Virol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1126\/science.286.5438.287","article-title":"X-ray Crystallographic Structure of the Norwalk Virus Capsid","volume":"286","author":"Prasad","year":"1999","journal-title":"Science"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"8048","DOI":"10.1073\/pnas.0600421103","article-title":"X-ray Structure of a Native Calicivirus: Structural Insights into Antigenic Diversity and Host Specificity","volume":"103","author":"Chen","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1146\/annurev.bi.58.070189.002533","article-title":"Icosahedral RNA Virus Structure","volume":"58","author":"Rossmann","year":"1989","journal-title":"Annu. Rev. Biochem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"8051","DOI":"10.1128\/JVI.00550-08","article-title":"Structural Insights into Calicivirus Attachment and Uncoating","volume":"82","author":"Bhella","year":"2008","journal-title":"J. Virol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"14017","DOI":"10.1128\/JVI.79.22.14017-14030.2005","article-title":"The p Domain of Norovirus Capsid Protein Forms a Subviral Particle That Binds to Histo-Blood Group Antigen Receptors","volume":"79","author":"Tan","year":"2005","journal-title":"J. Virol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2799","DOI":"10.1099\/vir.0.81134-0","article-title":"Epitopes in the P2 Domain of Norovirus VP1 Recognized by Monoclonal Antibodies That Block Cell Interactions","volume":"86","author":"Lochridge","year":"2005","journal-title":"J. Gen. Virol."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Allen, D.J., Gray, J.J., Gallimore, C.I., Xerry, J., and Iturriza-G\u00f3mara, M. (2008). Analysis of Amino Acid Variation in the P2 Domain of the GII-4 Norovirus VP1 Protein Reveals Putative Variant-Specific Epitopes. PLoS ONE, 3.","DOI":"10.1371\/journal.pone.0001485"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Lindesmith, L.C., Donaldson, E.F., LoBue, A.D., Cannon, J.L., Zheng, D.-P., Vinje, J., and Baric, R.S. (2008). Mechanisms of GII.4 Norovirus Persistence in Human Populations. PLoS Med., 5.","DOI":"10.1371\/journal.pmed.0050031"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"2803","DOI":"10.1128\/JVI.03106-12","article-title":"Emergence of a Norovirus GII.4 Strain Correlates with Changes in Evolving Blockade Epitopes","volume":"87","author":"Lindesmith","year":"2013","journal-title":"J. Virol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"e01716-22","DOI":"10.1128\/jvi.01716-22","article-title":"Minimal Antigenic Evolution after a Decade of Norovirus GII.4 Sydney_2012 Circulation in Humans","volume":"97","author":"Parra","year":"2023","journal-title":"J. Virol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1877","DOI":"10.1093\/infdis\/jit370","article-title":"Emergence of New Pandemic GII.4 Sydney Norovirus Strain Correlates with Escape from Herd Immunity","volume":"208","author":"Debbink","year":"2013","journal-title":"J. Infect. Dis."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1186\/1743-422X-6-150","article-title":"Characterisation of a GII-4 Norovirus Variant-Specific Surface-Exposed Site Involved in Antibody Binding","volume":"6","author":"Allen","year":"2009","journal-title":"Virol. J."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"110689","DOI":"10.1016\/j.celrep.2022.110689","article-title":"Dynamic Immunodominance Hierarchy of Neutralizing Antibody Responses to Evolving GII.4 Noroviruses","volume":"39","author":"Tohma","year":"2022","journal-title":"Cell Rep."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"e00518-17","DOI":"10.1128\/mSphere.00518-17","article-title":"Conformational Occlusion of Blockade Antibody Epitopes, a Novel Mechanism of GII.4 Human Norovirus Immune Evasion","volume":"3","author":"Lindesmith","year":"2018","journal-title":"mSphere"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Lindesmith, L.C., Beltramello, M., Donaldson, E.F., Corti, D., Swanstrom, J., Debbink, K., Lanzavecchia, A., and Baric, R.S. (2012). Immunogenetic Mechanisms Driving Norovirus GII.4 Antigenic Variation. PLoS Pathog., 8.","DOI":"10.1371\/journal.ppat.1002705"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"e02202-19","DOI":"10.1128\/mBio.02202-19","article-title":"Population Genomics of GII.4 Noroviruses Reveal Complex Diversification and New Antigenic Sites Involved in the Emergence of Pandemic Strains","volume":"10","author":"Tohma","year":"2019","journal-title":"mBio"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"7414","DOI":"10.1128\/JVI.06729-11","article-title":"Multiple Antigenic Sites Are Involved in Blocking the Interaction of GII.4 Norovirus Capsid with ABH Histo-Blood Group Antigens","volume":"86","author":"Parra","year":"2012","journal-title":"J. Virol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1128\/JVI.06189-11","article-title":"Genetic Mapping of a Highly Variable Norovirus GII.4 Blockade Epitope: Potential Role in Escape from Human Herd Immunity","volume":"86","author":"Debbink","year":"2012","journal-title":"J. Virol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/s13099-023-00594-5","article-title":"Comprehensive Full Genome Analysis of Norovirus Strains from Eastern India, 2017\u20132021","volume":"16","author":"Lo","year":"2024","journal-title":"Gut Pathog."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"D94","DOI":"10.1093\/nar\/gky989","article-title":"GenBank","volume":"47","author":"Sayers","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1007\/978-1-0716-1036-7_13","article-title":"Alignment of Biological Sequences with Jalview","volume":"2231","author":"Procter","year":"2021","journal-title":"Methods Mol. Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"4044","DOI":"10.1128\/JVI.76.8.4044-4055.2002","article-title":"Structural Requirements for the Assembly of Norwalk Virus-like Particles","volume":"76","author":"White","year":"2002","journal-title":"J. Virol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"6469","DOI":"10.1128\/JVI.78.12.6469-6479.2004","article-title":"Inter- and Intragenus Structural Variations in Caliciviruses and Their Functional Implications","volume":"78","author":"Chen","year":"2004","journal-title":"J. Virol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2664","DOI":"10.1128\/JVI.02916-15","article-title":"Antigenic and Cryo-Electron Microscopy Structure Analysis of a Chimeric Sapovirus Capsid","volume":"90","author":"Miyazaki","year":"2016","journal-title":"J. Virol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"2079","DOI":"10.1128\/JVI.02200-07","article-title":"Structure of Antibody-Neutralized Murine Norovirus and Unexpected Differences from Viruslike Particles","volume":"82","author":"Katpally","year":"2008","journal-title":"J. Virol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1083\/jcb.122.5.1023","article-title":"Early Steps in Reovirus Infection Are Associated with Dramatic Changes in Supramolecular Structure and Protein Conformation: Analysis of Virions and Subviral Particles by Cryoelectron Microscopy and Image Reconstruction","volume":"122","author":"Dryden","year":"1993","journal-title":"J. Cell Biol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"3635","DOI":"10.1128\/JVI.06868-11","article-title":"Structural Basis for Broad Detection of Genogroup II Noroviruses by a Monoclonal Antibody That Binds to a Site Occluded in the Viral Particle","volume":"86","author":"Hansman","year":"2012","journal-title":"J. Virol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"5550","DOI":"10.1128\/JVI.02371-09","article-title":"Conformational Changes in the Capsid of a Calicivirus upon Interaction with Its Functional Receptor","volume":"84","author":"Ossiboff","year":"2010","journal-title":"J. Virol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"5836","DOI":"10.1128\/JVI.00314-10","article-title":"High-Resolution Cryo-Electron Microscopy Structures of Murine Norovirus 1 and Rabbit Hemorrhagic Disease Virus Reveal Marked Flexibility in the Receptor Binding Domains","volume":"84","author":"Katpally","year":"2010","journal-title":"J. Virol."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Song, C., Takai-Todaka, R., Miki, M., Haga, K., Fujimoto, A., Ishiyama, R., Oikawa, K., Yokoyama, M., Miyazaki, N., and Iwasaki, K. (2020). Dynamic Rotation of the Protruding Domain Enhances the Infectivity of Norovirus. PLoS Pathog., 16.","DOI":"10.1371\/journal.ppat.1008619"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"e01735-23","DOI":"10.1128\/jvi.01735-23","article-title":"The Reversible Activation of Norovirus by Metal Ions","volume":"98","author":"Sherman","year":"2024","journal-title":"J. Virol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"e0147121","DOI":"10.1128\/JVI.01471-21","article-title":"Multiple Signals in the Gut Contract the Mouse Norovirus Capsid To Block Antibody Binding While Enhancing Receptor Affinity","volume":"95","author":"Williams","year":"2021","journal-title":"J. Virol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"e0017621","DOI":"10.1128\/JVI.00176-21","article-title":"A Norovirus Uses Bile Salts To Escape Antibody Recognition While Enhancing Receptor Binding","volume":"95","author":"Williams","year":"2021","journal-title":"J. Virol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1038\/s41467-022-28757-z","article-title":"Atomic Structure of the Predominant GII.4 Human Norovirus Capsid Reveals Novel Stability and Plasticity","volume":"13","author":"Hu","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"992","DOI":"10.1016\/j.tibs.2020.08.003","article-title":"Divalent Cations: A Molecular Glue for Protein Materials","volume":"45","author":"Unzueta","year":"2020","journal-title":"Trends Biochem. Sci."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Sun, C., Huang, P., Xu, X., Vago, F.S., Li, K., Klose, T., Jiang, X.J., and Jiang, W. (2024). The 2.6 \u00c5 Structure of a Tulane Virus Variant with Minor Mutations Leading to Receptor Change. Biomolecules, 14.","DOI":"10.3390\/biom14010119"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1107\/S090744490706595X","article-title":"Metals in Proteins: Correlation between the Metal-Ion Type, Coordination Number and the Amino-Acid Residues Involved in the Coordination","volume":"64","year":"2008","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"e1525","DOI":"10.1093\/cid\/ciaa1001","article-title":"Characteristics of GII.4 Norovirus Versus Other Genotypes in Sporadic Pediatric Infections in Davidson County, Tennessee, USA","volume":"73","author":"Haddadin","year":"2020","journal-title":"Clin. Infect. Dis."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1093\/cid\/cir478","article-title":"Impact of an Emergent Norovirus Variant in 2009 on Norovirus Outbreak Activity in the United States","volume":"53","author":"Yen","year":"2011","journal-title":"Clin. Infect. Dis."},{"key":"ref_75","first-page":"8","article-title":"Indications for Worldwide Increased Norovirus Activity Associated with Emergence of a New Variant of Genotype II.4, Late 2012","volume":"18","author":"Botteldoorn","year":"2013","journal-title":"Eurosurveillance"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"e00035-18","DOI":"10.1128\/JVI.00035-18","article-title":"Conserved Surface Residues on the Feline Calicivirus Capsid Are Essential for Interaction with Its Receptor Feline Junctional Adhesion Molecule A (fJAM-A)","volume":"92","author":"Lu","year":"2018","journal-title":"J. Virol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"2579","DOI":"10.1111\/tbed.13605","article-title":"Identification of Feline Calicivirus in Cats with Enteritis","volume":"67","author":"Lanave","year":"2020","journal-title":"Transbound. Emerg. Dis."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Williams, A., Smith, H.Q., Sherman, M., and Smith, T.J. (2020). Bile Salts Alter the Mouse Norovirus Capsid Conformation\u2014Possible Implications for Cell Attachment and Immune Evasion. Biophys. J., 118.","DOI":"10.1016\/j.bpj.2019.11.1674"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"E9201","DOI":"10.1073\/pnas.1805797115","article-title":"Structural Basis for Murine Norovirus Engagement of Bile Acids and the CD300lf Receptor","volume":"115","author":"Nelson","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Sherman, M.B., Williams, A.N., Smith, H.Q., Pettitt, B.M., Wobus, C.E., and Smith, T.J. (2021). Structural Studies on the Shapeshifting Murine Norovirus. Viruses, 13.","DOI":"10.3390\/v13112162"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1079\/PNS19990020","article-title":"The Regulation of Mineral Absorption in the Gastrointestinal Tract","volume":"58","author":"Powell","year":"1999","journal-title":"Proc. Nutr. Soc."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"e00334-17","DOI":"10.1128\/mSphere.00334-17","article-title":"Norovirus Escape from Broadly Neutralizing Antibodies Is Limited to Allostery-Like Mechanisms","volume":"2","author":"Kolawole","year":"2017","journal-title":"mSphere"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"5408","DOI":"10.1128\/JVI.00070-08","article-title":"Characterization of a Rhesus Monkey Calicivirus Representing a New Genus of Caliciviridae","volume":"82","author":"Farkas","year":"2008","journal-title":"J. Virol."},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Helm, E.W., Peiper, A.M., Phillips, M., Williams, C.G., Sherman, M.B., Kelley, T., Smith, H.Q., Jacobs, S.O., Shah, D., and Tatum, S.M. (2022). Environmentally-Triggered Contraction of the Norovirus Virion Determines Diarrheagenic Potential. Front. Immunol., 13.","DOI":"10.3389\/fimmu.2022.1043746"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"2950","DOI":"10.1128\/JVI.07038-11","article-title":"Protruding Domain of Capsid Protein Is Necessary and Sufficient To Determine Murine Norovirus Replication and Pathogenesis In Vivo","volume":"86","author":"Strong","year":"2012","journal-title":"J. Virol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"7725","DOI":"10.1128\/JVI.00237-08","article-title":"A Single Amino Acid Substitution in the Murine Norovirus Capsid Protein Is Sufficient for Attenuation In Vivo","volume":"82","author":"Bailey","year":"2008","journal-title":"J. Virol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"4320","DOI":"10.1038\/s41467-021-24649-w","article-title":"Broadly Cross-Reactive Human Antibodies That Inhibit Genogroup I and II Noroviruses","volume":"12","author":"Alvarado","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"2449","DOI":"10.1099\/vir.0.021212-0","article-title":"Size and Mechanical Stability of Norovirus Capsids Depend on pH: A Nanoindentation Study","volume":"91","author":"Cuellar","year":"2010","journal-title":"J. Gen. Virol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"064006","DOI":"10.1088\/1361-648X\/aaa43b","article-title":"Norovirus-like VP1 Particles Exhibit Isolate Dependent Stability Profiles","volume":"30","author":"Pogan","year":"2018","journal-title":"J. Phys. Condens. Matter"},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Tan, M., Wei, C., Huang, P., Fan, Q., Quigley, C., Xia, M., Fang, H., Zhang, X., Zhong, W., and Klassen, J.S. (2015). Tulane Virus Recognizes Sialic Acids as Cellular Receptors. Sci. Rep., 5.","DOI":"10.1038\/srep11784"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"4092","DOI":"10.1128\/JVI.02245-08","article-title":"Ganglioside-Linked Terminal Sialic Acid Moieties on Murine Macrophages Function as Attachment Receptors for Murine Noroviruses","volume":"83","author":"Taube","year":"2009","journal-title":"J. Virol."},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Kim, D.-S., Hosmillo, M., Alfajaro, M.M., Kim, J.-Y., Park, J.-G., Son, K.-Y., Ryu, E.-H., Sorgeloos, F., Kwon, H.-J., and Park, S.-J. (2014). Both A2,3- and A2,6-Linked Sialic Acids on O-Linked Glycoproteins Act as Functional Receptors for Porcine Sapovirus. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1004172"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1099\/vir.0.82158-0","article-title":"Alpha2,6-Linked Sialic Acid Acts as a Receptor for Feline Calicivirus","volume":"88","author":"Stuart","year":"2007","journal-title":"J. Gen. Virol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"2378","DOI":"10.1128\/JVI.02832-14","article-title":"Structural Analysis of a Rabbit Hemorrhagic Disease Virus Binding to Histo-Blood Group Antigens","volume":"89","author":"Leuthold","year":"2014","journal-title":"J. Virol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"e01581-18","DOI":"10.1128\/JVI.01581-18","article-title":"Structural Basis for Human Norovirus Capsid Binding to Bile Acids","volume":"93","author":"Kilic","year":"2019","journal-title":"J. Virol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1086\/375742","article-title":"Noroviruses Bind to Human ABO, Lewis, and Secretor Histo\u2013Blood Group Antigens: Identification of 4 Distinct Strain-Specific Patterns","volume":"188","author":"Huang","year":"2003","journal-title":"J. Infect. Dis."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"8635","DOI":"10.1128\/JVI.00848-11","article-title":"Structural Analysis of Histo-Blood Group Antigen Binding Specificity in a Norovirus GII.4 Epidemic Variant: Implications for Epochal Evolution","volume":"85","author":"Shanker","year":"2011","journal-title":"J. Virol."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"D\u00fclfer, J., Yan, H., Brodmerkel, M.N., Creutznacher, R., Mallagaray, A., Peters, T., Caleman, C., Marklund, E.G., and Uetrecht, C. (2021). Glycan-Induced Protein Dynamics in Human Norovirus P Dimers Depend on Virus Strain and Deamidation Status. Molecules, 26.","DOI":"10.3390\/molecules26082125"},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Creutznacher, R., Maass, T., D\u00fclfer, J., Feldmann, C., Hartmann, V., Lane, M.S., Knickmann, J., Westermann, L.T., Thiede, L., and Smith, T.J. (2022). Distinct Dissociation Rates of Murine and Human Norovirus P-Domain Dimers Suggest a Role of Dimer Stability in Virus-Host Interactions. Commun. Biol., 5.","DOI":"10.1038\/s42003-022-03497-4"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1002\/cbic.201900572","article-title":"Chemical-Shift Perturbations Reflect Bile Acid Binding to Norovirus Coat Protein: Recognition Comes in Different Flavors","volume":"21","author":"Creutznacher","year":"2020","journal-title":"ChemBioChem"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"e00869-19","DOI":"10.1128\/JVI.00869-19","article-title":"The Coxsackievirus and Adenovirus Receptor, a Required Host Factor for Recovirus Infection, Is a Putative Enteric Calicivirus Receptor","volume":"93","author":"Farkas","year":"2019","journal-title":"J. Virol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1504","DOI":"10.1099\/jgv.0.000020","article-title":"Rhesus Enteric Calicivirus Surrogate Model for Human Norovirus Gastroenteritis","volume":"96","author":"Farkas","year":"2015","journal-title":"J. Gen. Virol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"e01851-23","DOI":"10.1128\/jvi.01851-23","article-title":"Strain-Specific Requirements of Susceptibility to Rhesus Enteric Calicivirus Infection","volume":"98","author":"Farkas","year":"2024","journal-title":"J. Virol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1038\/s41467-019-09251-5","article-title":"A Post-Translational Modification of Human Norovirus Capsid Protein Attenuates Glycan Binding","volume":"10","author":"Mallagaray","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1631\/jzus.B1900150","article-title":"O-GlcNAcylation, a Sweet Link to the Pathology of Diseases","volume":"20","author":"Nie","year":"2019","journal-title":"J. Zhejiang Univ. Sci. B"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1111\/imm.13245","article-title":"The Role of O-GlcNAcylation in Immunity against Infections","volume":"161","author":"Quik","year":"2020","journal-title":"Immunology"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"e00113-19","DOI":"10.1128\/JVI.00113-19","article-title":"Envelope Protein Glycosylation Mediates Zika Virus Pathogenesis","volume":"93","author":"Carbaugh","year":"2019","journal-title":"J. Virol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"e02215-16","DOI":"10.1128\/JVI.02215-16","article-title":"Glycosylation of the Hemagglutinin Protein of H5N1 Influenza Virus Increases Its Virulence in Mice by Exacerbating the Host Immune Response","volume":"91","author":"Zhao","year":"2017","journal-title":"J. Virol."},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Grant, O.C., Montgomery, D., Ito, K., and Woods, R.J. (2020). Analysis of the SARS-CoV-2 Spike Protein Glycan Shield Reveals Implications for Immune Recognition. Sci. Rep., 10.","DOI":"10.1038\/s41598-020-71748-7"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1093\/glycob\/cwac017","article-title":"Recombinant Norovirus Capsid Protein VP1 (GII.4) Expressed in H5 Insect Cells Exhibits Post-Translational Modifications with Potential Impact on Lectin Activity and Vaccine Design","volume":"32","author":"Hanisch","year":"2022","journal-title":"Glycobiology"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"e01261-23","DOI":"10.1128\/jvi.01261-23","article-title":"Production of Infectious Reporter Murine Norovirus by VP2 Trans-Complementation","volume":"98","author":"Ishiyama","year":"2024","journal-title":"J. Virol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"11429","DOI":"10.1128\/JVI.00696-08","article-title":"Recovery of Infectious Virus by Transfection of In Vitro-Generated RNA from Tulane Calicivirus cDNA","volume":"82","author":"Wei","year":"2008","journal-title":"J. Virol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"3080","DOI":"10.1099\/vir.0.2008\/003525-0","article-title":"A DNA-Launched Reverse Genetics System for Rabbit Hemorrhagic Disease Virus Reveals That the VP2 Protein Is Not Essential for Virus Infectivity","volume":"89","author":"Liu","year":"2008","journal-title":"J. Gen. Virol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.1126\/science.aaf5211","article-title":"Replication of Human Noroviruses in Stem Cell-Derived Human Enteroids","volume":"353","author":"Ettayebi","year":"2016","journal-title":"Science"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1939","DOI":"10.1038\/nprot.2015.121","article-title":"Human Norovirus Culture in B Cells","volume":"10","author":"Jones","year":"2015","journal-title":"Nat. Protoc."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1073\/pnas.1910138117","article-title":"Bile Acids and Ceramide Overcome the Entry Restriction for GII.3 Human Norovirus Replication in Human Intestinal Enteroids","volume":"117","author":"Murakami","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"e01136-20","DOI":"10.1128\/mSphere.01136-20","article-title":"New Insights and Enhanced Human Norovirus Cultivation in Human Intestinal Enteroids","volume":"6","author":"Ettayebi","year":"2021","journal-title":"mSphere"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"e00251-20","DOI":"10.1128\/mBio.00251-20","article-title":"Genetic Manipulation of Human Intestinal Enteroids Demonstrates the Necessity of a Functional Fucosyltransferase 2 Gene for Secretor-Dependent Human Norovirus Infection","volume":"11","author":"Haga","year":"2020","journal-title":"mBio"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"23782","DOI":"10.1073\/pnas.2010834117","article-title":"Human Norovirus Exhibits Strain-Specific Sensitivity to Host Interferon Pathways in Human Intestinal Enteroids","volume":"117","author":"Lin","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Yu, G., Zhang, D., Guo, F., Tan, M., Jiang, X., and Jiang, W. (2013). Cryo-EM Structure of a Novel Calicivirus, Tulane Virus. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0059817"},{"key":"ref_121","doi-asserted-by":"crossref","unstructured":"Snowden, J.S., Hurdiss, D.L., Adeyemi, O.O., Ranson, N.A., Herod, M.R., and Stonehouse, N.J. (2020). Dynamics in the Murine Norovirus Capsid Revealed by High-Resolution Cryo-EM. PLoS Biol., 18.","DOI":"10.1371\/journal.pbio.3000649"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"e01833-22","DOI":"10.1128\/jvi.01833-22","article-title":"Direct Blockade of the Norovirus Histo-Blood Group Antigen Binding Pocket by Nanobodies","volume":"97","author":"Kher","year":"2023","journal-title":"J. Virol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"6516","DOI":"10.1038\/s41467-023-42146-0","article-title":"A Single Nanobody Neutralizes Multiple Epochally Evolving Human Noroviruses by Modulating Capsid Plasticity","volume":"14","author":"Salmen","year":"2023","journal-title":"Nat. Commun."}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/16\/12\/1835\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T16:40:08Z","timestamp":1760114408000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/16\/12\/1835"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,11,26]]},"references-count":123,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2024,12]]}},"alternative-id":["v16121835"],"URL":"https:\/\/doi.org\/10.3390\/v16121835","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,11,26]]}}}