Cryo-electron microscopy structures of capsids and in situ portals of DNA-devoid capsids of human cytomegalovirus

Cryo-electron microscopy structures of capsids and in situ portals of DNA-devoid capsids of human cytomegalovirus | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Article Cryo-electron microscopy structures of capsids and in situ portals of DNA-devoid capsids of human cytomegalovirus Zhihai Li, Jingjing Pang, Rongchao Gao, Qingxia Wang, Xuekui Yu, and 1 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-2270722/v1 This work is licensed under a CC BY 4.0 License Status: Published Journal Publication published 11 Apr, 2023 Read the published version in Nature Communications → Version 1 posted You are reading this latest preprint version Abstract The portal-scaffold complex is believed to nucleate the assembly of procapsids of herpesviruses. During capsid maturation process, two events occur: expulsion of the scaffold and the incorporation of DNA. The portal-scaffold interaction and the conformational changes to the portal during the different stages of capsid assembly and maturation have yet to be elucidated structurally. Here, we present high-resolution structures of the A- and B-capsids and in-situ portals of human cytomegalovirus. We show that scaffolds bind to the hydrophobic cavities formed by the dimerization and Johnson-fold domains of the major capsid proteins. We further show that 12 loop-helix-loop fragments, presumably from the scaffold domain of the scaffold, insert into the hydrophobic pocket of the portal crown domain. The portal also undergoes significant changes both positionally and conformationally accompanying DNA packaging. These findings not only provide insights into how the portal interacts with the scaffold proteins to nucleate capsid assembly but further our understanding of the mechanism of scaffold expulsion and DNA incorporation during maturation. Biological sciences/Structural biology/Electron microscopy/Cryoelectron microscopy Health sciences/Diseases/Infectious diseases/Viral infection Full Text Additional Declarations There is NO Competing Interest. Supplementary Files NCOMMS2253040TYu.pdf Reporting Summary Cite Share Download PDF Status: Published Journal Publication published 11 Apr, 2023 Read the published version in Nature Communications → Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. 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Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-2270722","acceptedTermsAndConditions":true,"allowDirectSubmit":false,"archivedVersions":[],"articleType":"Article","associatedPublications":[],"authors":[{"id":161875789,"identity":"22cca9f6-62fb-4561-8d92-a676b29c5616","order_by":0,"name":"Zhihai Li","email":"","orcid":"","institution":"Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Zhihai","middleName":"","lastName":"Li","suffix":""},{"id":161875790,"identity":"76256b23-4078-4143-837f-4b99cbf252d0","order_by":1,"name":"Jingjing 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