ArticleStructure (London, England : 1993)2014
Four levels of hierarchical organization, including noncovalent chainmail, brace the mature tumor herpesvirus capsid against pressurization.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The Structural Diversity of Encapsulin Protein Shells.Chembiochem : a European journal of chemical biology · 2024Review
- Capsid Structure ofJournal of virology · 2021Article
- Near-atomic cryo-electron microscopy structures of varicella-zoster virus capsids.Nature microbiology · 2020Article
- DNA-Packing Portal and Capsid-Associated Tegument Complexes in the Tumor Herpesvirus KSHV.Cell · 2019Article
- Article
- Structure and mutagenesis reveal essential capsid protein interactions for KSHV replication.Nature · 2018Article
- Structure of a headful DNA-packaging bacterial virus at 2.9 Å resolution by electron cryo-microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Extensive subunit contacts underpin herpesvirus capsid stability and interior-to-exterior allostery.Nature structural & molecular biology · 2016Article
- Article
- Article
- Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold.Virology · 2015Review
- CryoEM and mutagenesis reveal that the smallest capsid protein cements and stabilizes Kaposi's sarcoma-associated herpesvirus capsid.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Protein chainmail variants in dsDNA viruses.AIMS biophysics · 2015Article
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
Abstract
Like many double-stranded DNA viruses, tumor gammaherpesviruses Epstein-Barr virus and Kaposi's sarcoma-associated herpesvirus withstand high internal pressure. Bacteriophage HK97 uses covalent chainmail for this purpose, but how this is achieved noncovalently in the much larger gammaherpesvirus capsid is unknown. Our cryoelectron microscopy structure of a gammaherpesvirus capsid reveals a hierarchy of four levels of organization: (1) Within a hexon capsomer, each monomer of the major capsid protein (MCP), 1,378 amino acids and six domains, interacts with its neighboring MCPs at four sites. (2) Neighboring capsomers are linked in pairs by MCP dimerization domains and in groups of three by heterotrimeric triplex proteins. (3) Small (∼280 amino acids) HK97-like domains in MCP monomers alternate with triplex heterotrimers to form a belt that encircles each capsomer. (4) One hundred sixty-two belts concatenate to form noncovalent chainmail. The triplex heterotrimer orchestrates all four levels and likely drives maturation to an angular capsid that can withstand pressurization.
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