ArticleNature communications2019
Atomic structure of the human herpesvirus 6B capsid and capsid-associated tegument complexes.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- Cryogenic electron tomography reveals herpesvirus capsid assembly intermediates inside the cell nucleus.Nature communications · 2026Article
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- The functions of herpesvirus shuttling proteins in the virus lifecycle.Frontiers in microbiology · 2025Review
- Structures of Epstein-Barr virus and Kaposi's sarcoma-associated herpesvirus virions reveal species-specific tegument and envelope features.Journal of virology · 2024Article
- Mirusviruses link herpesviruses to giant viruses.Nature · 2023Article
- Structures of pseudorabies virus capsids.Nature communications · 2022Article
- Assembly of infectious Kaposi's sarcoma-associated herpesvirus progeny requires formation of a pORF19 pentamer.PLoS biology · 2021Article
- The Ins and Outs of Herpesviral Capsids: Divergent Structures and Assembly Mechanisms across the Three Subfamilies.Viruses · 2021Review
- Structure of human cytomegalovirus virion reveals host tRNA binding to capsid-associated tegument protein pp150.Nature communications · 2021Article
- Structural basis for genome packaging, retention, and ejection in human cytomegalovirus.Nature communications · 2021Article
- Article
- Structures and Divergent Mechanisms in Capsid Maturation and Stabilization Following Genome Packaging of Human Cytomegalovirus and Herpesviruses.Life (Basel, Switzerland) · 2021Review
- Near-atomic cryo-electron microscopy structures of varicella-zoster virus capsids.Nature microbiology · 2020Article
- Structures of capsid and capsid-associated tegument complex inside the Epstein-Barr virus.Nature microbiology · 2020Article
- Cryo-EM structure of the varicella-zoster virus A-capsid.Nature communications · 2020Article
- Genome organization and interaction with capsid protein in a multipartite RNA virus.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Human herpesvirus 6B (HHV-6B) belongs to the β-herpesvirus subfamily of the Herpesviridae. To understand capsid assembly and capsid-tegument interactions, here we report atomic structures of HHV-6B capsid and capsid-associated tegument complex (CATC) obtained by cryoEM and sub-particle reconstruction. Compared to other β-herpesviruses, HHV-6B exhibits high similarity in capsid structure but organizational differences in its CATC (pU11 tetramer). 180 "VΛ"-shaped CATCs are observed in HHV-6B, distinguishing from the 255 "Λ"-shaped dimeric CATCs observed in murine cytomegalovirus and the 310 "Δ"-shaped CATCs in human cytomegalovirus. This trend in CATC quantity correlates with the increasing genomes sizes of these β-herpesviruses. Incompatible distances revealed by the atomic structures rationalize the lack of CATC's binding to triplexes Ta, Tc, and Tf in HHV-6B. Our results offer insights into HHV-6B capsid assembly and the roles of its tegument proteins, including not only the β-herpesvirus-specific pU11 and pU14, but also those conserved across all subfamilies of Herpesviridae.
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