ArticleNature communications2020
Cryo-EM structure of the varicella-zoster virus A-capsid.
Article in Nature communications, 2020. 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.
- Therapeutic Poxviruses Induce the Secretion of Immunostimulating and Anti-Tumoral Extracellular Vesicles.Journal of extracellular vesicles · 2026Article
- Varicella Zoster Virus Infection: Clinical Features, Molecular Pathogenesis, Treatment, and Prevention.MedComm · 2026Review
- Cryogenic electron tomography reveals herpesvirus capsid assembly intermediates inside the cell nucleus.Nature communications · 2026Article
- Bee products as alternatives in the treatment of viral infections.Journal of the science of food and agriculture · 2026Review
- Review
- Cyclic GMP-AMP synthase recognizes the physical features of DNA.Acta pharmacologica Sinica · 2025Review
- Herpes Zoster in Pregnancy: Clinical Outcomes and Treatment Patterns from a Multicenter Retrospective Cohort.Journal of pain research · 2025Article
- Structures of Epstein-Barr virus and Kaposi's sarcoma-associated herpesvirus virions reveal species-specific tegument and envelope features.Journal of virology · 2024Article
- Advances in Alpha Herpes Viruses Vaccines for Human.Vaccines · 2023Review
- New Look of EBV LMP1 Signaling Landscape.Cancers · 2021Review
- Minimal Design Principles for Icosahedral Virus Capsids.ACS nano · 2021Article
- Article
- Structures and Divergent Mechanisms in Capsid Maturation and Stabilization Following Genome Packaging of Human Cytomegalovirus and Herpesviruses.Life (Basel, Switzerland) · 2021Review
- Congenital and Perinatal Varicella Infections.Newborn (Clarksville, Md.)Article
Corrections and comments
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Authors and funding
15 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Varicella-zoster virus (VZV), a member of the Alphaherpesvirinae subfamily, causes severe diseases in humans of all ages. The viral capsids play critical roles in herpesvirus infection, making them potential antiviral targets. Here, we present the 3.7-Å-resolution structure of the VZV A-capsid and define the molecular determinants underpinning the assembly of this complicated viral machinery. Overall, the VZV capsid has a similar architecture to that of other known herpesviruses. The major capsid protein (MCP) assembles into pentons and hexons, forming extensive intra- and inter-capsomer interaction networks that are further secured by the small capsid protein (SCP) and the heterotriplex. The structure reveals a pocket beneath the floor of MCP that could potentially be targeted by antiviral inhibitors. In addition, we identified two alphaherpesvirus-specific structural features in SCP and Tri1 proteins. These observations highlight the divergence of different herpesviruses and provide an important basis for developing antiviral drugs.
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