The Ins and Outs of Herpesviral Capsids: Divergent Structures and Assembly Mechanisms across the Three Subfamilies
Autor: | Elizabeth B Draganova, Ekaterina E. Heldwein, Jonathan Valentin |
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Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
assembly
viruses Population Severe disease Review Computational biology Biology Virus Replication Genome Microbiology Viral Proteins chemistry.chemical_compound herpesvirus Virology capsid Humans education Herpesviridae education.field_of_study Virus Assembly Cryoelectron Microscopy Virion Replication cycle QR1-502 capsid associated-tegument complex (CATC) Infectious Diseases Capsid chemistry Capsid Proteins Human herpesvirus DNA |
Zdroj: | Viruses, Vol 13, Iss 1913, p 1913 (2021) Viruses |
ISSN: | 1999-4915 |
Popis: | Human herpesviruses, classified into three subfamilies, are double-stranded DNA viruses that establish lifelong latent infections within most of the world’s population and can cause severe disease, especially in immunocompromised people. There is no cure, and current preventative and therapeutic options are limited. Therefore, understanding the biology of these viruses is essential for finding new ways to stop them. Capsids play a central role in herpesvirus biology. They are sophisticated vehicles that shelter the pressurized double-stranded-DNA genomes while ensuring their delivery to defined cellular destinations on the way in and out of the host cell. Moreover, the importance of capsids for multiple key steps in the replication cycle makes their assembly an attractive therapeutic target. Recent cryo-electron microscopy reconstructions of capsids from all three subfamilies of human herpesviruses revealed not only conserved features but also remarkable structural differences. Furthermore, capsid assembly studies have suggested subfamily-specific roles of viral capsid protein homologs. In this review, we compare capsid structures, assembly mechanisms, and capsid protein functions across human herpesvirus subfamilies, highlighting the differences. |
Databáze: | OpenAIRE |
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