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1. Virus capsid assembly across different length scales inspire the development of virus-based biomaterials

   https://doi.org/10.1016/j.coviro.2019.02.010  

   Selivanovitch, Ekaterina; Douglas, Trevor (June 2019, Current Opinion in Virology)
2. The Integrity of the Intradimer Interface of the Hepatitis B Virus Capsid Protein Dimer Regulates Capsid Self-Assembly

   https://doi.org/10.1021/acschembio.0c00277  

   Zhao, Zhongchao; Wang, Joseph Che-Yen; Segura, Carolina Pérez; Hadden-Perilla, Jodi A.; Zlotnick, Adam (December 2020, ACS Chemical Biology)
3. Multiscale Modeling of Hepatitis B Virus Capsid Assembly and Its Dimorphism

   https://doi.org/10.1021/acsnano.2c02119  

   Mohajerani, Farzaneh; Tyukodi, Botond; Schlicksup, Christopher J.; Hadden-Perilla, Jodi A.; Zlotnick, Adam; Hagan, Michael F. (September 2022, ACS Nano)
4. Genome organization and interaction with capsid protein in a multipartite RNA virus

   https://doi.org/10.1073/pnas.1915078117  

   Beren, Christian; Cui, Yanxiang; Chakravarty, Antara; Yang, Xue; Rao, A. L. N.; Knobler, Charles M.; Zhou, Z. Hong; Gelbart, William M. (May 2020, Proceedings of the National Academy of Sciences)

   We report the asymmetric reconstruction of the single-stranded RNA (ssRNA) content in one of the three otherwise identical virions of a multipartite RNA virus, brome mosaic virus (BMV). We exploit a sample consisting exclusively of particles with the same RNA content—specifically, RNAs 3 and 4—assembled in planta by agrobacterium-mediated transient expression. We find that the interior of the particle is nearly empty, with most of the RNA genome situated at the capsid shell. However, this density is disordered in the sense that the RNA is not associated with any particular structure but rather, with an ensemble of secondary/tertiary structures that interact with the capsid protein. Our results illustrate a fundamental difference between the ssRNA organization in the multipartite BMV viral capsid and the monopartite bacteriophages MS2 and Qβ for which a dominant RNA conformation is found inside the assembled viral capsids, with RNA density conserved even at the center of the particle. This can be understood in the context of the differing demands on their respective lifecycles: BMV must package separately each of several different RNA molecules and has been shown to replicate and package them in isolated, membrane-bound, cytoplasmic complexes, whereas the bacteriophages exploit sequence-specific “packaging signals” throughout the viral RNA to package their monopartite genomes. 

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5. The Structure of Spiroplasma Virus 4: Exploring the Capsid Diversity of the Microviridae

   https://doi.org/10.3390/v16071103  

   Mietzsch, Mario; Kailasan, Shweta; Bennett, Antonette; Chipman, Paul; Fane, Bentley; Huiskonen, Juha T; Clarke, Ian N; McKenna, Robert (July 2024, Viruses)

   Spiroplasma virus 4 (SpV4) is a bacteriophage of the Microviridae, which packages circular ssDNA within non-enveloped T = 1 icosahedral capsids. It infects spiroplasmas, which are known pathogens of honeybees. Here, the structure of the SpV4 virion is determined using cryo-electron microscopy to a resolution of 2.5 Å. A striking feature of the SpV4 capsid is the mushroom-like protrusions at the 3-fold axes, which is common among all members of the subfamily Gokushovirinae. While the function of the protrusion is currently unknown, this feature varies widely in this subfamily and is therefore possibly an adaptation for host recognition. Furthermore, on the interior of the SpV4 capsid, the location of DNA-binding protein VP8 was identified and shown to have low structural conservation to the capsids of other viruses in the family. The structural characterization of SpV4 will aid future studies analyzing the virus–host interaction, to understand disease mechanisms at a molecular level. Furthermore, the structural comparisons in this study, including a low-resolution structure of the chlamydia phage 2, provide an overview of the structural repertoire of the viruses in this family that infect various bacterial hosts, which in turn infect a wide range of animals and plants. 

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