Structure of large dsDNA viruses

Klose, Thomas; Rossmann, Michael G.

doi:10.1515/hsz-2014-0145

Cited by 22 publications

(28 citation statements)

References 59 publications

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“…Viruses with icosahedral virions represent more than half of all recognized virus families (41). These viruses display remarkable diversity of virion sizes and complexity, from small capsids composed of a single protein, as in the case of simple single-stranded RNA (ssRNA) and ssDNA viruses (42,43), to extravagantly large, multilayered virions, such as those of mimiviruses (44). There are three major architectural classes of viruses with icosahedral capsids and dsDNA genomes, two of which are featured by viruses infecting hosts in all three cellular domains, testifying to their antiquity (41).…”

Section: Discussionmentioning

confidence: 99%

A Novel Type of Polyhedral Viruses Infecting Hyperthermophilic Archaea

Liu

Ishino

et al. 2017

J Virol

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Encapsidation of genetic material into polyhedral particles is one of the most common structural solutions employed by viruses infecting hosts in all three domains of life. Here, we describe a new virus of hyperthermophilic archaea, Sulfolobus polyhedral virus 1 (SPV1), which condenses its circular double-stranded DNA genome in a manner not previously observed for other known viruses. The genome complexed with virion proteins is wound up sinusoidally into a spherical coil which is surrounded by an envelope and further encased by an outer polyhedral capsid apparently composed of the 20-kDa virion protein. Lipids selectively acquired from the pool of host lipids are integral constituents of the virion. None of the major virion proteins of SPV1 show similarity to structural proteins of known viruses. However, minor structural proteins, which are predicted to mediate host recognition, are shared with other hyperthermophilic archaeal viruses infecting members of the order Sulfolobales. The SPV1 genome consists of 20,222 bp and contains 45 open reading frames, only one-fifth of which could be functionally annotated.IMPORTANCE Viruses infecting hyperthermophilic archaea display a remarkable morphological diversity, often presenting architectural solutions not employed by known viruses of bacteria and eukaryotes. Here we present the isolation and characterization of Sulfolobus polyhedral virus 1, which condenses its genome into a unique spherical coil. Due to the original genomic and architectural features of SPV1, the virus should be considered a representative of a new viral family, "Portogloboviridae."KEYWORDS archaea, hyperthermophile, viral genome, virion structure O ne of the most unexpected results of recent studies on viral diversity is the unveiling of astounding morphological variety of DNA viruses in geothermal environments with temperatures exceeding 80°C (1). Hardly over two dozen viruses isolated from such environments, all parasitizing hyperthermophilic members of the domain Archaea, display diverse virion shapes, many of which have not been observed among viruses from the two other domains of life, Bacteria and Eukarya. Due to distinct genome compositions and peculiar morphological properties of these viruses, 11 new virus families were established by the International Committee on Taxonomy of Viruses (ICTV) for the classification of these viruses (1-4).The remarkable morphological diversity of hyperthermophilic archaeal viruses radically contrasts the limited structural diversity of double-stranded DNA (dsDNA) viruses of Bacteria, nearly all of which, with the exception of several pleomorphic species, have icosahedral particles, with or without helical tails (5). The existing picture seems to accurately reflect the actual differences between bacterial and archaeal viruses. The morphological landscape of bacterial viruses is formed by more than six thousand species, whereas that of hyperthermophilic archaeal viruses is formed by only a couple of dozen known species. Moreover, while no new morpho...

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Section: Discussionmentioning

confidence: 99%

A Novel Type of Polyhedral Viruses Infecting Hyperthermophilic Archaea

Liu

Ishino

et al. 2017

J Virol

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“…In the models of large and giant viral capsids only the regular icosahedron is ordinarily taken from the CK model. [32][33][34] This icosahedron is not covered with a common hexagonal lattice. Instead, its neighboring faces are decorated with differently oriented (but symmetrically equivalent) trigonal patterns.…”

Section: Introductionmentioning

confidence: 99%

Static and dynamic hidden symmetries of icosahedral viral capsids

2017

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Viral shells self-assemble from identical proteins, which tend to form equivalent environments in the resulting assembly. However, in icosahedral capsids containing more than 60 proteins, they are enforced to occupy not only the symmetrically equivalent locations but also the quasi-equivalent ones. Due to this important fact, static and dynamic symmetries of viral shells can include additional hidden components. Here, developing the Caspar and Klug ideas concerning the quasi-equivalence of protein environments, we derive the simplest hexagonal tilings, that in principle could correspond to the local protein order in viral shells, and apply the resulting theory to nucleocytoplasmic large dsDNA viruses. In addition, analyzing the dynamic symmetry of the P22 viral shell, we demonstrate that the collective critical modes responsible for the protein reorganization during the procapsid maturation are approximately equivalent to the normal modes of the isotropic spherical membrane with O(3) symmetry. Furthermore, we establish the relationship between the dynamic symmetry of the P22 procapsid and the protein arrangement regularities that appear only in the mature capsid.

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“…The hexon monomer comprises two β‐barrel structures, each of which is comprised of eight stranded β‐sheets that form a jelly‐roll‐type fold. The jelly‐roll motif was subsequently identified in the structural proteins of other unrelated viruses , consistent with the idea that multiple virus protein species have evolved from a common ancestor (Fig. ).…”

Section: Topic 3: Lessons Learned From Structural Analyses Of Hadvmentioning

confidence: 99%

Lessons learned from adenovirus (1970–2019)

Nemerow

Flint

2019

FEBS Letters

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Animal viruses are well recognized for their ability to uncover fundamental cell and molecular processes, and adenovirus certainly provides a prime example. This review illustrates the lessons learned from studying adenovirus over the past five decades. We take a look back at the key studies of adenovirus structure and biophysical properties, which revealed the mechanisms of adenovirus association with antibody, cell receptor, and immune molecules that regulate infection. In addition, we discuss the critical contribution of studies of adenovirus gene expression to elucidation of fundamental reactions in pre‐mRNA processing and its regulation. Other pioneering studies furnished the first examples of protein‐primed initiation of DNA synthesis and viral small RNAs. As a nonenveloped virus, adenoviruses have furnished insights into the modes of virus attachment, entry, and penetration of host cells, and we discuss the diversity of cell receptors that support these processes, as well as membrane penetration. As a result of these extensive studies, adenovirus vectors were among the first to be developed for therapeutic applications. We highlight some of the early (unsuccessful) trials and the lessons learned from them.

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Structure of large dsDNA viruses

Cited by 22 publications

References 59 publications

A Novel Type of Polyhedral Viruses Infecting Hyperthermophilic Archaea

A Novel Type of Polyhedral Viruses Infecting Hyperthermophilic Archaea

Static and dynamic hidden symmetries of icosahedral viral capsids

Lessons learned from adenovirus (1970–2019)

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