Faculty Opinions recommendation of Characterization of the archaeal thermophile Sulfolobus turreted icosahedral virus validates an evolutionary link among double-stranded DNA viruses from all domains of life.

2006 ◽  
Author(s):  
Eddie Holmes
Keyword(s):  
Dna Viruses ◽  
Double Stranded Dna ◽  
Icosahedral Virus ◽  
Domains Of Life ◽  
Sulfolobus Turreted Icosahedral Virus

scholarly journals Characterization of the Archaeal Thermophile Sulfolobus Turreted Icosahedral Virus Validates an Evolutionary Link among Double-Stranded DNA Viruses from All Domains of Life

2006 ◽  
Vol 80 (15) ◽  
pp. 7625-7635 ◽  
Author(s):  
Walid S. A. Maaty ◽  
Alice C. Ortmann ◽  
Mensur Dlakić ◽  
Katie Schulstad ◽  
Jonathan K. Hilmer ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
Hot Spring ◽  
Viral Proteins ◽  
Limited Information ◽  
Double Stranded Dna ◽  
Icosahedral Virus ◽  
Domains Of Life ◽  
Dsdna Viruses

ABSTRACT Icosahedral nontailed double-stranded DNA (dsDNA) viruses are present in all three domains of life, leading to speculation about a common viral ancestor that predates the divergence of Eukarya, Bacteria, and Archaea. This suggestion is supported by the shared general architecture of this group of viruses and the common fold of their major capsid protein. However, limited information on the diversity and replication of archaeal viruses, in general, has hampered further analysis. Sulfolobus turreted icosahedral virus (STIV), isolated from a hot spring in Yellowstone National Park, was the first icosahedral virus with an archaeal host to be described. Here we present a detailed characterization of the components forming this unusual virus. Using a proteomics-based approach, we identified nine viral and two host proteins from purified STIV particles. Interestingly, one of the viral proteins originates from a reading frame lacking a consensus start site. The major capsid protein (B345) was found to be glycosylated, implying a strong similarity to proteins from other dsDNA viruses. Sequence analysis and structural predication of virion-associated viral proteins suggest that they may have roles in DNA packaging, penton formation, and protein-protein interaction. The presence of an internal lipid layer containing acidic tetraether lipids has also been confirmed. The previously presented structural models in conjunction with the protein, lipid, and carbohydrate information reported here reveal that STIV is strikingly similar to viruses associated with the Bacteria and Eukarya domains of life, further strengthening the hypothesis for a common ancestor of this group of dsDNA viruses from all domains of life.

scholarly journals Phylogeny of the Varidnaviria Morphogenesis Module: Congruence and Incongruence With the Tree of Life and Viral Taxonomy

2021 ◽  
Vol 12 ◽  
Author(s):  
Anthony C. Woo ◽  
Morgan Gaia ◽  
Julien Guglielmini ◽  
Violette Da Cunha ◽  
Patrick Forterre
Keyword(s):  
Evolutionary History ◽  
International Committee ◽  
Tree Of Life ◽  
Dna Viruses ◽  
Origin And Evolution ◽  
Double Stranded Dna ◽  
Domains Of Life ◽  
History Of ◽  
Recent Classification ◽  
Jelly Roll

Double-stranded DNA viruses of the realm Varidnaviria (formerly PRD1-adenovirus lineage) are characterized by homologous major capsid proteins (MCPs) containing one (kingdom: Helvetiavirae) or two β-barrel domains (kingdom: Bamfordvirae) known as the jelly roll folds. Most of them also share homologous packaging ATPases (pATPases). Remarkably, Varidnaviria infect hosts from the three domains of life, suggesting that these viruses could be very ancient and share a common ancestor. Here, we analyzed the evolutionary history of Varidnaviria based on single and concatenated phylogenies of their MCPs and pATPases. We excluded Adenoviridae from our analysis as their MCPs and pATPases are too divergent. Sphaerolipoviridae, the only family in the kingdom Helvetiavirae, exhibit a complex history: their MCPs are very divergent from those of other Varidnaviria, as expected, but their pATPases groups them with Bamfordvirae. In single and concatenated trees, Bamfordvirae infecting archaea were grouped with those infecting bacteria, in contradiction with the cellular tree of life, whereas those infecting eukaryotes were organized into three monophyletic groups: the Nucleocytoviricota phylum, formerly known as the Nucleo-Cytoplasmic Large DNA Viruses (NCLDVs), Lavidaviridae (virophages) and Polintoviruses. Although our analysis mostly supports the recent classification proposed by the International Committee on Taxonomy of Viruses (ICTV), it also raises questions, such as the validity of the Adenoviridae and Helvetiavirae ranking. Based on our phylogeny, we discuss current hypotheses on the origin and evolution of Varidnaviria and suggest new ones to reconcile the viral and cellular trees.

scholarly journals The Architecture and Chemical Stability of the Archaeal Sulfolobus Turreted Icosahedral Virus

2010 ◽  
Vol 84 (18) ◽  
pp. 9575-9583 ◽  
Author(s):  
Reza Khayat ◽  
Chi-yu Fu ◽  
Alice C. Ortmann ◽  
Mark J. Young ◽  
John E. Johnson
Keyword(s):  
Major Capsid Protein ◽  
Virus Genome ◽  
Archaeal Virus ◽  
Double Stranded Dna ◽  
Cryo Electron Microscopy ◽  
Resolution Electron ◽  
Capsid Shell ◽  
Icosahedral Virus ◽  
Sulfolobus Turreted Icosahedral Virus ◽  
Made In

ABSTRACT Viruses utilize a diverse array of mechanisms to deliver their genomes into hosts. While great strides have been made in understanding the genome delivery of eukaryotic and prokaryotic viruses, little is known about archaeal virus genome delivery and the associated particle changes. The Sulfolobus turreted icosahedral virus (STIV) is a double-stranded DNA (dsDNA) archaeal virus that contains a host-derived membrane sandwiched between the genome and the proteinaceous capsid shell. Using cryo-electron microscopy (cryo-EM) and different biochemical treatments, we identified three viral morphologies that may correspond to biochemical disassembly states of STIV. One of these morphologies was subtly different from the previously published 27-Å-resolution electron density that was interpreted with the crystal structure of the major capsid protein (MCP). However, these particles could be analyzed at 12.5-Å resolution by cryo-EM. Comparing these two structures, we identified the location of multiple proteins forming the large turret-like appendages at the icosahedral vertices, observed heterogeneous glycosylation of the capsid shell, and identified mobile MCP C-terminal arms responsible for tethering and releasing the underlying viral membrane to and from the capsid shell. Collectively, our studies allow us to propose a fusogenic mechanism of genome delivery by STIV, in which the dismantled capsid shell allows for the fusion of the viral and host membranes and the internalization of the viral genome.

scholarly journals Diversification of giant and large eukaryotic dsDNA viruses predated the origin of modern eukaryotes

2018 ◽  
Author(s):  
Julien Guglielmini ◽  
Anthony Woo ◽  
Mart Krupovic ◽  
Patrick Forterre ◽  
Morgan Gaia
Keyword(s):  
Phylogenetic Trees ◽  
Dna Viruses ◽  
Double Stranded Dna ◽  
Virion Morphogenesis ◽  
History Of ◽  
Eukaryotic Dna ◽  
Dsdna Viruses ◽  
Virion Formation

AbstractGiant and large eukaryotic double-stranded DNA viruses from the Nucleo-Cytoplasmic Large DNA Virus (NCLDV) assemblage represent a remarkably diverse and potentially ancient component of the eukaryotic virome. However, their origin(s), evolution and potential roles in the emergence of modern eukaryotes remain a subject of intense debate. Since the characterization of the mimivirus in 2003, many big and giant viruses have been discovered at a steady pace, offering a vast material for evolutionary investigations. In parallel, phylogenetic tools are constantly being improved, offering more rigorous approaches for reconstruction of deep evolutionary history of viruses and their hosts. Here we present robust phylogenetic trees of NCLDVs, based on the 8 most conserved proteins responsible for virion morphogenesis and informational processes. Our results uncover the evolutionary relationships between different NCLDV families and support the existence of two superclades of NCLDVs, each encompassing several families. We present evidence strongly suggesting that the NCLDV core genes, which are involved in both informational processes and virion formation, were acquired vertically from a common ancestor. Among them, the largest subunits of the DNA-dependent RNA polymerase were seemingly transferred from two clades of NCLDVs to proto-eukaryotes, giving rise to two of the three eukaryotic DNA-dependent RNA polymerases. Our results strongly suggest that these transfers and the diversification of NCLDVs predated the emergence of modern eukaryotes, emphasizing the major role of viruses in the evolution of cellular domains.

scholarly journals Evolution of the PRD1-adenovirus lineage: a viral tree of life incongruent with the cellular universal tree of life

2019 ◽  
Author(s):  
Anthony C. Woo ◽  
Morgan Gaia ◽  
Julien Guglielmini ◽  
Violette Da Cunha ◽  
Patrick Forterre
Keyword(s):  
Evolutionary History ◽  
Common Ancestor ◽  
Tree Of Life ◽  
Capsid Proteins ◽  
Dna Viruses ◽  
Universal Tree ◽  
Double Stranded Dna ◽  
Domains Of Life ◽  
History Of ◽  
Jelly Roll

AbstractDouble-stranded DNA viruses of the PRD1-adenovirus lineage are characterized by homologous major capsid proteins containing one or two β-barrel domains known as the jelly roll folds. Most of them also share homologous packaging ATPases of the FtsK/HerA superfamily P-loop ATPases. Remarkably, members of this lineage infect hosts from the three domains of life, suggesting that viruses from this lineage could be very ancient and share a common ancestor. Here we analyzed the evolutionary history of these cosmopolitan viruses by inferring phylogenies based on single or concatenated genes. These viruses can be divided into two supergroups infecting either eukaryotes or prokaryotes. The latter can be further divided into two groups of bacterioviruses and one group of archaeoviruses. This viral tree is thus incongruent with the cellular tree of life in which Archaea are closer to Eukarya and more divergent from Bacteria. We discuss various evolutionary scenarios that could explain this paradox.

scholarly journals Structure of A197 from Sulfolobus Turreted Icosahedral Virus: a Crenarchaeal Viral Glycosyltransferase Exhibiting the GT-A Fold

2006 ◽  
Vol 80 (15) ◽  
pp. 7636-7644 ◽  
Author(s):  
Eric T. Larson ◽  
Dirk Reiter ◽  
Mark Young ◽  
C. Martin Lawrence
Keyword(s):  
Hot Springs ◽  
Three Dimensional ◽  
Open Reading Frames ◽  
Dimensional Structure ◽  
Evolutionary Information ◽  
Reading Frame ◽  
Bacteriophage Prd1 ◽  
Icosahedral Virus ◽  
Domains Of Life ◽  
Sulfolobus Turreted Icosahedral Virus

ABSTRACT Sulfolobus turreted icosahedral virus (STIV) was the first icosahedral virus characterized from an archaeal host. It infects Sulfolobus species that thrive in the acidic hot springs (pH 2.9 to 3.9 and 72 to 92°C) of Yellowstone National Park. The overall capsid architecture and the structure of its major capsid protein are very similar to those of the bacteriophage PRD1 and eukaryotic viruses Paramecium bursaria Chlorella virus 1 and adenovirus, suggesting a viral lineage that predates the three domains of life. The 17,663-base-pair, circular, double-stranded DNA genome contains 36 potential open reading frames, whose sequences generally show little similarity to other genes in the sequence databases. However, functional and evolutionary information may be suggested by a protein's three-dimensional structure. To this end, we have undertaken structural studies of the STIV proteome. Here we report our work on A197, the product of an STIV open reading frame. The structure of A197 reveals a GT-A fold that is common to many members of the glycosyltransferase superfamily. A197 possesses a canonical DXD motif and a putative catalytic base that are hallmarks of this family of enzymes, strongly suggesting a glycosyltransferase activity for A197. Potential roles for the putative glycosyltransferase activity of A197 and their evolutionary implications are discussed.

scholarly journals Functional expression of the eukaryotic proton pump rhodopsin OmR2 in Escherichia coli and its photochemical characterization

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Masuzu Kikuchi ◽  
Keiichi Kojima ◽  
Shin Nakao ◽  
Susumu Yoshizawa ◽  
Shiho Kawanishi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Proton Pump ◽  
Expression System ◽  
Spectroscopic Characterization ◽  
Functional Expression ◽  
Proton Pumping ◽  
E Coli ◽  
Oxyrrhis Marina ◽  
Domains Of Life

AbstractMicrobial rhodopsins are photoswitchable seven-transmembrane proteins that are widely distributed in three domains of life, archaea, bacteria and eukarya. Rhodopsins allow the transport of protons outwardly across the membrane and are indispensable for light-energy conversion in microorganisms. Archaeal and bacterial proton pump rhodopsins have been characterized using an Escherichia coli expression system because that enables the rapid production of large amounts of recombinant proteins, whereas no success has been reported for eukaryotic rhodopsins. Here, we report a phylogenetically distinct eukaryotic rhodopsin from the dinoflagellate Oxyrrhis marina (O. marina rhodopsin-2, OmR2) that can be expressed in E. coli cells. E. coli cells harboring the OmR2 gene showed an outward proton-pumping activity, indicating its functional expression. Spectroscopic characterization of the purified OmR2 protein revealed several features as follows: (1) an absorption maximum at 533 nm with all-trans retinal chromophore, (2) the possession of the deprotonated counterion (pKa = 3.0) of the protonated Schiff base and (3) a rapid photocycle through several distinct photointermediates. Those features are similar to those of known eukaryotic proton pump rhodopsins. Our successful characterization of OmR2 expressed in E. coli cells could build a basis for understanding and utilizing eukaryotic rhodopsins.

Optical Absorption Spectroscopy of DNA-Wrapped HiPco Carbon Nanotubes

2019 ◽  
Vol 943 ◽  
pp. 95-99
Author(s):  
Li Jun Wang ◽  
Kazuo Umemura
Keyword(s):  
Carbon Nanotubes ◽  
Aqueous Solution ◽  
Optical Absorption ◽  
Absorption Spectroscopy ◽  
Near Infrared ◽  
Nir Spectroscopy ◽  
Optical Characterization ◽  
Optical Absorption Spectroscopy ◽  
Double Stranded Dna

Optical absorption spectroscopy provides evidence for individually dispersed carbon nanotubes. A common method to disperse SWCNTs into aqueous solution is to sonicate the mixture in the presence of a double-stranded DNA (dsDNA). In this paper, optical characterization of dsDNA-wrapped HiPco carbon nanotubes (dsDNA-SWCNT) was carried out using near infrared (NIR) spectroscopy and photoluminescence (PL) experiments. The findings suggest that SWCNT dispersion is very good in the environment of DNA existing. Additionally, its dispersion depends on dsDNA concentration.

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