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Lipothrixviridae | ICTV

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data-contextual-token="EGZbqN49OnqdTCv6ryGIQ0ncfHWO3AIGYwkVMbp46SI" data-drupal-ajax-container=""></div> <h1 class="title page-title">Lipothrixviridae</h1> </div> </div> </div> </div> </div> </div> </div> </div> </div> </div> <div class="system-messages clearfix"> <div class="container"> <div class="row"> <div class="col-12"> <div class="region region-system-messages"> <div data-drupal-messages-fallback class="hidden"></div> </div> </div> </div> </div> </div> <div id="main-content" class="clearfix main-content region--bright-background region--no-separator"> <div class="container-fluid"> <div class="clearfix main-content__container"> <div class="row"> <section class="col-12 pe-xl-5 ps-xl-5"> <div class="clearfix main-content__section region--no-block-paddings region--no-paddings" > <div class="region region-content"> <article data-history-node-id="2045" class="contextual-region node node--type-report-9th node--view-mode-full clearfix"> <div class="node__container"> <div class="node__main-content clearfix"> <div class="_none bs-pb-4"><div class="container-fluid"> <div class="row-9height layout row layout-builder__layout"> <div class="col-lg-6 col-md-6 col-12 col-9left"> <div class="_none clearfix block block-layout-builder block-field-blocknodereport-9thfield-mt-srv-body"> <div class="content"> <div class="clearfix text-formatted field field--name-field-mt-srv-body field--type-text-with-summary field--label-hidden field__item"><h1 class="ChapterNumber">Family:&nbsp;<em>Lipothrixviridae</em></h1> <div> <h4><b>Chapter Version: ICTV Ninth Report; 2009 Taxonomy Release</b></h4> </div> <h2>General properties</h2> <p class="para">Virions are flexible filaments that vary from 410 to 2200 nm in length and 24 to 38 nm in diameter. They are enveloped, and the envelope consists of viral proteins and host derived lipids. The helical nucleoprotein core contains a single molecule of linear dsDNA, 15.9&ndash;56 kbp long. Virion ends have specific structures that vary between genera (Figure 1).</p> <h1></h1> <h1>Genus <em>Alphalipothrixvirus</em></h1> <p class="UnnumberedList">Type species <b>Thermoproteus tenax virus 1</b></p> <h2>Distinguishing features</h2> <p class="para">The width of the virion significantly exceeds that of other members of the family, most likely reflecting exceptional properties of the helical core. The terminal structures are also exceptional: both ends are rounded and do not taper, as in case of members of the other genera. None of the putative genes of the sole member of the genus shows any sequence similarity to sequences in extant databases.</p> <h2>Virion properties</h2> <h3>Morphology</h3> <p class="para">The virion is a rigid rod, about 410 nm long and 38 nm in diameter, with apparently asymmetric extensions at each end. The envelope encloses a helical core consisting of dsDNA and two DNA-binding proteins (Figures 1, 2).</p> <h3>Physicochemical and physical properties</h3> <p class="para">Virion Mr is 3.3&thinsp;&times;10<sup>8</sup> and buoyant density in CsCl is 1.25 g cm<sup>&minus;3</sup>. The virions are stable at 100 &deg;C and a fraction remains viable after autoclaving at 120 &deg;C. Particles maintain their structure in 6M urea and 7M guanidine hydrochloride. Detergents (e.g. Triton X-100 and octylglycoside), dissociate virions into viral cores, containing the DNA and DNA-binding proteins, and viral envelopes, containing isoprenyl ether lipids and capsid proteins (Figure 2). The virion consists of about 3% (w/w) DNA, 75% protein and 22% isoprenyl ether lipids.</p> <h3>Nucleic acid</h3> <p class="para">The virion contains one molecule of linear dsDNA of 15.9 kbp. The ends of the molecule are masked in an unknown manner.</p> <h3>Proteins</h3> <p class="para">The virion contains at least four proteins with molecular masses of 12.9, 16.3, 18.1 and 24.5 kDa. The two smallest form the virion core and highly hydrophobic 18.1 kDa protein is present in the envelope. Additional minor proteins may be present.</p> <h3>Lipids</h3> <p class="para">The virion envelope carries the same lipids as the host membrane, essentially diphytanyl tetraether lipids. The envelope has a bilayer structure. The phosphate residues of the phospholipids are oriented towards the inside and the glycosyl residues towards the outside of the particles.</p> <h3>Carbohydrates</h3> <p class="para">No information available.</p> <h2>Genome organization and replication</h2> <p class="para">About 85% of the total genome sequence has been determined. The genome contains several transcription units. So far, the function of only a few genes is known, among them those encoding the four structural proteins. These genes are not linked. The genome carries two low complexity sequence regions consisting of the repetitive sequence CCNACN (where N is any nucleotide), one located within the tpx gene and the other in a noncoding region. Frequent recombination appears to occur between these two regions which generates multiple variants of the TPX protein, which is present in infected cells in high amounts, however, is absent among virion proteins. No information is available on genome replication.</p> <h2>Antigenic properties</h2> <p class="para">No information available.</p> <h2>Biological properties</h2> <p class="para">Host range is limited to the hyperthermophilic archaeaon <i>Thermoproteus tenax</i>. Adsorption and infection appear to proceed via interaction of the terminal protrusions of the virion with the host pili. The virus is temperate and virions are released by cell lysis. The viral genome is present in the host cells in a linear non-integrated form, and only its fragments were found to be integrated in the host chromosome. Mature virions assemble in host cell lumen prior to their release.</p> <h2>List of species demarcation criteria in the genus</h2> <p class="para">Not applicable.</p> <p class="para"></p> <h2>List of species in the genus <i>Alphalipothrixvirus</i></h2> <p class="para">&nbsp;</p> <table border="1" cellspacing="0" cellpadding="0" style="border:none;"> <tbody> <tr> <td valign="top" style="border:1pt solid windowtext;"> <p><i>Thermoproteus tenax virus 1</i></p> </td> <td valign="top"> <p>&nbsp;</p> </td> <td valign="top"> <p>&nbsp;</p> </td> </tr> <tr> <td valign="top"> <p>&nbsp;Thermoproteus tenax virus 1</p> </td> <td valign="top"> <p>[X14855]</p> </td> <td valign="top"> <p>(TTV-1)</p> </td> </tr> </tbody> </table> <p class="Legend">Species names are in italic script; names of isolates are in roman script. Sequence accession numbers [ ] and assigned abbreviations ( ) are also listed.</p> <h2>Other related viruses which may be members of the genus <i>Alphalipothrixvirus</i> but have not been approved as species</h2> <p class="para">None reported.</p> <h1></h1> <h1>Genus <em>Betalipothrixvirus</em></h1> <p class="UnnumberedList">Type species <b>Sulfolobus islandicus filamentous virus</b></p> <h2>Distinguishing features</h2> <p class="para">The virions are the longest in the family. Their terminal structures, as well as DNA arrangement in the virion core, differ from those of members of the other genera. The genomes show a limited sequence similarity to the genomes of members of the other genera.</p> <h2>Virion properties</h2> <h3>Morphology</h3> <p class="para">The virion is a flexuous filament, about 2000 nm long and 23 nm wide (Figures 1, 3). It consists of a cylindrical 3.1 nm thick envelope which encases an inner core consisting of DNA and DNA-binding proteins. Each end of the virion is tapered and carries short filaments; their number is either three or six, dependent on the species.</p> <h3>Physicochemical and physical properties</h3> <p class="para">The buoyant density of the virions is about 1.3 g cm<sup>&minus;3</sup>. Short treatment with detergents removes the terminal structures and the envelope and uncovers a filament about 17 nm in width. The cylindrical envelope contains small globular subunits arranged in a helical formation. The envelope encases an inner core with two parallel rows, producing a zigzag pattern, which is likely to be the projection of a double row of nucleosome-like particles (Figure 3). The linear dsDNA appears to wrap around the nucleosome-like particles.</p> <h3>Nucleic acid</h3> <p class="para">The genome is linear dsDNA, varying is size from 36.895 to 41.050 kbp. The termini of the two strands are not covalently linked, and are strongly associated with protein(s).</p> <h3>Proteins</h3> <p class="para">The virion carries two major proteins, of about 17.0&ndash;18.5 and 22.5&ndash;25.0 kDa, in equal amounts, which are involved in formation of the virion core. Among six minor proteins with molecular masses of in the range of 8.0&ndash;19.0 and 30.5 kDa; four are conserved in all known species and two are exclusive to only two viruses.</p> <h3>Lipids</h3> <p class="para">In the virion, presumably in the envelope, modified host lipids were detected.</p> <h3>Carbohydrates</h3> <p class="para">No information available.</p> <h2>Genome organization and replication</h2> <p class="para">The genomes of different species reveal a high level of conservation in both gene content and gene order over large regions (Figure 4). Other shared features of the genomes are: (i) large inverted terminal repeats exhibiting conserved, regularly spaced direct repeats; (ii) a highly conserved operon encoding the two major structural proteins; and (iii) multiple overlapping ORFs which may be indicative of gene recoding. A few predicted gene products of each species, in addition to the structural proteins, could be assigned functions, including a putative helicase, a nuclease, a protein phosphatase, glycosyltransferase and transcription regulators. No information is available on DNA replication.</p> <h2>Antigenic properties</h2> <p class="para">No information available.</p> <h2>Biological properties</h2> <p class="para">The host range is restricted to hyperthermophilic archaea from the genera <i>Sulfolobus</i> and <i>Acidianus</i>. The virus genome does not integrate into the host chromosome. Host cell lysis was not observed. A population of infected host cells continuously produces the virus. Details of virus&ndash;host interactions are not known.</p> <h2>List of species demarcation criteria in the genus</h2> <p class="para">Species in the genus differ in the length and the terminal structure of the virion, the size and nucleotide sequence of the genomes and their host range.</p> <h2>List of species in the genus <i>Betalipothrixvirus</i></h2> <p class="para">&nbsp;</p> <table border="1" cellspacing="0" cellpadding="0" style="border:none;"> <tbody> <tr> <td valign="top" style="border:1pt solid windowtext;"> <p>Acidianus <i>filamentous virus 3</i></p> </td> <td valign="top"> <p>&nbsp;</p> </td> <td valign="top"> <p>&nbsp;</p> </td> </tr> <tr> <td valign="top"> <p>&nbsp;Acidianus filamentous virus 3</p> </td> <td valign="top"> <p>[AM087120]</p> </td> <td valign="top"> <p>(AFV-3)</p> </td> </tr> <tr> <td valign="top"> <p>Acidianus <i>filamentous virus 6</i></p> </td> <td valign="top"> <p>&nbsp;</p> </td> <td valign="top"> <p>&nbsp;</p> </td> </tr> <tr> <td valign="top"> <p>&nbsp;Acidianus filamentous virus 6</p> </td> <td valign="top"> <p>[AM087121]</p> </td> <td valign="top"> <p>(AFV-6)</p> </td> </tr> <tr> <td valign="top"> <p>Acidianus <i>filamentous virus 7</i></p> </td> <td valign="top"> <p>&nbsp;</p> </td> <td valign="top"> <p>&nbsp;</p> </td> </tr> <tr> <td valign="top"> <p>&nbsp;Acidianus filamentous virus 7</p> </td> <td valign="top"> <p>[AM087122]</p> </td> <td valign="top"> <p>(AFV-7)</p> </td> </tr> <tr> <td valign="top"> <p>Acidianus <i>filamentous virus 8</i></p> </td> <td valign="top"> <p>&nbsp;</p> </td> <td valign="top"> <p>&nbsp;</p> </td> </tr> <tr> <td valign="top"> <p>&nbsp;Acidianus filamentous virus 8</p> </td> <td valign="top"> <p>[AM087123]</p> </td> <td valign="top"> <p>(AFV-8)</p> </td> </tr> <tr> <td valign="top"> <p>Acidianus <i>filamentous virus 9</i></p> </td> <td valign="top"> <p>&nbsp;</p> </td> <td valign="top"> <p>&nbsp;</p> </td> </tr> <tr> <td valign="top"> <p>&nbsp;Acidianus filamentous virus 9</p> </td> <td valign="top"> <p>[EU545650]</p> </td> <td valign="top"> <p>(AFV-9)</p> </td> </tr> <tr> <td valign="top"> <p>Sulfolobus <i>islandicus filamentous virus</i></p> </td> <td valign="top"> <p>&nbsp;</p> </td> <td valign="top"> <p>&nbsp;</p> </td> </tr> <tr> <td valign="top"> <p>&nbsp;Sulfolobus islandicus filamentous virus</p> </td> <td valign="top"> <p>[AF440571]</p> </td> <td valign="top"> <p>(SIFV)</p> </td> </tr> </tbody> </table> <p class="Legend">Species names are in italic script; names of isolates are in roman script. Sequence accession numbers [ ] and assigned abbreviations ( ) are also listed.</p> <h2>Other related viruses which may be members of the genus <i>Betalipothrixvirus</i> but have not been approved as species</h2> <p class="para">&nbsp;</p> <table border="1" cellspacing="0" cellpadding="0" style="border:none;"> <tbody> <tr> <td valign="top" style="border:1pt solid windowtext;"> <p>Desulfurolobus ambivalens filamentous virus</p> </td> <td valign="top"> <p>(DAFV)</p> </td> </tr> <tr> <td valign="top"> <p>Thermoproteus tenax virus 2</p> </td> <td valign="top"> <p>(TTV-2)</p> </td> </tr> <tr> <td valign="top"> <p>Thermoproteus tenax virus 3</p> </td> <td valign="top"> <p>(TTV-3)</p> </td> </tr> </tbody> </table> <p class="TableSource">&nbsp;</p> <h1></h1> <h1>Genus <em>Gammalipothrixvirus</em></h1> <p class="UnnumberedList">Type species <b>Acidianus filamentous virus 1</b></p> <h2>Distinguishing features</h2> <p class="para">The virion has distinctive claw-like structures at its termini (Figures 1, 5). The virion is the shortest in the family, and the genome is the smallest and significantly differs in sequence from the genomes of other members of the family. Moreover the genome does not carry long ITRs, as other members of the family.</p> <h2>Virion properties</h2> <h3>Morphology</h3> <p class="para">The filamentous virion is 900 nm long and 24 nm wide (Figures 1, 5). Terminal structures at both ends of the linear virion are identical and resemble claws. They are 20 nm in diameter. Each claw is connected to the virion body by a 60 nm long tapering appendage and a collar (Figure 5). The body of the virion is covered with an envelope about 3.4 nm thick (Figure 6).</p> <h3>Physicochemical and physical properties</h3> <p class="para">The buoyant density is about 1.3 g cm<sup>&minus;3</sup>. The virion envelope is partially degraded by treatment with 0.3% Triton X-100 and completely removed by treatment with 0.1% SDS. Concomitant with the removal of the envelope, the terminal structures are removed. Conformational changes occur in the virion termini at an initial phase of adsorption: the claw-like terminal structures fold and keep the virion tightly attached to the host cell pili.</p> <h3>Nucleic acid</h3> <p class="para">The genome is linear dsDNA of 20.869 kbp. The ends are modified in an unknown manner. The short inverted terminal repeat CG<sub>10</sub> is present at the termini, preceded by about 350-bp-long sequence which contains clusters of short direct repeats of the sequence TTGTT or close variants thereof. The structural organisation resembles the telomeric ends of linear eukaryotic chromosomes.</p> <h3>Proteins</h3> <p class="para">The virion carries two major proteins P132 and P140, and several minor proteins. They bind DNA and form filaments when incubated with linear dsDNA. A C-terminal domain is identified in their crystal structure with a four-helix-bundle fold. In the topological model, the genomic dsDNA superhelix wraps around P132 basic core, and the P140 basic N-terminus binds genomic DNA, while its lipophilic C-terminal domain is embedded in the lipidic outer shell (Figure 6). The four-helix bundle fold of P132 and P140 is identical to that of the coat protein of the members of the family <i>Rudiviridae.</i></p> <h3>Lipids</h3> <p class="para">In the virion, presumably in the envelope, modified host lipids were detected.</p> <h3>Carbohydrates</h3> <p class="para">No information available.</p> <h2>Genome organization and replication</h2> <p class="para">From 40 putative genes, seven have homologs in betalipothrixviruses and rudiviruses (Figure 7). Three of these, ORFs 135, 426 and 223, are ordered similarly to their respective homologs on the genomes of the rudiviruses SIRV1 and SIRV2.</p> <h2>Antigenic properties</h2> <p class="para">No information available.</p> <h2>Biological properties</h2> <p class="para">The host range is restricted to hyperthermophilic archaea of the genus <i>Acidianus</i>. Virions adsorb to the pili of the host cell, their adsorption to cell surface was never observed. The unusual termini of the virion appear to have a special function in the process of adsorption: the claw folds and keeps the virion firmly attached to a pilus.</p> <p class="para-ind">During a cycle of productive infection neither formation of any significant amounts of cell debris, nor decrease in cell density were observed. Latent period is about 4 h. Infected host cell culture was not cured of the virus after several successive transfers into fresh medium and prolonged, continuous growth. Integration of viral genome into the host chromosome was not observed.</p> <h2>List of species demarcation criteria in the genus</h2> <p class="para">Not applicable.</p> <h2>List of species in the genus <i>Gammalipothrixvirus</i></h2> <p class="para">&nbsp;</p> <table border="1" cellspacing="0" cellpadding="0" style="border:none;"> <tbody> <tr> <td valign="top" style="border:1pt solid windowtext;"> <p><i>Acidianus filamentous virus 1</i></p> </td> <td valign="top"> <p>&nbsp;</p> </td> <td valign="top"> <p>&nbsp;</p> </td> </tr> <tr> <td valign="top"> <p>Acidianus filamentous virus 1</p> </td> <td valign="top"> <p>[AJ567472]</p> </td> <td valign="top"> <p>(AFV-1)</p> </td> </tr> </tbody> </table> <p class="Legend">Species names are in italic script; names of isolates are in roman script. Sequence accession numbers [ ] and assigned abbreviations ( ) are also listed.</p> <h2>Other related viruses which may be members of the genus <i>Gammalipothrixvirus</i> but have not been approved as species</h2> <p class="para">None reported.</p> <h1>Genus <em>Deltalipothrixvirus</em></h1> <p class="UnnumberedList">Type species <b>Acidianus filamentous virus 2</b></p> <h2>Distinguishing features</h2> <p class="para">The virion carries exceptional structures at the termini, not observed in the virions of other members of the family. Moreover, the virion core does not exhibit any regular structure on its surface and, thereby, differs from both the nucleoprotein complex of the alphalipothrixvirus TTV1 and the nucleosome-like arrangement of the betalipothrixvirus virion cores.</p> <h2>Virion properties</h2> <h3>Morphology</h3> <p class="para">The virion is a flexuous filament, about 1100 nm in length and 24 nm in width (Figures 1, 8). It is enveloped with a 3&ndash;4 nm thick envelope. At the two ends of the virion identical structures are present, constituting a complex collar with two sets of filaments, resembling a bottle brush with a solid cap 17 nm in diameter on its top (Figure 8).</p> <h3>Physicochemical and physical properties</h3> <p class="para">The buoyant density of the virions is about 1.3 g cm<sup>&minus;3</sup>. Short treatment with detergents removes the envelope and uncovers a thinner filament about 17 nm in width.</p> <h3>Nucleic acid</h3> <p class="para">The genome is linear dsDNA of 31.787 kbp. No information is available on modification of the ends of the molecule.</p> <h3>Proteins</h3> <p class="para">The virion carries seven proteins with apparent molecular masses of 65, 50, 45, 40, 35, 26 and 6 kDa.</p> <h3>Lipids</h3> <p class="para">Lipids could not be detected.</p> <h3>Carbohydrates</h3> <p class="para">None reported.</p> <h2>Genome organization and replication</h2> <p class="para">From 34 putative genes, eight have homologs in betalipotrixviruses and rudiviruses. The genome contains an unusual 1.008 kbp region close to the centre, which carries two large 46-bp direct repeats and multiple imperfect short repeats throughout the region (Figure 9). Its base composition is strongly biased, with one DNA strand containing only 7% guanosines. The region is bordered by short inverted repeats and may constitute a replication initiation site. In the central part of the genome is present also a tRNA<sup>Lys</sup> gene, and it contains a 12-bp archaeal intron. No information is available on genome replication.</p> <h2>Antigenic properties</h2> <p class="para">No information available.</p> <h2>Biological properties</h2> <p class="para">The host range is restricted to hyperthermophilic archaea of the genus <i>Acidianus</i>. The virus host is devoid of pilus-like structures and virions attach directly to the cell surface. The terminal structures of the virion appear to be involved in adsorption. No conformational changes could be detected in these structures upon adsorption.</p> <p class="para-ind">During a cycle of productive infection neither formation of any significant amounts of cell debris, nor decrease in cell density was observed. Infected host cell culture was not cured of the virus after several successive transfers into fresh medium and prolonged, continuous cultivation. Integration of the viral genome into the host chromosome was not observed.</p> <h2>List of species demarcation criteria in the genus</h2> <p class="para">Not applicable.</p> <h1></h1> <h2>List of species in the genus <i>Deltalipothrixvirus</i></h2> <p class="para">&nbsp;</p> <table border="1" cellspacing="0" cellpadding="0" style="border:none;"> <tbody> <tr> <td valign="top" style="border:1pt solid windowtext;"> <p><i>Acidianus filamentous virus 2</i></p> </td> <td valign="top"> <p>&nbsp;</p> </td> <td valign="top"> <p>&nbsp;</p> </td> </tr> <tr> <td valign="top"> <p>&nbsp;Acidianus filamentous virus 2</p> </td> <td valign="top"> <p>[AJ854042]</p> </td> <td valign="top"> <p>(AFV-2)</p> </td> </tr> </tbody> </table> <p class="Legend">Species names are in italic script; names of isolates are in roman script. Sequence accession numbers [ ] and assigned abbreviations ( ) are also listed.</p> <h2>Other related viruses which may be members of the genus <i>Deltalipothrixvirus</i> but have not been approved as species</h2> <p class="para">Not applicable.</p> <h2>List of unassigned species in the family <i>Lipothrixviridae</i></h2> <p class="para">None reported.</p> <h2>Phylogenetic relationships within the family</h2> <p class="para">The alphalipothrixvirus does not share any homologous gene with the members of the three other genera. There is limited similarity in gene content between beta-, gamma- and deltalipothrixviruses, and only a few ORFs are highly conserved in all of them. A dendrogram constructed by alignment of the sequence of ORF235 of the betalipothrixviruses and its homologs in the gamma- and deltalipothrixviruses reflects relationships within the family (Figure 10).</p> <h2>Similarity with other taxa</h2> <p class="para">Originally, the two families of dsDNA viruses with linear genomes, the <i>Rudiviridae</i> and the <i>Lipothrixviridae</i>, were distinguished by differences in virion structure and this was later supported by comparative genomics. Nevertheless, a substantial fraction of orthologous genes, including some encoding glycosyl transferases and transcriptional regulators, are shared by the rudiviruses and lipothrixviruses. For example, of the 45 predicted genes of the rudivirus Sulfolobus islandicus rod-shaped virus 1, nine share orthologs with the lipothrixvirus Sulfolobus islandicus filamentous virus. Moreover, the structure of the major virion protein of the rudiviruses turned out to be identical to the structures of the two major virion proteins of the lipothrixvirus Acidianus filamentous virus 1. These observations indicate that the known linear dsDNA viruses, all of which infect hyperthermopilic members of the domain Archaea, share a common ancestor. One can suggest a sequence of evolutionary events in which the major virion protein of a &ldquo;simpler&rdquo; non-enveloped virion of the <i>Rudiviridae</i> has been duplicated and evolved so as to facilitate interactions with a hydrophobic envelope, producing the more complex virion of the <i>Lipothrixviridae</i>. Therefore, it has been suggested that the two the families <i>Rudiviridae</i> and <i>Lipothrixviridae</i> should be placed into a new order.</p> <h2>Derivation of names</h2> <p class="UnnumberedList"><i>Lipo</i>: from Greek <i>lipos</i>, &ldquo;fat&rdquo;.</p> <p class="UnnumberedList"><i>Thrix</i>: from Greek <i>thrix</i>, &ldquo;hair&rdquo;.</p> <h2>Further reading</h2> <p class="Refs">Arnold, H.P., Zillig, W., Ziese, U., Holz, I., Crosby, M., Utterback, T., Weidmann, J.F., Kristjanson, J.K., Klenk, H.P., Nelson, K.E. and Fraser, C.M. (2000). A novel lipothrixvirus, SIFV, of the extremely thermophilic crenarchaeon <i>Sulfolobus</i>. <i>Virology</i>, <b>267</b>, 252-266.</p> <p class="Refs">Bettstetter, M., Peng, X., Rachel, R., Garrett, R.A. and Prangishvili, D. (2003). AFV1, a novel virus of the hyperthermophilic crenarchaeon <i>Acidianus</i>. <i>Virology</i>, <b>315</b>, 68-79.</p> <p class="Refs">Bize, A., Peng, X., Prokofeva, M., MacLellan, K., Lucas, S., Forterre, P., Garrett, R.A., Bonch-Osmolovskaya, E.A. and Prangishvili, D. (2008). Viruses in acidic geothermal environments of the Kamchatka Peninsula. <i>Res. Microbiol.</i>, <b>159</b>, 358-366.</p> <p class="Refs">Goulet, A., Blangy, S., Redder, P., Prangishvili, D., Felisberto-Rodriguesa, C., Forterre, P. Campanacci, V. and Cambillau, C. (2009). <i>Acidianus </i>filamentous virus 1 coat proteins display a helical fold spanning the filamentous archaeal viruses lineage. <i>Proc. Natl Acad. Sci. USA</i>,<i> </i><b>106</b>, 21155-21160.</p> <p class="Refs">H&auml;ring M., Rachel, R., Vestergaard, G., Br&uuml;gger, K., Rachel, R., Garrett, R.A. and<strong> Prangishvili (2005).</strong><b> </b>Structure and genome organisation of AFV2, a novel archaeal virus with unusual terminal and core structures. <em>J. Bacteriol.,</em> <b>187</b>, 3855-3858.</p> <p class="Refs">Janekovic, D., Wunderl, S., Holz, I., Zillig, W., Gierl, A. and Neumann, H. (1983). TTV1, TTV3 and TTV3, a family of viruses of the extremely thermophilic, acidophilic sulfur-reducing archaeobacterium Thermoproteus tenax. <i>Mol. Gen. Genet</i>., <b>192</b>, 39-45.</p> <p class="Refs">Prangishvili, D., Forterre, P. and Garrett, R.A. (2006). Viruses of the Archaea: a unifying view. <i>Nat. Rev. Microbiol.</i>,<i> </i><b>4</b>, 837-848.</p> <p class="Refs">Prangishvili, D., Garrett, R.A. and Koonin, E.V. (2006). Evolutionary genomics of archaeal viruses: Unique viral genomes in the third domain of life. <i>Virus Res</i>., <b>117</b>, 52-67.</p> <p class="Refs">Vestergaard, G., Aramayo, R., Basta, T., H&auml;ring, M., Peng, X., Br&uuml;gger, K., Chen, L., Rachel, R., Biosset, N., Garrett, R.A. and Prangishvili, D. (2008). Structure of the <i>Acidianus</i> Filamentous Virus 3 and comparative genomics of related archaeal lipothrixviruses. <i>J. Virol.</i>, <b>82</b>, 371-381.</p> <p class="Refs">Zillig, W., Prangishvili, D., Schleper, C., Elferink, M., Holz, I., Albers, S., Janekovic, D. and G&ouml;tz, D. (1996). Viruses, plasmids and other genetic elements of thermophilic and hyperthermophilic Archaea. <i>FEMS Microbiol. Rev</i>., <b>18</b>, 225-236.</p> <h2>Contributed by</h2> <p class="para">Prangishvili, D.</p> <p class="para"></p> </div> </div> </div> </div> <div class="col-lg-6 col-md-6 col-12 col-9right"> <div class="_none bs-pl-1 bs-pt-4 clearfix block block-layout-builder block-field-blocknodereport-9thfield-mt-srv-subheader-body"> <h2 class="title">Figures</h2> <div class="content"> <div class="clearfix text-formatted field field--name-field-mt-srv-subheader-body field--type-text-with-summary field--label-hidden field__item"><p><b>Figure 1&nbsp;</b>Negative contrast electron micrographs of virions of representatives of four genera of the family&nbsp;<i>Lipothrixviridae</i>. (Top, left) Thermoproteus tenax virus 1 from the genus&nbsp;<i>Alphalipothrixvirus</i>; (center; left) Sulfolobus islandicus filamentous virus from the genus&nbsp;<i>Betalipothrixvirus</i>; (top, right) Acidianus filamentous virus 1 from the genus&nbsp;<i>Gammalipothrixvirus</i>; (bottom) Acidianus filamentous virus 2 from the genus&nbsp;<i>Deltalipothrixvirus</i>. The bars represent 100 nm.</p> <p>(Modified from Arnold&nbsp;<i>et al</i>., 2000; Bettstetter&nbsp;<i>et al</i>., 2003, Hring&nbsp;<i>et al</i>., 2005; Vestergaard&nbsp;<i>et al</i>. 2008.)</p> <p><img alt=" " border="0" src="/sites/default/files/inline-images/f20-01-9780123846846.png"></p> <p><b>Figure 2&nbsp;</b>Negative contrast electron micrograph of intact and partially deteriorated virions of Thermoproteus tenax virus 1, exhibiting the envelope and the core. The bar represents 100 nm.</p> <p><img alt=" " border="0" src="/sites/default/files/inline-images/f20-02-9780123846846.png"></p> <p><b>Figure 3&nbsp;</b>(Top) Negative contrast electron micrograph of AFV3 virion. The bar represents 100 nm. (Middle row) Image processing of AFV3 virion: (left) average 2D map computed from a set of the negatively stained sample, and (right) average 2D map computed from a set of images taken from cryo-EM micrographs; the contrast is inverted. The bars represent 5 nm. (Bottom) Schematic model of the virion of the Acidianus filamentous virus 3.</p> <p><img alt=" " border="0" src="/sites/default/files/inline-images/f20-03-9780123846846.png"></p> <p><b>Figure 4&nbsp;</b>Genome maps aligned for the betalipothrixviruses, showing the relative size, location and orientation of the predicted genes. Homologous genes are coded with identical colors. Homologous operons carrying three or more genes are displayed as a consecutive set of genes with the same color. White boxes indicate that no homologous genes were detected in the other genomes. The ORFs of AFV-3 are labelled according to their amino acid lengths. Predicted protein functions are shown as follows: hc, helicase; gt, glycosyltransferase; mt, SAM-dependent methyltransferase; nc, nuclease; pp, protein phosphatase; sp, structural protein; and tr, transcriptional regulator.</p> <p><img alt=" " border="0" src="/sites/default/files/inline-images/f20-04-9780123846846.png"></p> <p><b>Figure 5&nbsp;</b>Schematic model of the virion of the Acidianus filamentous virus 1.</p> <p><img alt=" " border="0" src="/sites/default/files/inline-images/f20-05-9780123846846.png"></p> <p><b>Figure 6&nbsp;</b>Topological model of the virion of Acidianus filamentous virus 1, indicating location of the two major structural proteins, P132 and P140. The P132 patch is represented by the blue surface in the center. The dsDNA backbone is orange and the P140 is represented by the grey surface. P140 contacts both the lipid-containing outer shell (in green) and the genomic DNA.</p> <p><img alt=" " border="0" src="/sites/default/files/inline-images/f20-06-9780123846846.png"></p> <p>(From Goulet&nbsp;<i>et al</i>., 2009.)</p> <p><b>Figure 7&nbsp;</b>Genome map of Acidianus filamentous virus 1, showing relative size, location, and orientations of the predicted genes. ORFs with significant sequence similarities to ORFs in other viruses are shaded and labeled.</p> <p>(From Bettstetter&nbsp;<i>et al</i>., 2003.)</p> <p><img alt=" " border="0" src="/sites/default/files/inline-images/f20-07-9780123846846.png"></p> <p><b>Figure 8&nbsp;</b>Schematic model of the virion of the Acidianus filamentous virus 2.</p> <p><img alt=" " border="0" src="/sites/default/files/inline-images/f20-08-9780123846846.png"></p> <p><b>Figure 9&nbsp;</b>Genome map of Acidianus filamentous virus 2, showing relative size and location of the predicted genes. Genes are expressed from left to right in the upper row and from right to left in the lower row. ORFs shared with the beta- and gammalipothrixviruses, and with the rudiviruses, are represented by filled rectangles.</p> <p><img alt=" " border="0" src="/sites/default/files/inline-images/f20-09-9780123846846.png"></p> <p><b>Figure 10&nbsp;</b>Dendrogram for genera&nbsp;<i>Betalipothrixvirus</i>,&nbsp;<i>Gammalipothrixvirus</i>, and&nbsp;<i>Deltalipothrixvirus</i>, derived from comparison of sequences of the only well-conserved putative gene shared by all members of the genera.</p> <p>(Modified from Vestergaard&nbsp;<i>et al</i>., 2008.)</p> <p><img alt=" " border="0" src="/sites/default/files/inline-images/f20-10-9780123846846.png"></p></div> </div> </div> </div> </div> </div></div> </div> </div> </article> </div> </div> </section> </div> </div> </div> </div> <div class="footers-container"> <div id="subfooter" class="clearfix subfooter region--shade-background region--no-separator region--no-block-paddings region--no-paddings"> <div class="container-fluid"> <div class="clearfix 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