SH1: A novel, spherical halovirus isolated from an Australian hypersaline lake

Porter, Kate; Kukkaro, Petra; Bamford, Jaana K. H.; Bath, Carolyn; Kivelä, Hanna M.; Dyall‐Smith, Mike; Bamford, Dennis H.

doi:10.1016/j.virol.2005.01.043

Cited by 113 publications

(141 citation statements)

References 37 publications

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“…It is highly likely that identification and characterization of archaeal viruses will provide additional examples of viral evolutionary relationships that span all the domains of life. Indeed, preliminary characterization of SH1, a spherical halovirus, suggests that this virus too may be related to this lineage (39).…”

Section: Discussionmentioning

confidence: 99%

Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses

Khayat

Tang

Larson

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

163

181

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Archaea and their viruses are poorly understood when compared with the Eukarya and Bacteria domains of life. We report here the crystal structure of the major capsid protein (MCP) of the Sulfolobus turreted icosahedral virus, an archaeal virus isolated from an acidic hot spring (pH 2-4, 72-92°C) in Yellowstone National Park. The structure is nearly identical to the MCP structures of the eukaryotic Paramecium bursaria Chlorella virus, and the bacteriophage PRD1, and shows a common fold with the mammalian adenovirus. Structural analysis of the capsid architecture, determined by fitting the subunit into the electron cryomicroscopy reconstruction of the virus, identified a number of key interactions that are akin to those observed in adenovirus and PRD1. The similar capsid proteins and capsid architectures strongly suggest that these viral capsids originated and evolved from a common ancestor. Hence, this work provides a previously undescribed example of a viral relationship spanning the three domains of life (Eukarya, Bacteria, and Archaea). The MCP structure also provides insights into the stabilizing forces required for extracellular hyperthermophilic proteins to tolerate high-temperature hot springs.crystallography ͉ evolution ͉ hyperthermophile ͉ electron cryomicroscopy T he Sulfolobus turreted icosahedral virus (STIV) infects Sulfolobus solfataricus, an acidophilic hyperthermophilic organism (grows optimally at pH 2-4 and at Ͼ80°C) that is emerging as a model for studying hyperthermophilic archaea and their viruses (1). STIV possesses a 17,663-bp circular dsDNA genome that encodes 36 predicted ORFs (2). The viral particle is composed of a 37-kDa major capsid protein (MCP) and several 25-, 12.5-, and 10-kDa minor capsid proteins (2). The electron cryomicroscopy (cryo-EM) image reconstruction of STIV showed a pseudo T ϭ 31 icosahedral capsid with trimers at the quasi sixfold coordinated positions, turret-like appendages at the vertices, and what appears to be an internal lipid membrane sandwiched between the genome and capsid shell (2). The capsid architecture of STIV is reminiscent of the mammalian adenovirus, bacteriophage PRD1, and Paramecium bursaria Chlorella virus (PBCV-1). The viral capsids of adenovirus, PRD1, and PBCV-1 are believed to have descended from a common ancestor (3). By using sequence alignment and modeling techniques, this lineage was recently extended to include additional large-faceted viruses containing a double-barrel trimeric major coat protein (4).Here we report the crystal structure of the STIV MCP and show its structural homology and sequence similarity to the MCPs of the adenovirus, PRD1, and PBCV-1. We further analyze the capsid architecture of STIV by docking the MCP crystal structure into the cryo-EM reconstruction and calculating a difference map. Our analysis reveals a number of quaternary interactions similar to those observed in adenovirus and PRD1. The structural and sequence comparison between the MCPs of these viruses, and similarities between their capsid architectures su...

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Section: Discussionmentioning

confidence: 99%

Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses

Khayat

Tang

Larson

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

163

181

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“…Alphasphaerolipoviruses display a narrow host range. Besides the common host, H. hispanica ATCC33960 [24], Halorubrum strain CSW 2.09.4 [42] was identified as an alternative host for SH1 and PH1, while SH1 and HHIV-2 could also infect Haloarcula sp. PV7 [5].…”

Section: Genus Alphasphaerolipovirusmentioning

confidence: 99%

“…In 2003, a spherical halovirus, SH1, infecting the euryarchaeon Haloarcula hispanica was isolated from Lake Serpentine in Western Australia [13] and characterized in detail during the next few years [7,23,29,[42][43][44]. The particle morphology and genome structure of this virus resemble those of bacteriophages belonging to the family Tectiviridae [2].…”

Section: Introductionmentioning

confidence: 99%

Gammasphaerolipovirus, a newly proposed bacteriophage genus, unifies viruses of halophilic archaea and thermophilic bacteria within the novel family Sphaerolipoviridae

et al. 2014

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A new family of viruses named Sphaerolipoviridae has been proposed recently. It comprises icosahedral, tailless haloarchaeal viruses with an internal lipid membrane located between the protein capsid and the dsDNA genome. The proposed family Sphaerolipoviridae was divided into two genera: Alphasphaerolipovirus, including Haloarcula hispanica viruses SH1, PH1 and HHIV-2, and Betasphaerolipovirus, including Natrinema virus SNJ1. Here, we propose to expand the family Sphaerolipoviridae to include a group of bacteriophages infecting extreme thermophilic Thermus thermophilus and sharing a number of structural and genomic properties with archaeal sphaerolipoviruses. This new group comprises two members, lytic phage P23-77 and temperate phage IN93, as well as putative members P23-72 and P23-65H. In addition, several related proviruses have been discovered as integrated elements in bacterial genomes of the families Thermus and Meiothermus. Morphology of the virus particles and the overall capsid architecture of these bacteriophages resembles that of archaeal members of the Sphaerolipoviridae, including an unusual capsid arrangement in a T = 28 dextro lattice. Alpha-and betasphaerolipoviruses share with P23-77-like bacteriophages a conserved block of core genes that encode a putative genome-packaging ATPase and the two major capsid proteins (MCPs). The recently determined X-ray structure of the small and large MCPs of P23-77 revealed a single beta-barrel (jelly-roll) fold that is superimposable with the cryo-EM density maps of the SH1 capsomers. Given the common features of these viruses, we propose to include the so far unclassified P23-77-like bacteriophages into a new genus, ''Gammasphaerolipovirus'', within the family Sphaerolipoviridae.

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“…The major capsid protein can sometimes self-assemble into (a part of) the virion (Vestergaard et al 2008). While many archaeal hosts have evolved a highly robust machinery to thrive under harsh conditions, such as extreme temperature, pH and salinity, their virions have co-evolved to adopt equally stable properties (Witte et al 1997;Porter et al 2005;Prangishvili 2006;Pina et al 2011). These remarkable characteristics make archaeal viruses attractive subjects for structural biology research.…”

Section: Introductionmentioning

confidence: 99%

Structure and assembly mechanism of virus-associated pyramids

Quax

Daum

2017

Biophys Rev

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Viruses have developed intricate molecular machines to infect, replicate within and escape from their host cells. Perhaps one of the most intriguing of these mechanisms is the pyramidal egress structure that has evolved in archaeal viruses, such as SIRV2 or STIV1. The structure and mechanism of these virus-associated pyramids (VAPs) has been studied by cryo-electron tomography and complementary biochemical techniques, revealing that VAPs are formed by multiple copies of a virus-encoded 10-kDa protein (PVAP) that integrate into the cell membrane and assemble into hollow, sevenfold symmetric pyramids. In this process, growing VAPs puncture the protective surface layer and ultimately open to release newly replicated viral particles into the surrounding medium. PVAP has the striking capability to spontaneously integrate and self-assemble into VAPs in biological membranes of the archaea, bacteria and eukaryotes. This renders the VAP a universal membrane remodelling system. In this review, we provide an overview of the VAP structure and assembly mechanism and discuss the possible use of VAPs in nanobiotechnology.

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SH1: A novel, spherical halovirus isolated from an Australian hypersaline lake

Cited by 113 publications

References 37 publications

Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses

Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses

Gammasphaerolipovirus, a newly proposed bacteriophage genus, unifies viruses of halophilic archaea and thermophilic bacteria within the novel family Sphaerolipoviridae

Structure and assembly mechanism of virus-associated pyramids

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