Insights into a Viral Lytic Pathway from an Archaeal Virus-Host System

Snyder, Jamie C.; Brumfield, Susan K.; Kerchner, Keshia M.; Quax, Tessa E. F.; Prangishvili, David; Young, Mark

doi:10.1128/jvi.02956-12

Cited by 22 publications

(29 citation statements)

References 25 publications

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“…Perhaps one of the best studied archaeal virus-host systems is the STIV-Sulfolobus model system (Brumfield et al, 2009;Dellas et al, in preparation;Fu and Johnson, 2012;Fu et al, 2010;Khayat et al, 2010Khayat et al, , 2005Larson et al, 2007aLarson et al, , 2007bLarson et al, , 2006Maaty et al, 2006Maaty et al, , 2012Ortmann et al, 2008;Rice et al, 2004;Snyder et al, 2011aSnyder et al, , 2011bSnyder et al, , 2013aSnyder et al, , 2013bVeesler et al, 2013;Wirth et al, 2011). Even though a complete archaeal virus replication cycle has not been solved, several steps of the STIV replication cycle have been described (Brumfield et al, 2009;Dellas et al, in preparation;Fu et al, 2010;Happonen et al, 2013;Snyder et al, 2011bSnyder et al, , 2013b.…”

Section: Archaeal Virus-host Model Systemsmentioning

confidence: 94%

40 Years of archaeal virology: Expanding viral diversity

2015

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The first archaeal virus was isolated over 40 years ago prior to the recognition of the three domain structure of life. In the ensuing years, our knowledge of Archaea and their viruses has increased, but they still remain the most mysterious of life's three domains. Currently, over 100 archaeal viruses have been discovered, but few have been described in biochemical or structural detail. However, those that have been characterized have revealed a new world of structural, biochemical and genetic diversity. Several model systems for studying archaeal virus-host interactions have been developed, revealing evolutionary linkages between viruses infecting the three domains of life, new viral lysis systems, and unusual features of host-virus interactions. It is likely that the study of archaeal viruses will continue to provide fertile ground for fundamental discoveries in virus diversity, structure and function.

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Section: Archaeal Virus-host Model Systemsmentioning

confidence: 94%

40 Years of archaeal virology: Expanding viral diversity

2015

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“…For example, VAP opening may be dependent on the specific growth conditions (temperature and pH). However, it is also possible that the opening mechanism is directly controlled by a factor encoded by the virions themselves, as they are dependent on the precise timing of VAP opening to avoid the release of immature virions Snyder et al 2013a;Daum et al 2014). …”

Section: Vap Assembly and Openingmentioning

confidence: 99%

“…Expression of STIV1-and SIRV2-based PVAP chimeras in the STIV1 infection system showed that both proteins and all chimeras resulted in the formation of VAPs of the same size and geometry (Snyder et al 2013a). However, neither the chimeras nor SIRV2_PVAP were sufficient to support STIV1 infection, suggesting that the two proteins are not completely interchangeable.…”

Section: Vap Diversitymentioning

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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“…Of the predicted 38 open reading frames encoded by STIV (including the more recently identified B129 [8]), 11 have been experimentally investigated through genetic knockout experiments (9), biochemical analysis (2, 10, 11), or structural characterization (5)(6)(7)(12)(13)(14). While certain steps of the STIV infection cycle are under investigation (11,15), much remains to be understood, including the processes of viral attachment and viral DNA packaging.STIV B204 belongs to the FtsK/HerA superfamily (3), whose members share several conserved amino acid sequence motifs. In …”

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confidence: 99%

Structure-Based Mutagenesis of Sulfolobus Turreted Icosahedral Virus B204 Reveals Essential Residues in the Virion-Associated DNA-Packaging ATPase

Dellas

Snyder

Dills

et al. 2016

J Virol

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Sulfolobus turreted icosahedral virus (STIV), an archaeal virus that infects the hyperthermoacidophile Sulfolobus solfataricus, is one of the most well-studied viruses of the domain Archaea. STIV shares structural, morphological, and sequence similarities with viruses from other domains of life, all of which are thought to belong to the same viral lineage. Several of these common features include a conserved coat protein fold, an internal lipid membrane, and a DNA-packaging ATPase. B204 is the ATPase encoded by STIV and is thought to drive packaging of viral DNA during the replication process. Here, we report the crystal structure of B204 along with the biochemical analysis of B204 mutants chosen based on structural information and sequence conservation patterns observed among members of the same viral lineage and the larger FtsK/HerA superfamily to which B204 belongs. Both in vitro ATPase activity assays and transfection assays with mutant forms of B204 confirmed the essentiality of conserved and nonconserved positions. We also have identified two distinct particle morphologies during an STIV infection that differ in the presence or absence of the B204 protein. The biochemical and structural data presented here are not only informative for the STIV replication process but also can be useful in deciphering DNA-packaging mechanisms for other viruses belonging to this lineage. IMPORTANCE STIV is a virus that infects a host from the domainArchaea that replicates in high-temperature, acidic environments. While STIV has many unique features, there exist several striking similarities between this virus and others that replicate in different environments and infect a broad range of hosts from Bacteria and Eukarya. Aside from structural features shared by viruses from this lineage, there exists a significant level of sequence similarity between the ATPase genes carried by these different viruses; this gene encodes an enzyme thought to provide energy that drives DNA packaging into the virion during infection. The experiments described here highlight the elements of this enzyme that are essential for proper function and also provide supporting evidence that B204 is present in the mature STIV virion. In Sulfolobus turreted icosahedral virus (STIV), the open reading frame B204 (previously described as B164) (1, 2) encodes a putative ATPase that is predicted to function as the molecular motor driving viral DNA packaging during infection (3). Interestingly, it has been demonstrated that viruses harboring ATPases homologous to B204 share other common features, such as a spherical morphology, an internal lipid membrane, and a structurally homologous coat protein fold (termed the double ␤-barrel or double jelly roll fold) (4). The structural and functional assessment of viruses belonging to this putative viral lineage can provide insights on viral infection strategies across the three domains of life. In the case of B204, understanding its function has implications for mechanisms by which an ancient molecular motor may h...

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Insights into a Viral Lytic Pathway from an Archaeal Virus-Host System

Cited by 22 publications

References 25 publications

40 Years of archaeal virology: Expanding viral diversity

40 Years of archaeal virology: Expanding viral diversity

Structure and assembly mechanism of virus-associated pyramids

Structure-Based Mutagenesis of Sulfolobus Turreted Icosahedral Virus B204 Reveals Essential Residues in the Virion-Associated DNA-Packaging ATPase

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