The thermo‐ and acido‐stable ORF‐99 from the archaeal virus AFV1

Goulet, Adeline; Spinelli, S.; Blangy, Stéphanie; Tilbeurgh, Herman van; Leulliot, Nicolas; Basta, Tamara; Prangishvili, David; Cambillau, Christian; Campanacci, Valérie

doi:10.1002/pro.122

Cited by 13 publications

(13 citation statements)

References 28 publications

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“…Most of the early expressed genes located on the genome termini have unknown functions. SIRV2_ORF103a and SIRV2_ORF119b have a homolog in Acidianus filamentous virus 1 (AFV1), AFV1_ORF99, of which the crystal structure was determined (43). AFV1_ORF99 displays a completely novel fold from which no function prediction could be derived (43).…”

Section: Discussionmentioning

confidence: 99%

Massive Activation of Archaeal Defense Genes during Viral Infection

Quax

Voet

Sismeiro

et al. 2013

J Virol

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dArchaeal viruses display unusually high genetic and morphological diversity. Studies of these viruses proved to be instrumental for the expansion of knowledge on viral diversity and evolution. The Sulfolobus islandicus rod-shaped virus 2 (SIRV2) is a model to study virus-host interactions in Archaea. It is a lytic virus that exploits a unique egress mechanism based on the formation of remarkable pyramidal structures on the host cell envelope. Using whole-transcriptome sequencing, we present here a global map defining host and viral gene expression during the infection cycle of SIRV2 in its hyperthermophilic host S. islandicus LAL14/1. This information was used, in combination with a yeast two-hybrid analysis of SIRV2 protein interactions, to advance current understanding of viral gene functions. As a consequence of SIRV2 infection, transcription of more than one-third of S. islandicus genes was differentially regulated. While expression of genes involved in cell division decreased, those genes playing a role in antiviral defense were activated on a large scale. Expression of genes belonging to toxin-antitoxin and clustered regularly interspaced short palindromic repeat (CRISPR)-Cas systems was specifically pronounced. The observed different degree of activation of various CRISPR-Cas systems highlights the specialized functions they perform. The information on individual gene expression and activation of antiviral defense systems is expected to aid future studies aimed at detailed understanding of the functions and interplay of these systems in vivo.

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Section: Discussionmentioning

confidence: 99%

Massive Activation of Archaeal Defense Genes during Viral Infection

Quax

Voet

Sismeiro

et al. 2013

J Virol

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“…To date, four protein structures from lipothrixviruses (23)(24)(25)(26) have been determined. To complete structural information about Lipothrixviridae, and in particular to determine the structure of their MCPs, we have studied the Gamma-lipothrixvirus Acidianus filamentous virus 1 (AFV1).…”

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confidence: 99%

Acidianus filamentous virus 1 coat proteins display a helical fold spanning the filamentous archaeal viruses lineage

Goulet

Blangy

Redder

et al. 2009

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

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Acidianus filamentous virus 1 (AFV1), a member of the Lipothrixviridae family, infects the hyperthermophilic, acidophilic crenarchaeaon Acidianus hospitalis. The virion, covered with a lipidic outer shell, is 9,100-Å long and contains a 20.8-kb linear dsDNA genome. We have identified the two major coat proteins of the virion (MCPs; 132 and 140 amino acids). 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 of the virion filament core, the genomic dsDNA superhelix wraps around the AFV1-132 basic protein, and the AFV1-140 basic N terminus binds genomic DNA, while its lipophilic C-terminal domain is imbedded in the lipidic outer shell. The four-helix bundle fold of the MCPs from AFV1 is identical to that of the coat protein (CP) of Sulfolobus islandicus rod-shaped virus (SIRV), a member of the Rudiviridae family. Despite low sequence identity between these proteins, their high degree of structural similarity suggests that they could have derived from a common ancestor and could thus define an yet undescribed viral lineage.crystal structure ͉ viral coat proteins ͉ viral lineages ͉ virus evolution

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“…A tobacco etch virus (TEV) protease cleavage site was inserted between attB1 and the gene of interest. The resulting vector was transformed in Escherichia coli strain Rosetta(DE3)pLysS (Novagen) (18,19). After overnight induction with 1 mM isopropyl 1-thio-␤-D-galactopyranoside at 25°C, the cells were harvested by centrifugation for 10 min at 4,000 ϫ g. The bacterial pellets were resuspended in lysis buffer (50 mM Tris, pH 8, 300 mM NaCl, 10 mM imidazole) supplemented with 0.25 mg/ml lysozyme, 1 g/ml DNase, 20 mM MgSO 4 , and antiproteases (Complete EDTA-free antiproteases; Roche) and were frozen at Ϫ80°C.…”

Section: Methodsmentioning

confidence: 99%

“…Therefore, to get insight into the biology of the Lipothrixviridae, we performed crystallographic studies of the AFV1 proteome. Although the solved structures of AFV1-102 (23) and the homologs AFV1-99 (19) and SIFV-014 (18) have not revealed any structural homologs, they have suggested that the proteins are involved in protein-protein interaction and are minor structural components, respectively.…”

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confidence: 99%

“…Because structures generally are much better conserved than sequences, structural studies have aimed at uncovering functional and evolutionary relationships that are not apparent from the primary sequence. To date, 11 protein structures from crenarchaeal viruses have been reported (18,19,22,23,(25)(26)(27)(28)(29)(30)33). Most of these proteins share structural similarity with proteins of known function: three winged-helix proteins are likely involved in transcriptional regulation (two from the fusellovirus SSV1 [27,33] and one from STIV [28]); one glycosyltransferase from STIV displays the GT-A fold (30); one adaptor protein from SSV1 is similar to the repressor of primer (ROP) of Escherichia coli (26); and the major coat protein of STIV has revealed the first evolutionary relationship spanning the three domains of life (25).…”

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confidence: 99%

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ORF157 from the Archaeal VirusAcidianusFilamentous Virus 1 Defines a New Class of Nuclease

Goulet

Pina

Redder

et al. 2010

J Virol

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Acidianus filamentous virus 1 (AFV1) (Lipothrixviridae) is an enveloped filamentous virus that was characterized from a crenarchaeal host. It infects Acidianus species that thrive in the acidic hot springs (>85°C and pH <3) of Yellowstone National Park, WY. The AFV1 20.8-kb, linear, double-stranded DNA genome encodes 40 putative open reading frames whose sequences generally show little similarity to other genes in the sequence databases. Because three-dimensional structures are more conserved than sequences and hence are more effective at revealing function, we set out to determine protein structures from putative AFV1 open reading frames (ORF). The crystal structure of ORF157 reveals an ␣؉␤ protein with a novel fold that remotely resembles the nucleotidyltransferase topology. In vitro, AFV1-157 displays a nuclease activity on linear doublestranded DNA. Alanine substitution mutations demonstrated that E86 is essential to catalysis. AFV1-157 represents a novel class of nuclease, but its exact role in vivo remains to be determined.

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The thermo‐ and acido‐stable ORF‐99 from the archaeal virus AFV1

Cited by 13 publications

References 28 publications

Massive Activation of Archaeal Defense Genes during Viral Infection

Massive Activation of Archaeal Defense Genes during Viral Infection

Acidianus filamentous virus 1 coat proteins display a helical fold spanning the filamentous archaeal viruses lineage

ORF157 from the Archaeal VirusAcidianusFilamentous Virus 1 Defines a New Class of Nuclease

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