title: A novel rudivirus, ARV1, of the hyperthermophilic archaeal genus Acidianus.
abstract: Virus ARV1, the first member of the family Rudiviridae infecting hyperthermophilic archaea of the genus Acidianus, was isolated from a hot spring in Pozzuoli, Italy. The rod-shaped virions, 610 +/- 50 nm long and 22 +/- 3 nm wide, are non-enveloped and carry a helical nucleoprotein core, with three tail fibers protruding at each end which appear to be involved in adsorption onto the host cell surface. The virions contain two protein components, a major one of 14.4 kDa, which is glycosylated and a minor of about 124 kDa. The linear double-stranded DNA genome yielded 24,655 bp of sequence, including 1365 bp inverted terminal repeats. Coding is on both strands and about 40% of the predicted genes are homologous to those of other hyperthermophilic crenarchaeal viruses, mainly rudiviruses. They include genes encoding the coat protein, two glycosyl transferases and a Holliday junction resolvase. Other assigned functions include a thymidylate synthase and three DNA-binding proteins. The genome sequence and composition differ strongly from those of the Sulfolobus rudiviruses SIRV1 and SIRV2, and the genome stability is very high, with no sequence variants being detected. Although the sequences of the inverted terminal repeats of the three rudiviruses are different, they all carry the motif AATTTAGGAATTTAGGAATTT near the genome ends which may constitute a signal for the Holliday junction resolvase and DNA replication.
authors.affiliation: Danish Archaea Centre, Institute of Molecular Biology, Copenhagen University, Sølvgade 83H, DK-1307 Copenhagen K, Denmark.
authors.forename: Gisle
authors.initials: G
authors.lastname: Vestergaard
authors.forename: Monika
authors.initials: M
authors.lastname: Häring
authors.forename: Xu
authors.initials: X
authors.lastname: Peng
authors.forename: Reinhard
authors.initials: R
authors.lastname: Rachel
authors.forename: Roger A
authors.initials: RA
authors.lastname: Garrett
authors.forename: David
authors.initials: D
authors.lastname: Prangishvili
mesh_terms: D041541:Acidianus / Q000821:virology*; D036022:Capsid Proteins / Q000235:genetics; D004279:DNA, Viral / Q000737:chemistry / Q000235:genetics; D004268:DNA-Binding Proteins / Q000235:genetics; D016695:Glycosyltransferases / Q000235:genetics; D045565:Holliday Junction Resolvases / Q000235:genetics; D045482:Hot Springs / Q000821:virology*; D007558:Italy; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009698:Nucleoproteins / Q000648:ultrastructure; D016366:Open Reading Frames / Q000235:genetics; D023642:Rudiviridae / Q000302:isolation & purification* / Q000648:ultrastructure; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D020079:Terminal Repeat Sequences / Q000235:genetics; D013940:Thymidylate Synthase / Q000235:genetics; D014764:Viral Proteins / Q000032:analysis / Q000302:isolation & purification; D017376:Viral Tail Proteins / Q000648:ultrastructure; D014871:Water Microbiology
chemical_list: D036022:Capsid Proteins; D004279:DNA, Viral; D004268:DNA-Binding Proteins; D009698:Nucleoproteins; D014764:Viral Proteins; D017376:Viral Tail Proteins; D013940:Thymidylate Synthase; D016695:Glycosyltransferases; D045565:Holliday Junction Resolvases