Structure of the acidianus filamentous virus 3 and comparative genomics of related archaeal lipothrixviruses

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Structure of the acidianus filamentous virus 3 and comparative genomics of related archaeal lipothrixviruses. / Vestergaard, Gisle Alberg; Aramayo, Ricardo; Basta, Tamara; Häring, Monika; Peng, Xu; Brügger, Kim; Chen, Lanming; Rachel, Reinhard; Boisset, Nicolas; Garrett, Roger Antony; Prangishvili, David.

I: Journal of Virology, Bind 82, Nr. 1, 2008, s. 371-381.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Vestergaard, GA, Aramayo, R, Basta, T, Häring, M, Peng, X, Brügger, K, Chen, L, Rachel, R, Boisset, N, Garrett, RA & Prangishvili, D 2008, 'Structure of the acidianus filamentous virus 3 and comparative genomics of related archaeal lipothrixviruses', Journal of Virology, bind 82, nr. 1, s. 371-381. https://doi.org/10.1128/JVI.01410-07

APA

Vestergaard, G. A., Aramayo, R., Basta, T., Häring, M., Peng, X., Brügger, K., Chen, L., Rachel, R., Boisset, N., Garrett, R. A., & Prangishvili, D. (2008). Structure of the acidianus filamentous virus 3 and comparative genomics of related archaeal lipothrixviruses. Journal of Virology, 82(1), 371-381. https://doi.org/10.1128/JVI.01410-07

Vancouver

Vestergaard GA, Aramayo R, Basta T, Häring M, Peng X, Brügger K o.a. Structure of the acidianus filamentous virus 3 and comparative genomics of related archaeal lipothrixviruses. Journal of Virology. 2008;82(1):371-381. https://doi.org/10.1128/JVI.01410-07

Author

Vestergaard, Gisle Alberg ; Aramayo, Ricardo ; Basta, Tamara ; Häring, Monika ; Peng, Xu ; Brügger, Kim ; Chen, Lanming ; Rachel, Reinhard ; Boisset, Nicolas ; Garrett, Roger Antony ; Prangishvili, David. / Structure of the acidianus filamentous virus 3 and comparative genomics of related archaeal lipothrixviruses. I: Journal of Virology. 2008 ; Bind 82, Nr. 1. s. 371-381.

Bibtex

@article{4f8c5a80db3911dd9473000ea68e967b,
title = "Structure of the acidianus filamentous virus 3 and comparative genomics of related archaeal lipothrixviruses",
abstract = "Four novel filamentous viruses with double-stranded DNA genomes, namely, Acidianus filamentous virus 3 (AFV3), AFV6, AFV7, and AFV8, have been characterized from the hyperthermophilic archaeal genus Acidianus, and they are assigned to the Betalipothrixvirus genus of the family Lipothrixviridae. The structures of the approximately 2-mum-long virions are similar, and one of them, AFV3, was studied in detail. It consists of a cylindrical envelope containing globular subunits arranged in a helical formation that is unique for any known double-stranded DNA virus. The envelope is 3.1 nm thick and encases an inner core with two parallel rows of protein subunits arranged like a zipper. Each end of the virion is tapered and carries three short filaments. Two major structural proteins were identified as being common to all betalipothrixviruses. The viral genomes were sequenced and analyzed, and they reveal a high level of conservation in both gene content and gene order over large regions, with this similarity extending partly to the earlier described betalipothrixvirus Sulfolobus islandicus filamentous virus. A few predicted gene products of each virus, in addition to the structural proteins, could be assigned specific functions, including a putative helicase involved in Holliday junction branch migration, a nuclease, a protein phosphatase, transcriptional regulators, and glycosyltransferases. The AFV7 genome appears to have undergone intergenomic recombination with a large section of an AFV2-like viral genome, apparently resulting in phenotypic changes, as revealed by the presence of AFV2-like termini in the AFV7 virions. Shared features of the genomes include (i) large inverted terminal repeats exhibiting conserved, regularly spaced direct repeats; (ii) a highly conserved operon encoding the two major structural proteins; (iii) multiple overlapping open reading frames, which may be indicative of gene recoding; (iv) putative 12-bp genetic elements; and (v) partial gene sequences corresponding closely to spacer sequences of chromosomal repeat clusters.",
author = "Vestergaard, {Gisle Alberg} and Ricardo Aramayo and Tamara Basta and Monika H{\"a}ring and Xu Peng and Kim Br{\"u}gger and Lanming Chen and Reinhard Rachel and Nicolas Boisset and Garrett, {Roger Antony} and David Prangishvili",
note = "Keywords: Acidianus; Conserved Sequence; Cryoelectron Microscopy; Gene Order; Genome, Viral; Lipothrixviridae; Microscopy, Electron, Transmission; Molecular Sequence Data; Operon; Sequence Analysis, DNA; Terminal Repeat Sequences; Viral Nonstructural Proteins; Viral Structural Proteins; Virion",
year = "2008",
doi = "10.1128/JVI.01410-07",
language = "English",
volume = "82",
pages = "371--381",
journal = "Journal of Virology",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "1",

}

RIS

TY - JOUR

T1 - Structure of the acidianus filamentous virus 3 and comparative genomics of related archaeal lipothrixviruses

AU - Vestergaard, Gisle Alberg

AU - Aramayo, Ricardo

AU - Basta, Tamara

AU - Häring, Monika

AU - Peng, Xu

AU - Brügger, Kim

AU - Chen, Lanming

AU - Rachel, Reinhard

AU - Boisset, Nicolas

AU - Garrett, Roger Antony

AU - Prangishvili, David

N1 - Keywords: Acidianus; Conserved Sequence; Cryoelectron Microscopy; Gene Order; Genome, Viral; Lipothrixviridae; Microscopy, Electron, Transmission; Molecular Sequence Data; Operon; Sequence Analysis, DNA; Terminal Repeat Sequences; Viral Nonstructural Proteins; Viral Structural Proteins; Virion

PY - 2008

Y1 - 2008

N2 - Four novel filamentous viruses with double-stranded DNA genomes, namely, Acidianus filamentous virus 3 (AFV3), AFV6, AFV7, and AFV8, have been characterized from the hyperthermophilic archaeal genus Acidianus, and they are assigned to the Betalipothrixvirus genus of the family Lipothrixviridae. The structures of the approximately 2-mum-long virions are similar, and one of them, AFV3, was studied in detail. It consists of a cylindrical envelope containing globular subunits arranged in a helical formation that is unique for any known double-stranded DNA virus. The envelope is 3.1 nm thick and encases an inner core with two parallel rows of protein subunits arranged like a zipper. Each end of the virion is tapered and carries three short filaments. Two major structural proteins were identified as being common to all betalipothrixviruses. The viral genomes were sequenced and analyzed, and they reveal a high level of conservation in both gene content and gene order over large regions, with this similarity extending partly to the earlier described betalipothrixvirus Sulfolobus islandicus filamentous virus. A few predicted gene products of each virus, in addition to the structural proteins, could be assigned specific functions, including a putative helicase involved in Holliday junction branch migration, a nuclease, a protein phosphatase, transcriptional regulators, and glycosyltransferases. The AFV7 genome appears to have undergone intergenomic recombination with a large section of an AFV2-like viral genome, apparently resulting in phenotypic changes, as revealed by the presence of AFV2-like termini in the AFV7 virions. Shared features of the genomes include (i) large inverted terminal repeats exhibiting conserved, regularly spaced direct repeats; (ii) a highly conserved operon encoding the two major structural proteins; (iii) multiple overlapping open reading frames, which may be indicative of gene recoding; (iv) putative 12-bp genetic elements; and (v) partial gene sequences corresponding closely to spacer sequences of chromosomal repeat clusters.

AB - Four novel filamentous viruses with double-stranded DNA genomes, namely, Acidianus filamentous virus 3 (AFV3), AFV6, AFV7, and AFV8, have been characterized from the hyperthermophilic archaeal genus Acidianus, and they are assigned to the Betalipothrixvirus genus of the family Lipothrixviridae. The structures of the approximately 2-mum-long virions are similar, and one of them, AFV3, was studied in detail. It consists of a cylindrical envelope containing globular subunits arranged in a helical formation that is unique for any known double-stranded DNA virus. The envelope is 3.1 nm thick and encases an inner core with two parallel rows of protein subunits arranged like a zipper. Each end of the virion is tapered and carries three short filaments. Two major structural proteins were identified as being common to all betalipothrixviruses. The viral genomes were sequenced and analyzed, and they reveal a high level of conservation in both gene content and gene order over large regions, with this similarity extending partly to the earlier described betalipothrixvirus Sulfolobus islandicus filamentous virus. A few predicted gene products of each virus, in addition to the structural proteins, could be assigned specific functions, including a putative helicase involved in Holliday junction branch migration, a nuclease, a protein phosphatase, transcriptional regulators, and glycosyltransferases. The AFV7 genome appears to have undergone intergenomic recombination with a large section of an AFV2-like viral genome, apparently resulting in phenotypic changes, as revealed by the presence of AFV2-like termini in the AFV7 virions. Shared features of the genomes include (i) large inverted terminal repeats exhibiting conserved, regularly spaced direct repeats; (ii) a highly conserved operon encoding the two major structural proteins; (iii) multiple overlapping open reading frames, which may be indicative of gene recoding; (iv) putative 12-bp genetic elements; and (v) partial gene sequences corresponding closely to spacer sequences of chromosomal repeat clusters.

U2 - 10.1128/JVI.01410-07

DO - 10.1128/JVI.01410-07

M3 - Journal article

C2 - 17942536

VL - 82

SP - 371

EP - 381

JO - Journal of Virology

JF - Journal of Virology

SN - 0022-538X

IS - 1

ER -

ID: 9513323