Abstract
Pyrococcus furiosus is a hyperthermophilic archaeal microorganism found near deep-sea thermal vents and its optimal growth temperature of 100 °C. Recently, a 38.8-kDa protein from P. furiosus DSM 3638 was isolated and characterized. Electron microscopy revealed that this protein aggregated as spheres of approximately 30 nm in diameter, which we designated P. furiosus virus-like particles (PfVs). X-ray crystallographic analysis at 3.6-Å resolution revealed that each PfV consisted of 180 copies of the 38.8-kDa protein and retained T = 3 icosahedral symmetry, as is often the case in spherical viruses. The total molecular mass of each particle was approximately 7 MDa. An examination of capsid structures suggested strong evolutionary links among PfV, tailed double-stranded DNA bacteriophages, and herpes viruses. The similar three-dimensional structures of the various coat proteins indicate that these viral capsids might have originated and evolved from a common ancestor. The structure of PfV provides a previously undescribed example of viral relationships across the three domains of life (Eukarya, Bacteria, and Archaea).
| Original language | English |
|---|---|
| Pages (from-to) | 1469-1483 |
| Number of pages | 15 |
| Journal | Journal of Molecular Biology |
| Volume | 368 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - May 18 2007 |
| Externally published | Yes |
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Keywords
- hyperthermophilic Archaea
- PfV (Pyrococcus furiosus virus-like particle)
- Pyrococcus furiosus
- tailed bacteriophage
- X-ray crystallography
ASJC Scopus subject areas
- Virology
Cite this
The Crystal Structure of a Virus-like Particle from the Hyperthermophilic Archaeon Pyrococcus furiosus Provides Insight into the Evolution of Viruses. / Akita, Fusamichi; Chong, Khoon Tee; Tanaka, Hideaki; Yamashita, Eiki; Miyazaki, Naoyuki; Nakaishi, Yuichiro; Suzuki, Mamoru; Namba, Kazunori; Ono, Yasuko; Tsukihara, Tomitake; Nakagawa, Atsushi.
In: Journal of Molecular Biology, Vol. 368, No. 5, 18.05.2007, p. 1469-1483.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The Crystal Structure of a Virus-like Particle from the Hyperthermophilic Archaeon Pyrococcus furiosus Provides Insight into the Evolution of Viruses
AU - Akita, Fusamichi
AU - Chong, Khoon Tee
AU - Tanaka, Hideaki
AU - Yamashita, Eiki
AU - Miyazaki, Naoyuki
AU - Nakaishi, Yuichiro
AU - Suzuki, Mamoru
AU - Namba, Kazunori
AU - Ono, Yasuko
AU - Tsukihara, Tomitake
AU - Nakagawa, Atsushi
PY - 2007/5/18
Y1 - 2007/5/18
N2 - Pyrococcus furiosus is a hyperthermophilic archaeal microorganism found near deep-sea thermal vents and its optimal growth temperature of 100 °C. Recently, a 38.8-kDa protein from P. furiosus DSM 3638 was isolated and characterized. Electron microscopy revealed that this protein aggregated as spheres of approximately 30 nm in diameter, which we designated P. furiosus virus-like particles (PfVs). X-ray crystallographic analysis at 3.6-Å resolution revealed that each PfV consisted of 180 copies of the 38.8-kDa protein and retained T = 3 icosahedral symmetry, as is often the case in spherical viruses. The total molecular mass of each particle was approximately 7 MDa. An examination of capsid structures suggested strong evolutionary links among PfV, tailed double-stranded DNA bacteriophages, and herpes viruses. The similar three-dimensional structures of the various coat proteins indicate that these viral capsids might have originated and evolved from a common ancestor. The structure of PfV provides a previously undescribed example of viral relationships across the three domains of life (Eukarya, Bacteria, and Archaea).
AB - Pyrococcus furiosus is a hyperthermophilic archaeal microorganism found near deep-sea thermal vents and its optimal growth temperature of 100 °C. Recently, a 38.8-kDa protein from P. furiosus DSM 3638 was isolated and characterized. Electron microscopy revealed that this protein aggregated as spheres of approximately 30 nm in diameter, which we designated P. furiosus virus-like particles (PfVs). X-ray crystallographic analysis at 3.6-Å resolution revealed that each PfV consisted of 180 copies of the 38.8-kDa protein and retained T = 3 icosahedral symmetry, as is often the case in spherical viruses. The total molecular mass of each particle was approximately 7 MDa. An examination of capsid structures suggested strong evolutionary links among PfV, tailed double-stranded DNA bacteriophages, and herpes viruses. The similar three-dimensional structures of the various coat proteins indicate that these viral capsids might have originated and evolved from a common ancestor. The structure of PfV provides a previously undescribed example of viral relationships across the three domains of life (Eukarya, Bacteria, and Archaea).
KW - hyperthermophilic Archaea
KW - PfV (Pyrococcus furiosus virus-like particle)
KW - Pyrococcus furiosus
KW - tailed bacteriophage
KW - X-ray crystallography
UR - http://www.scopus.com/inward/record.url?scp=34247209698&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34247209698&partnerID=8YFLogxK
U2 - 10.1016/j.jmb.2007.02.075
DO - 10.1016/j.jmb.2007.02.075
M3 - Article
C2 - 17397865
AN - SCOPUS:34247209698
VL - 368
SP - 1469
EP - 1483
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 5
ER -