Journal
VIROLOGY
Volume 417, Issue 2, Pages 362-368Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2011.06.019
Keywords
Archaea; Provirus; HK97; Bacteriophage; Herpesvirus; Encapsulin; Linocin; Virus; Particle
Categories
Funding
- National Science Foundation [MCB 1022481, MCB 0646499, DEB-0936178, EF-080220]
- Murdock Charitable Trust
- NIH NCRR COBRE [P20 RR024237]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0920312] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1022481] Funding Source: National Science Foundation
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One of the outstanding questions in biology today is the origin of viruses. We have discovered a protein in the hyperthermophile Sulfolobus solfataricus while following proteome regulation during viral infection that led to the discovery of a fossil provirus. Characterization of the wild type and recombinant protein revealed that it assembled into virus-like particles with a diameter of similar to 32 nm. Sequence and structural analyses showed that the likely proviral capsid protein. Sso2749, is homologous to a protein from Pyrococcus furiosus that forms virus-like particles using the HK-97 major capsid protein fold. The SsP2-provirus appears mosaic and contains proteins with similarity to, among others, eukaryotic herpesviruses and tailed dsDNA bacteriophage families, reinforcing the hypothesis of a common ancestral gene pool across all three domains of life. This is the first description of the HK-97 fold in a crenarchaeal virus and the first direct genomic connection of linocin-like protein cages to a virus. (C) 2011 Elsevier Inc. All rights reserved.
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