1. Fossil record of an archaeal HK97-like provirus
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Narahari Akkaladevi, Vamseedhar Rayaprolu, Brian Bothner, Mark J. Young, Walid S. Maaty, Joshua Heinemann, George H. Gauss, C. Martin Lawrence, and Susan K. Brumfield
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Archaeal Viruses ,Models, Molecular ,Virosomes ,Archaeal Proteins ,viruses ,ved/biology.organism_classification_rank.species ,Encapsulin ,Particle ,Virus ,Bacteriophage ,03 medical and health sciences ,Proviruses ,Virology ,HK97 ,Linocin ,030304 developmental biology ,Genetics ,0303 health sciences ,Sequence Homology, Amino Acid ,biology ,030306 microbiology ,ved/biology ,Sulfolobus solfataricus ,Herpesvirus ,Provirus ,biology.organism_classification ,Archaea ,Recombinant Proteins ,Hyperthermophile ,3. Good health ,Pyrococcus furiosus ,Microscopy, Electron ,Capsid ,Proteome - Abstract
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 ~32nm. 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.
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