Unique architecture of thermophilic archaeal virus APBV1 and its genome packaging

• Published in: Nature communications Vol. 8; no. 1; pp. 1436 - 6
• Main Authors: Ptchelkine, Denis, Gillum, Ashley, Mochizuki, Tomohiro, Lucas-Staat, Soizick, Liu, Ying, Krupovic, Mart, Phillips, Simon E. V., Prangishvili, David, Huiskonen, Juha T.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 10.11.2017; Nature Publishing Group; Nature Portfolio
• Subjects: 631/326/26; 631/326/596/2148; 631/535/1258; Aeropyrum; Aeropyrum - virology; Aeropyrum pernix; Archaeal Viruses; Archaeal Viruses - genetics; Archaeal Viruses - physiology; Archaeal Viruses - ultrastructure; Atomic structure; Cryoelectron Microscopy; Deoxyribonucleic acid; Disease resistance; DNA; DNA, Superhelical; DNA, Superhelical - chemistry; DNA, Superhelical - genetics; DNA, Viral; DNA, Viral - chemistry; DNA, Viral - genetics; Electron microscopy; Genome, Viral; Genomes; Glycoproteins; Glycosylation; Handedness; Humanities and Social Sciences; Hydrophobic and Hydrophilic Interactions; Hydrophobicity; Imaging, Three-Dimensional; Interfaces; Life Sciences; Microbiology and Parasitology; Models, Molecular; multidisciplinary; Packaging; Packing; Protein Subunits; Science; Science (multidisciplinary); Superhelix; Thermal stability; Viral Structural Proteins; Viral Structural Proteins - chemistry; Viral Structural Proteins - genetics; Virions; Virology; Virus Assembly; Virus Assembly - genetics; Viruses; VP1 protein
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-017-01668-0

Archaeal viruses have evolved to infect hosts often thriving in extreme conditions such as high temperatures. However, there is a paucity of information on archaeal virion structures, genome packaging, and determinants of temperature resistance. The rod-shaped virus APBV1 ( Aeropyrum pernix bacilliform virus 1) is among the most thermostable viruses known; it infects a hyperthermophile Aeropyrum pernix , which grows optimally at 90 °C. Here we report the structure of APBV1, determined by cryo-electron microscopy at near-atomic resolution. Tight packing of the major virion glycoprotein (VP1) is ensured by extended hydrophobic interfaces, and likely contributes to the extreme thermostability of the helical capsid. The double-stranded DNA is tightly packed in the capsid as a left-handed superhelix and held in place by the interactions with positively charged residues of VP1. The assembly is closed by specific capping structures at either end, which we propose to play a role in DNA packing and delivery. The rod-shaped virus APBV1 is among the most thermostable viruses known. Here, Ptchelkine et al. determine its structure at near-atomic resolution, show that the DNA is packed as left-handed superhelix and identify extended hydrophobic interfaces that likely contribute to the extreme thermostability of the capsid.