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Insights into virus evolution and membrane biogenesis from the structure of the marine lipid-containing bacteriophage PM2

DOI: 10.1016/j.molcel.2008.06.026 DOI Help

Authors: Nicola Abrescia (University of Oxford) , Jonathan Grimes (Division of Structural Biology, University of Oxford) , Hanna M. Kivela (University of Jyväskylä; University of Helsinki) , Rene Assenberg (University of Oxford) , Geoff C. Sutton (University of Oxford) , Sarah J. Butcher (University of Helsinki) , Jaana K. H. Bamford (University of Jyväskylä) , Dennis M. Bamford (University of Helsinki) , David I. Stuart (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Molecular Cell , VOL 31 (5) , PAGES 749-761

State: Published (Approved)
Published: January 2008

Abstract: Recent, primarily structural observations indicate that related viruses, harboring no sequence similarity, infect hosts of different domains of life. One such clade of viruses, defined by common capsid architecture and coat protein fold, is the so-called PRD1-adenovirus lineage. Here we report the structure of the marine lipid-containing bacteriophage PM2 determined by crystallographic analyses of the entire similar to 45 MDa virion and of the outer coat proteins P1 and P2, revealing PM2 to be a primeval member of the PRD1-adenovirus lineage with an icosahedral, shell and canonical double beta barrel major coat protein. The view of the lipid bilayer, richly decorated with membrane proteins, constitutes a rare visualization of an in vivo membrane. The viral membrane proteins P3 and P6 are organized into a lattice, suggesting a possible assembly pathway to produce the mature virus.

Subject Areas: Biology and Bio-materials


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