Abstract
Biological membranes are notoriously resistant to structural analysis. Excellent candidates to tackle this problem in situ are membrane-containing viruses where the membrane is constrained by an icosahedral capsid. Cryo-EM and image reconstruction of bacteriophage PM2 revealed a membrane bilayer following the internal surface of the capsid. The viral genome closely interacts with the inner leaflet. The capsid, at a resolution of 8.4 Å, reveals 200 trimeric capsomers with a pseudo T = 21 dextro organization. Pentameric receptor-binding spikes protrude from the surface. It is evident from the structure that the PM2 membrane has at least two important roles in the life cycle. First, it acts as a scaffold to nucleate capsid assembly. Second, after host recognition, it fuses with the host outer membrane to promote genome entry. The structure also sheds light on how the viral supercoiled circular double-stranded DNA genome might be packaged and released.
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Acknowledgements
We thank P. Laurinmäki for EM; L. Valmu of the Protein Chemistry core facility, Institute of Biotechnology, for MS analyses; R. Duda for the gift of HK97 proheads; D. Belnap, R. Burnett, J. Conway, S. Fuller, B. Heymann and Y. Ji for software and helpful discussions; Finnish IT Center for Science (CSC) for computer facilities. The work was funded by the National Graduate School in Informational and Structural Biology (J.T.H.), Helsinki Graduate School in Biotechnology and Molecular Biology (H.M.K.), the Academy of Finland Centre of Excellence Programme (2000–2005) (D.H.B.) and an Academy of Finland Research Fellowship (S.J.B.).
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Huiskonen, J., Kivelä, H., Bamford, D. et al. The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes. Nat Struct Mol Biol 11, 850–856 (2004). https://doi.org/10.1038/nsmb807
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DOI: https://doi.org/10.1038/nsmb807
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