Structural rearrangements in the membrane penetration protein of a non-enveloped virus

Philip R. Dormitzer (), Emma B. Nason, B. V. Venkataram Prasad and Stephen C. Harrison
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Philip R. Dormitzer: Harvard Medical School, and the Laboratory of Molecular Medicine, Children's Hospital
Emma B. Nason: Baylor College of Medicine
B. V. Venkataram Prasad: Baylor College of Medicine
Stephen C. Harrison: Harvard Medical School, and the Laboratory of Molecular Medicine, Children's Hospital

Nature, 2004, vol. 430, issue 7003, 1053-1058

Abstract: Abstract Non-enveloped virus particles (those that lack a lipid-bilayer membrane) must breach the membrane of a target host cell to gain access to its cytoplasm. So far, the molecular mechanism of this membrane penetration step has resisted structural analysis. The spike protein VP4 is a principal component in the entry apparatus of rotavirus, a non-enveloped virus that causes gastroenteritis and kills 440,000 children each year1. Trypsin cleavage of VP4 primes the virus for entry by triggering a rearrangement that rigidifies the VP4 spikes2. We have determined the crystal structure, at 3.2 Å resolution, of the main part of VP4 that projects from the virion. The crystal structure reveals a coiled-coil stabilized trimer. Comparison of this structure with the two-fold clustered VP4 spikes in a ∼12 Å resolution image reconstruction from electron cryomicroscopy of trypsin-primed virions shows that VP4 also undergoes a second rearrangement, in which the oligomer reorganizes and each subunit folds back on itself, translocating a potential membrane-interaction peptide from one end of the spike to the other. This rearrangement resembles the conformational transitions of membrane fusion proteins of enveloped viruses3,4,5,6.

Date: 2004
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DOI: 10.1038/nature02836

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