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An icosahedral algal virus has a complex unique vertex decorated by a spike.

ABSTRACT: Paramecium bursaria Chlorella virus-1 is an icosahedrally shaped, 1,900-A-diameter virus that infects unicellular eukaryotic green algae. A 5-fold symmetric, 3D reconstruction using cryoelectron microscopy images has now shown that the quasiicosahedral virus has a unique vertex, with a pocket on the inside and a spike structure on the outside of the capsid. The pocket might contain enzymes for use in the initial stages of infection. The unique vertex consists of virally coded proteins, some of which have been identified. Comparison of shape, size, and location of the spike with similar features in bacteriophages T4 and P22 suggests that the spike might be a cell-puncturing device. Similar asymmetric features may have been missed in previous analyses of many other viruses that had been assumed to be perfectly icosahedral.

SUBMITTER: Cherrier MV

PROVIDER: S-EPMC2708736 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature

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An icosahedral algal virus has a complex unique vertex decorated by a spike.

Cherrier Mickaël V MV Kostyuchenko Victor A VA Xiao Chuan C Bowman Valorie D VD Battisti Anthony J AJ Yan Xiaodong X Chipman Paul R PR Baker Timothy S TS Van Etten James L JL Rossmann Michael G MG

Proceedings of the National Academy of Sciences of the United States of America 20090618 27

Paramecium bursaria Chlorella virus-1 is an icosahedrally shaped, 1,900-A-diameter virus that infects unicellular eukaryotic green algae. A 5-fold symmetric, 3D reconstruction using cryoelectron microscopy images has now shown that the quasiicosahedral virus has a unique vertex, with a pocket on the inside and a spike structure on the outside of the capsid. The pocket might contain enzymes for use in the initial stages of infection. The unique vertex consists of virally coded proteins, some of w ...[more]

PMID: 19541619

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Project description:UnlabelledpU(L)34 and pU(L)31 of herpes simplex virus (HSV) comprise the nuclear egress complex (NEC) and are required for budding at the inner nuclear membrane. pU(L)31 also associates with capsids, suggesting it bridges the capsid and pU(L)34 in the nuclear membrane to initiate budding. Previous studies showed that capsid association of pU(L)31 was precluded in the absence of the C terminus of pU(L)25, which along with pU(L)17 comprises the capsid vertex-specific complex, or CVSC. The present studies show that the final 20 amino acids of pU(L)25 are required for pU(L)31 capsid association. Unexpectedly, in the complete absence of pU(L)25, or when pU(L)25 capsid binding was precluded by deletion of its first 50 amino acids, pU(L)31 still associated with capsids. Under these conditions, pU(L)31 was shown to coimmunoprecipitate weakly with pU(L)17. Based on these data, we hypothesize that the final 20 amino acids of pU(L)25 are required for pU(L)31 to associate with capsids. In the absence of pU(L)25 from the capsid, regions of capsid-associated pU(L)17 are bound by pU(L)31. Immunogold electron microscopy revealed that pU(L)31 could associate with multiple sites on a single capsid in the nucleus of infected cells. Electron tomography revealed that immunogold particles specific to pU(L)31 protein bind to densities at the vertices of the capsid, a location consistent with that of the CVSC. These data suggest that pU(L)31 loads onto CVSCs in the nucleus to eventually bind pU(L)34 located within the nuclear membrane to initiate capsid budding.ImportanceThis study is important because it localizes pU(L)1, a component previously known to be required for HSV capsids to bud through the inner nuclear membrane, to the vertex-specific complex of HSV capsids, which comprises the unique long region 25 (U(L)25) and U(L)17 gene products. It also shows this interaction is dependent on the C terminus of U(L)25. This information is vital for understanding how capsids bud through the inner nuclear membrane.

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An icosahedral algal virus has a complex unique vertex decorated by a spike.

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An icosahedral algal virus has a complex unique vertex decorated by a spike.

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