The Structure of the Cyprinid Herpesvirus 3 ORF112-Zα/Z-DNA Complex Reveals a Mechanism of Nucleic Acids Recognition Conserved with E3L, a Poxvirus Inhibitor of

The Structure of the Cyprinid Herpesvirus 3 ORF112-Zα/Z-DNA Complex Reveals a Mechanism of Nucleic Acids Recognition Conserved with E3L, a Poxvirus Inhibitor of

The Structure of the Cyprinid Herpesvirus 3 ORF112-Zα/Z-DNA Complex Reveals a Mechanism of Nucleic Acids Recognition Conserved with E3L, a Poxvirus Inhibitor of
Although nucleo-cytoplasmic transport is typically mediated through nuclear pore complexes, herpesvirus capsids exit the nucleus via a unique vesicular pathway. For a more comprehensive list of citations to this article, users are encouraged to perform a search in SciFinder. The structures of the major glycoproteins and receptors involved in the entry of the prototypical herpesviruses herpes simplex virus (HSV) and Epstein-Barr virus (EBV) are now known. Importantly, we confirmed that vIRF2 can specifically interact with the promoters of the genes encoding PIK3C3, HMGCR, and HMGCL, which are associated with autophagosome formation or tumor progression and metastasis, and regulate their transcription in vivo. We conclude that the pentons, like the hexons, are composed of VP5, which exists as a pentamer at the capsid vertices (the pentons) and as a hexamer in all other capsomers (the hexons). The observed resistance of this viral cyclin-cdk complex to inhibition by the p27(KIP:) cdk inhibitor is explained by sequence and conformational variation in the cyclin rendering the p27(KIP:)-binding site on the cyclin subunit non-functional. Three successive residues, L424, E425 and V426, which relate to viral growth, reside on the β hairpin close to the dimer’s two-fold axis.

Localization of ORF112 protein in stress granules induced in CyHV-3 infected fish cells suggests a functional behaviour similar to that of Zα domains of the interferon-regulated, nucleic acid surveillance proteins ADAR1 and DAI.

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