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Marek's disease virus VP22: subcellular localization and characterization of carboxyl terminal deletion Mutations.

Marek's disease virus (MDV) is an alphaherpesvirus that causes T cell lymphoma and severe immunosuppression in chickens. The MDV UL49 gene, which encodes the tegument viral protein 22 (VP22), has been expressed as a green fluorescent protein (GFP) fusion protein in chicken embryonic fibroblasts to examine its subcellular localization. As with both human herpesvirus 1 and bovine herpesvirus 1VP22-GFP fusion proteins, the MDV VP22-GFP product binds to microtubules and heterochromatin. In addition, the MDV protein also binds to the centrosomes. During mitosis, VP22-GFP binds to sister chromatids, but dissociates from the centrosomes and the microtubules of the mitotic spindle. A series of VP22 carboxy terminal truncation mutants were constructed to define regions responsible for these binding properties. These mutants identified separable domains or motifs responsible for binding microtubules and heterochromatin.[1]

References

  1. Marek's disease virus VP22: subcellular localization and characterization of carboxyl terminal deletion Mutations. O'Donnell, L.A., Clemmer, J.A., Czymmek, K., Schmidt, C.J. Virology (2002) [Pubmed]
 
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