DI-UMONS : Dépôt institutionnel de l’université de Mons

Recherche transversale
(titres de publication, de périodique et noms de colloque inclus)
2010-09-04 - Colloque/Présentation - communication orale - Anglais - 1 page(s)

Juillard Franceline, Bazot Quentin, Mure F, Tafforeau Lionel , Rabourdin-Combe Chantal, Lotteau Vincent, Manet Evelyne, Gruffat Henri, "EB2, the EBV viral mRNA export protein interacts with SRP20, a factor implicated in cellular mRNA splicing and export" in 14th Biennal Conference of the International Association for Research on Epstein-Barr Virus & Associated Diseases, Birmingham, UK, 2010

  • Codes CREF : Biologie (DI3100)
  • Unités de recherche UMONS : Biologie cellulaire (S815)
  • Instituts UMONS : Institut des Biosciences (Biosciences)

Abstract(s) :

(Anglais) The Epstein-Barr Virus (EBV) early nuclear protein, EB2 (also called Mta, SM and BMLF1), allows the nuclear export of a subset of early and late viral RNAs derived from intronless genes and its presence is essential for the production of infectious particles. Moreover, we recently found that EB2 strongly increases the translation of its target mRNAs. However, the mechanisms by which EB2 fulfils these various functions are not yet completely understood. By using a yeast two-hybrid screen, we have now identified the cellular factor, SRp20, as a cellular partner for EB2. We confirmed this interaction by means of interaction studies (co- immunoprecipitation assays and GST-pull down) and we have characterized the interaction domain in both proteins. In order to understand the importance of this interaction in terms of EB2 function, we first tested the effect of a specific siRNA directed against SRp20 on EB2- mediated mRNA export. Interestingly, we found that the export by EB2 of a luciferase reporter messenger generated from an intronless construct, was strongly diminished in the absence of SRp20. We then tested the effect of EB2 on a β-globin reporter construct in the presence of overexpressed SRp20. Overexpression of SRp20 alone is known to promote aberrant mRNA splicing in this model. In the presence of EB2, we found that overexpression of SRp20 strongly increases EB2-dependent accumulation of unspliced β-globin mRNA in the cytoplasm. Interaction of EB2 with SRp20 thus appears to be crucial for its capacity to efficiently export unspliced mRNA.