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

Recherche transversale
(titres de publication, de périodique et noms de colloque inclus)
2018-11-30 - Colloque/Présentation - poster - Anglais - 1 page(s)

Lamotte Laurie-Anne , Demeret Caroline, Tafforeau Lionel , "Interactions between Influenza A virus NS1 protein and Human ubiquitin-proteasome system" in 2nd Annual meeting of the Namur Research Pole in Infectiology, Namur, Belgique, 2018

  • Codes CREF : Biologie (DI3100)
  • Unités de recherche UMONS : Biologie cellulaire (S815)
  • Instituts UMONS : Institut des Sciences et Technologies de la Santé (Santé), Institut des Biosciences (Biosciences)

Abstract(s) :

(Anglais) As obligate intracellular parasites, viruses infect host cells and use their metabolism to replicate themselves through interactions between viral and cellular proteins. For example, the human ubiquitin-proteasome system (UPS) is particularly targeted by viral proteins. Ubiquitination is a post-translational modification regulating stability, localization or activity of targeted proteins. Ubiquitination occurs in several steps and requires three enzyme types (E1, E2 and E3). Ubiquitinated substrates can subsequently be recognized by ubiquitin-binding domain containing proteins such as the proteasome which will degrade targeted proteins. Ubiquitination plays a crucial role in cell infection by Influenza A virus (IAV) regulating entry and replication of the virus. Among IAV proteins, the non-structural protein NS1 is known to interact with a lot of cellular proteins e.g. within interferon and apoptosis pathways. By using GPCA (Gaussia princeps Protein Complementation Assay), we screened a human UPS library and identified that NS1 physically interacts with 98 UPS proteins. To estimate the involvement of NS1 interactors I will first examine the productive infectious cycle of IAV upon siRNA-mediated depletion of the individual interactors in A549 cells. A subset of interactors will be further characterized. To this end, I will perform subcellular localisation of some NS1 partners by immunofluorescence microscopy in A549 cells (i) in presence or absence of NS1 and (ii) during the course of IAV infection. In order to know whether these interactors are involved in NS1 ubiquitination I will then perform an ubiquitination assay on NS1. Finally, I will analyse the potential effect of NS1 on few interactors by performing an ubiquitination assay on known targets of the UPS factors.