Schmallenberg virus non-structural protein NSm

Highlights:
  • Identification of over 1000 direct and proximal LMP1 protein-protein interactions.
  • Many interactors are involved in signal transduction and protein/vesicle trafficking.
  • Novel validated interactions include HSC70, ITGB1, syntenin-1, TSG101, and STAT3.

R I N K I N T H E W I L D A I R (1)

Schmallenberg virus (SBV) induces fetal malformation, abortions and stillbirth in ruminants. While the non-structural protein NSs is a major virulence factor, the biological function of NSm, the second non-structural protein which consists of three hydrophobic transmembrane (I, III, V) and two non-hydrophobic regions (II, IV), is still unknown. Here, a series of NSm mutants displaying deletions of nearly the entire NSm or of the non-hydrophobic domains was generated and the intracellular distribution of NSm was assessed. SBV-NSm is dispensable for the generation of infectious virus and mutants lacking domains II – V showed growth properties similar to the wild-type virus. In addition, a comparable intracellular distribution of SBV-NSm was observed in mammalian cells infected with domain II mutants or wild-type virus. In both cases, NSm co-localized with the glycoprotein Gc in the Golgi compartment. However, domain IV-deletion mutants showed an altered distribution pattern and no co-localization of NSm and Gcseemore..

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