Schmallenberg virus non-structural protein NSm: Intracellular distribution and role of non-hydrophobic domains

Virology. 2018 Mar;516:46-54. doi: 10.1016/j.virol.2017.12.034. Epub 2018 Jan 9.

Abstract

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 Gc.

Keywords: Golgi complex; Monoclonal antibody; NSm; Non-structural protein; Orthobunyavirus; Reverse genetics; Schmallenberg virus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bunyaviridae Infections / veterinary*
  • Bunyaviridae Infections / virology
  • Golgi Apparatus / virology*
  • Mice
  • Mice, Inbred BALB C
  • Orthobunyavirus / chemistry
  • Orthobunyavirus / genetics
  • Orthobunyavirus / metabolism*
  • Protein Domains
  • Protein Transport
  • Sequence Deletion
  • Viral Nonstructural Proteins / chemistry*
  • Viral Nonstructural Proteins / genetics
  • Viral Nonstructural Proteins / metabolism*

Substances

  • Viral Nonstructural Proteins