The Membrane-Proximal "Stem" Region Increases the Stability of the Flavivirus E Protein Postfusion Trimer and Modulates Its Structure

J Virol. 2013 Sep;87(17):9933-8. doi: 10.1128/JVI.01283-13. Epub 2013 Jun 26.

Abstract

The flavivirus fusion protein E contains a "stem" region which is hypothesized to be crucial for driving fusion. This sequence element connects the ectodomain to the membrane anchor, and its structure in the trimeric postfusion conformation is still poorly defined. Using E trimers of tick-borne encephalitis virus with stem truncations of different lengths, we show that the N-terminal part of the stem increases trimer stability and also modulates the trimer structure outside the stem interaction site.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Encephalitis Viruses, Tick-Borne / chemistry
  • Encephalitis Viruses, Tick-Borne / genetics
  • Encephalitis Viruses, Tick-Borne / physiology
  • Flavivirus / chemistry*
  • Flavivirus / genetics
  • Flavivirus / physiology
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Protein Stability
  • Protein Structure, Quaternary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Sequence Homology, Amino Acid
  • Viral Fusion Proteins / chemistry*
  • Viral Fusion Proteins / genetics
  • Viral Fusion Proteins / physiology
  • Virus Internalization

Substances

  • Recombinant Proteins
  • Viral Fusion Proteins