The dengue virus M protein localises to the endoplasmic reticulum and forms oligomers

FEBS Lett. 2012 Apr 5;586(7):1032-7. doi: 10.1016/j.febslet.2012.02.047. Epub 2012 Mar 8.

Abstract

The dengue virus membrane (M) protein is a key component of the mature virion. Here, we characterised the cellular behaviour of M using a recombinant protein construct to understand its inherent properties. Using confocal microscopy, we showed that M and its intracellular precursor, prM, localised to the endoplasmic reticulum. M protein was also detected on the cell surface and secreted, suggesting that M can enter the secretory pathway. In addition, cross-linking studies showed that M can form dimers and tetramers. These findings suggest that M behaves as a secretory protein analogous to the major envelope protein E.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Membrane / metabolism
  • Chlorocebus aethiops
  • Cross-Linking Reagents / chemistry
  • Dengue Virus / metabolism*
  • Endoplasmic Reticulum / metabolism*
  • HEK293 Cells
  • Humans
  • Kidney / cytology
  • Kidney / metabolism*
  • Kidney / virology
  • Microscopy, Confocal
  • Molecular Weight
  • Protein Precursors / chemistry
  • Protein Precursors / genetics
  • Protein Precursors / metabolism
  • Protein Sorting Signals
  • Protein Transport
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Surface Properties
  • Vero Cells
  • Viral Matrix Proteins / chemistry
  • Viral Matrix Proteins / genetics
  • Viral Matrix Proteins / metabolism*

Substances

  • Cross-Linking Reagents
  • Protein Precursors
  • Protein Sorting Signals
  • Recombinant Proteins
  • Viral Matrix Proteins