Mitochondrial targeting sequence of the influenza A virus PB1-F2 protein and its function in mitochondria

FEBS Lett. 2004 Dec 17;578(3):331-6. doi: 10.1016/j.febslet.2004.11.017.

Abstract

The influenza A virus PB1-F2 protein predominantly localizes in the mitochondria of virus-infected cells. A series of cDNAs encoding N- and C-terminal deletion mutants and site-directed mutagenesis of the basic residues of PB1-F2 appended to 3xFLAG revealed the domain from residues 46 to 75 to be both necessary and sufficient for mitochondrial targeting. In addition, the subdomain residues 63-75 and both Lys73 and Arg75 are minimally required for mitochondrial localization. Transfection of untagged- and 3xFLAG tagged-PB1-F2 into Vero, HeLa and MDCK cells changed the mitochondrial morphology from a filamentous to a dotted structure and suppressed the inner-membrane potential.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal / metabolism
  • Arginine / chemistry
  • Benzimidazoles
  • Cell Line
  • Dogs
  • Fluorescein-5-isothiocyanate
  • Fluorescent Dyes
  • HeLa Cells
  • Humans
  • Influenza A virus / physiology*
  • Lysine / chemistry
  • Microscopy, Fluorescence
  • Mitochondria / metabolism*
  • Mutagenesis, Site-Directed
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Sequence Deletion
  • Viral Proteins* / chemistry
  • Viral Proteins* / genetics
  • Viral Proteins* / metabolism
  • Viral Proteins* / physiology

Substances

  • Antibodies, Monoclonal
  • Benzimidazoles
  • Fluorescent Dyes
  • PB1-F2 protein, Influenza A virus
  • Recombinant Fusion Proteins
  • Viral Proteins
  • Arginine
  • Fluorescein-5-isothiocyanate
  • Lysine
  • bisbenzimide ethoxide trihydrochloride