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Identification of Protein Interacting Partners Using Tandem Affinity Purification
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Recognition of eukaryotic initiation factor 4G isoforms by picornaviral proteinases

Nicole Foeger1, Walter Glaser, Tim Skern

  • 1Institute of Medical Biochemistry, Division of Biochemistry, University of Vienna, Vienna Bio Center, Dr. Bohr-Gasse 9/3, Austria.

The Journal of Biological Chemistry
|September 14, 2002
PubMed

Insights

Foot and mouth disease virus leader proteinase (L(pro)) binds to host factor eukaryotic initiation factor (eIF) 4GI. This interaction, crucial for viral replication, involves specific domains on both proteins.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Foot and mouth disease virus leader proteinase (L(pro)) is a cysteine proteinase essential for viral replication.
  • L(pro) inhibits host protein synthesis by cleaving eukaryotic initiation factor (eIF) 4GI.
  • Understanding L(pro) interactions with eIF4G is critical for developing antiviral strategies.

Purpose of the Study:

  • To investigate the interaction between FMDV L(pro) and host factors eIF4GI and eIF4GII.
  • To map the specific binding domains on L(pro) and eIF4GI involved in this interaction.
  • To compare the binding characteristics of L(pro) with human rhinovirus 2A proteinase (2A(pro)).

Main Methods:

  • Expression of catalytically inactive L(pro) as a glutathione S-transferase fusion protein.
  • Utilized deletion mutagenesis and specific mutagenesis to identify binding domains.
  • Employed proteolysis and in vitro translation to generate eIF4GI fragments for mapping.

Main Results:

  • L(pro) specifically binds to eIF4G isomers in vitro.
  • The binding domain on L(pro) was mapped to residues 183-195 and Cys(133).
  • The interaction region on eIF4GI was localized to residues 640-669, independent of the cleavage site.

Conclusions:

  • Picornaviral proteinases, including FMDV L(pro) and HRV 2A(pro), exhibit novel binding interactions with eIF4G isoforms.
  • These interactions are mediated by specific domains and do not require the canonical cleavage site.
  • This suggests a conserved mechanism of host factor manipulation among picornaviruses.

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