Identification of a Secreted Fatty Acid and Retinol-Binding Protein (Hp-FAR-1) from <I>Heligmosomoides polygyrus</I>


  • Jennifer L. Bath
  • Michael Robinson
  • Malcolm W. Kennedy
  • Chidimma Agbasi
  • Lucas Linz
  • Erin Maetzold
  • Michael Scheidt
  • Megan Knox
  • Daniel Ram
  • Jordan Hein
  • Colin Clark
  • Jeremy Drees


Heligmosomoides polygyrus, host-parasitic relationship, Hp-FAR-1, hp-far-1, lifecycle, molecular biology, nematode, retinol binding


Hp-FAR-1 is a major, secreted antigen of the parasitic nematode Heligmosomoides polygyrus, a laboratory mouse model frequently used to study the cellular mechanisms of chronic helminth infections. The DNA encoding Hp-FAR-1 was recovered by screening a fourth larval (L4) H. polygyrus cDNA expression library using antibodies raised against L4 stage excretory/secretory (E/S) proteins. Predictions of secondary structure based on the Hp-FAR-1 amino acid sequence indicated that an alpha-helix predominates in Hp-FAR-1, possibly with some coiled-coil conformation, with no beta-structure. Fluorescence-based ligand binding analysis confirmed that the recombinant Hp-FAR-1 (rHp-FAR-1) binds the fluorescent fatty acid analog 11-((5-[dimethylaminoaphthalene-1-sulfonyl)amino)undecanoic acid (DAUDA), and by competition oleic acid. RT-PCR amplification of the hp-far-1 gene indicated that the gene is transcribed in all parasitic stages of the organism's life cycle. The presence of a secreted FAR protein in the well-defined laboratory model of H. polygyrus provides an excellent model for the further study and analysis of the in vivo role of secreted FAR proteins in parasitism, and supports the mounting evidence that secreted FAR proteins play a major role in nematode parasitism.