Identification of the Treponema pallidum subsp. pallidum glycerophosphodiester phosphodiesterase homologue

FEMS Microbiol Lett. 1997 Sep 15;154(2):303-10. doi: 10.1111/j.1574-6968.1997.tb12660.x.


To identify potential opsonic targets of Treponema pallidum subsp. pallidum, a treponemal genomic expression library was constructed and differentially screened with opsonic and non-opsonic T. pallidum antisera. This method identified an immunoreactive clone containing an open reading frame encoding a 356 residue protein. Nucleotide sequence analysis demonstrated the translated protein to be a homologue of glycerophosphodiester phosphodiesterase, a glycerol metabolizing enzyme previously identified in Haemophilus influenzae, Escherichia coli, Bacillus subtilis and Borrelia hermsii. Sequence alignment analyses revealed the T. pallidum and H. influenzae enzymes share a high degree of amino acid sequence similarity (72%), suggesting that in T. pallidum this molecule may be surface exposed and involved in IgD binding as is the case with its counterpart in H. influenzae.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Molecular Sequence Data
  • Phosphoric Diester Hydrolases / chemistry
  • Phosphoric Diester Hydrolases / isolation & purification*
  • Treponema pallidum / enzymology*


  • Phosphoric Diester Hydrolases
  • glycerophosphodiester phosphodiesterase

Associated data

  • GENBANK/AF004286