Identification of the Treponema pallidum subsp. pallidum glycerophosphodiester phosphodiesterase homologue.
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.
Stebeck
C E
CE
Department of Medicine, University of Washington, Seattle 98195, USA.
Shaffer
J M
JM
Arroll
T W
TW
Lukehart
S A
SA
Van Voorhis
W C
WC
D000595:Amino Acid Sequence; D001483:Base Sequence; D008969:Molecular Sequence Data; D010727:Phosphoric Diester Hydrolases / Q000737:chemistry / Q000302:isolation & purification*; D014210:Treponema pallidum / Q000201:enzymology*
D010727:Phosphoric Diester Hydrolases; C038133:glycerophosphodiester phosphodiesterase