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...

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Bibliographic Details
Published in:FEMS microbiology letters 1997-09, Vol.154 (2), p.303-310
Main Authors: Stebeck, Caroline E., Shaffer, Jeanne M., Arroll, Thomas W., Lukehart, Sheila A., Van Voorhis, Wesley C.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Glycerophosphodiester phosphodiesterase
IgD binding
Lipoprotein
Molecular Sequence Data
Phosphoric Diester Hydrolases - chemistry
Phosphoric Diester Hydrolases - isolation & purification
Treponema pallidum - enzymology
Treponema pallidum subsp. pallidum
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Summary: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.
ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-1097(97)00346-7