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Identification of the Treponema pallidum subsp. pallidum glycerophosphodiester phosphodiesterase homologue.
Title | Identification of the Treponema pallidum subsp. pallidum glycerophosphodiester phosphodiesterase homologue. |
Publication Type | Journal Article |
Year of Publication | 1997 |
Authors | Stebeck, CE, Shaffer, JM, Arroll, TW, Lukehart, SA, Van Voorhis, WC |
Journal | FEMS Microbiol Lett |
Volume | 154 |
Issue | 2 |
Pagination | 303-10 |
Date Published | 1997 Sep 15 |
ISSN | 0378-1097 |
Keywords | Amino Acid Sequence, Base Sequence, Molecular Sequence Data, Phosphoric Diester Hydrolases, Treponema pallidum |
Abstract | 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. |
Alternate Journal | FEMS Microbiol. Lett. |
PubMed ID | 9311129 |