Open AccessIdentification of the Treponema pallidum subsp. pallidum glycerophosphodiester phosphodiesterase homologue
Author(s) -
Stebeck Caroline E.,
Shaffer Jeanne M.,
Arroll Thomas W.,
Lukehart Sheila A.,
Voorhis Wesley C.
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb12660.x
Subject(s) - treponema , biology , open reading frame , microbiology and biotechnology , peptide sequence , escherichia coli , virology , biochemistry , gene , syphilis , human immunodeficiency virus (hiv)
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 .