Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, Houston, TX 77225, USA.
Expression and sequence analysis of a Treponema pallidum gene, tpn38(b), encoding an exported protein with homology to T. pallidum and Borrelia burgdorferi proteins
Article first published online: 17 JAN 2006
FEMS Microbiology Letters
Volume 135, Issue 1, pages 57–63, January 1996
How to Cite
Stamm, L. V., Hardham, J. M. and Frye, J. G. (1996), Expression and sequence analysis of a Treponema pallidum gene, tpn38(b), encoding an exported protein with homology to T. pallidum and Borrelia burgdorferi proteins. FEMS Microbiology Letters, 135: 57–63. doi: 10.1111/j.1574-6968.1996.tb07966.x
- Issue published online: 17 JAN 2006
- Article first published online: 17 JAN 2006
- (Received 8 September 1995, Accepted 16 October 1995)
- Treponema pallidum;
- Borrelia burgdorferi;
Abstract An Escherichia coli clone containing recombinant plasmid C19 was identified from a Treponema pallidum genomic DNA library by in situ immunoassay. E. coli maxicells containing pC19 synthesized a treponemal protein doublet of 39.2 and 38.2 kDa, designated TpN38(b). Pulse-chase and protein processing studies showed that TpN38(b) is synthesized with a cleavable amino-terminal signal peptide. A 2.0-kb fragment of pC19 containing the tpn38(b) gene was subcloned and sequenced. The tpn38(b) gene is 1029 nucleotides long and encodes a protein of 343 amino acids with a calculated molecular mass of 37.9 kDa. The deduced amino acid sequence of TpN38(b) has homology with the T. pallidum TpN35 lipoprotein and the Borrelia burgdorferi BmpA, BmpB, BmpC, and BmpD proteins.