Expression and sequence analysis of a Treponema pallidum gene, tpn38(b), encoding an exported protein with homology to T. pallidum and Borrelia burgdorferi proteins

Authors

  • Lola V. Stamm,

    Corresponding author
    1. Program in Infectious Diseases, Department of Epidemiology, School of Public Health, University of North Carolina, 242 Rosenau Hall, CB#7400, Chapel Hill, NC 27599-7400, USA
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  • John M. Hardham,

    1. Department of Microbiology and Immunology, School of Medicine, University of North Carolina, Chapel Hill, NC 27599, USA
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    • 1

      Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, Houston, TX 77225, USA.

  • Jonathan G. Frye

    1. Program in Infectious Diseases, Department of Epidemiology, School of Public Health, University of North Carolina, 242 Rosenau Hall, CB#7400, Chapel Hill, NC 27599-7400, USA
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    • 2

      Department of Microbiology, University of Georgia, Athens, GA 30605, USA.


*Corresponding author. Tel.: + 1 (919) 966 3882; Fax: + 1 (919) 966 2089; E-mail: lstamm@email.unc.edu

Abstract

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.

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