Identification and sequence analysis of Treponema pallidum tprJ, a member of a polymorphic multigene family

FEMS Microbiol Lett. 1998 Dec 1;169(1):155-63. doi: 10.1111/j.1574-6968.1998.tb13312.x.


TnphoA mutagenesis was used to identify genes encoding exported proteins in a genomic DNA library of Treponema pallidum, the syphilis agent. The nucleotide sequence of an open reading frame (tprJ) that encodes a 755-amino acid protein with a predicted molecular mass of 81.1 kDa was determined. The deduced amino acid sequence of TprJ has homology to the major surface protein of Treponema denticola, a periodontal pathogen. Southern hybridization and genomic DNA sequence analysis indicate that tprJ is a member of a polymorphic multigene family. RT-PCR data showed that tprJ is expressed in treponemes during syphilitic infection. A putative tprJ gene was sequenced from T. pertenue, the closely related yaws agent. The deduced amino acid sequence of T. pertenue TprJ is 87.3% identical to that of T. pallidum TprJ. This is the first report of significant sequence differences within homologous genes of T. pallidum and T. pertenue.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • Base Sequence
  • Genes, Bacterial*
  • Genomic Library
  • Molecular Sequence Data
  • Multigene Family*
  • Mutagenesis, Insertional
  • Polymorphism, Genetic*
  • Porins / genetics*
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Species Specificity
  • Treponema / genetics
  • Treponema pallidum / genetics*


  • Bacterial Proteins
  • Porins
  • major outer sheath protein, Treponema

Associated data

  • GENBANK/AF073527
  • GENBANK/U88957