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

نویسندگان

  • L V Stamm
  • S R Greene
  • H L Bergen
  • J M Hardham
  • N Y Barnes
چکیده

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.

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عنوان ژورنال:
  • FEMS microbiology letters

دوره 169 1  شماره 

صفحات  -

تاریخ انتشار 1998