| Literature DB >> 9851047 |
L V Stamm1, S R Greene, H L Bergen, J M Hardham, N Y Barnes.
Abstract
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.Entities:
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Year: 1998 PMID: 9851047 DOI: 10.1111/j.1574-6968.1998.tb13312.x
Source DB: PubMed Journal: FEMS Microbiol Lett ISSN: 0378-1097 Impact factor: 2.742