| Autor: |
Stamm LV; Department of Epidemiology, School of Public Health, University of North Carolina, Chapel Hill 27599-7400, USA. lstamm@email.unc.edu, Greene SR, Bergen HL, Hardham JM, Barnes NY |
| Jazyk: |
angličtina |
| Zdroj: |
FEMS microbiology letters [FEMS Microbiol Lett] 1998 Dec 01; Vol. 169 (1), pp. 155-63. |
| DOI: |
10.1111/j.1574-6968.1998.tb13312.x |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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