Lv. Stamm et al., IDENTIFICATION AND SEQUENCE-ANALYSIS OF TREPONEMA-PALLIDUM TPRJ, A MEMBER OF A POLYMORPHIC MULTIGENE FAMILY, FEMS microbiology letters, 169(1), 1998, pp. 155-163
TnphoA mutagenesis was used to identify genes encoding exported protei
ns 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 w
as determined. The deduced amino acid sequence of TprJ has homology to
the major surface protein of Treponema denticola, a periodontal patho
gen. 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 infectio
n. A putative tprJ gene was sequenced from T. pertenue, the closely re
lated 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 repo
rt of significant sequence differences within homologous genes of T. p
allidum and T. pertenue. (C) 1998 Federation of European Microbiologic
al Societies. Published by Elsevier Science B.V. All rights reserved.