IDENTIFICATION AND SEQUENCE-ANALYSIS OF TREPONEMA-PALLIDUM TPRJ, A MEMBER OF A POLYMORPHIC MULTIGENE FAMILY

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.