Abstract
Interstrain differences in antigenic surface proteins may reflect immunological pressure or differences in receptor specificity of the antigen. Treponema denticola exhibits considerable interstrain variability in its major surface protein (Msp), but no studies have addressed this issue in dentilisin (CTLP), a surface protease complex that has a significant role in T. denticola-host interactions in periodontal disease. Furthermore, the genome annotation of the prcB-prcA-prtP operon encoding dentilisin contains apparent errors and lacks a deduced PrtP amino acid sequence. To address these issues we analysed the protease operon from diverse T. denticola strains, as well as clones of the ATCC 35405 Type strain from which the genome sequence and original GenBank prtP sequence were derived. 6xHis-tagging of the PrtP C-terminus in ATCC 35405 demonstrated absence of the 'authentic frameshift' in PrtP reported in the genome databases. We propose that T. denticola genome annotations be updated to reflect this new information. PrcB and the PrtP N-terminal region that includes the catalytic domain were highly conserved in common laboratory strains and clinical isolates of T. denticola. Dentilisin proteolytic activity varied considerably between strains. Antibodies against PrcB, PrcA and PrtP from the type strain recognized these proteins in most T. denticola strains. PrtP varied up to 20% over the C-terminal 270 residues between strains. The PrtP C-terminal eight-residues (DWFYVEYP) was present in all strains, with two strains containing an additional Y-residue preceding the stop codon. Such conserved PrtP domains may be required for interactions with PrcA and PrcB, or for substrate interactions.