N. Slakeski et al., CHARACTERIZATION OF A PORPHYROMONAS-GINGIVALIS GENE PRTR THAT ENCODESAN ARGININE-SPECIFIC THIOL PROTEINASE AND MULTIPLE ADHESINS, Biochemical and biophysical research communications, 224(3), 1996, pp. 605-610
Cysteine proteinases of Porphyromonas gingivalis have been implicated
as major virulence factors in the development of periodontitis. Severa
l groups have reported the characterisation of similar genes encoding
the same arginine-specific thiol proteinase from P. gingivalis; howeve
r, the reported size and structure of the genes have varied. We report
here the complete nucleotide sequence of the gene prtR that encodes a
polyprotein containing the Arg-specific proteinase and multiple haema
gglutinins/adhesins. The nascent polyprotein consists of a putative le
ader sequence and a prosequence followed by the 45 kDa Arg-specific pr
oteinase and 44, 15, 17 and 27 kDa sequence-related adhesins in that o
rder. The size and structure of the prtR are consistent with the size
of the mRNA transcript (5.3 kb) and the size and sequences of the indi
vidual protein components purified from P. gingivalis. (C) 1996 Academ
ic Press, Inc.