Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes

Biol Chem. 2012 Sep;393(9):971-7. doi: 10.1515/hsz-2012-0175.


RgpA and Kgp gingipains are non-covalent complexes of endoprotease catalytic and hemagglutinin-adhesin domains on the surface of Porphyromonas gingivalis. A motif conserved in each domain has been suggested to function as an oligomerization motif. We tested this hypothesis by mutating motif residues to hexahistidine or insertion of hexahistidine tag to disrupt the motif within the Kgp catalytic domain. All modifications led to the secretion of entire Kgp activity into the growth media, predominantly in a form without functional His-tag. This confirmed the role of the conserved motif in correct posttranslational proteolytic processing and assembly of the multidomain complexes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial / chemistry*
  • Adhesins, Bacterial / genetics
  • Adhesins, Bacterial / metabolism*
  • Amino Acid Sequence
  • Base Sequence
  • Cysteine Endopeptidases / chemistry*
  • Cysteine Endopeptidases / genetics
  • Cysteine Endopeptidases / metabolism*
  • Gingipain Cysteine Endopeptidases
  • Molecular Sequence Data


  • Adhesins, Bacterial
  • Gingipain Cysteine Endopeptidases
  • Cysteine Endopeptidases