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

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  • Maryta Sztukowska, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, United States
  • Florian Veillard, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, United States
  • Barbara Potempa, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, United States
  • Matthew Bogyo, Departments of Pathology, and Microbiology and Immunology, Stanford University School of Medicine, United States
  • Jan Johannes Enghild
  • Ida B Thøgersen
  • Ky-Anh Nguyen, Institute of Dental Research, Westmead Centre for Oral Health and Westmead Millenium Institute, Australia
  • Jan Potempa, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, United States
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
Original languageEnglish
JournalWorld Journal of Biological Chemistry
Volume393
Issue9
Pages (from-to)971-977
Number of pages7
ISSN1949-8454
DOIs
Publication statusPublished - Sep 2012

    Research areas

  • cysteine protease, limited proteolysis, periodontitis, Porphyromonas gingivalis, posttranslational processing

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