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PMID: 11953390 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Hydrolysis of epithelial junctional proteins by Porphyromonas gingivalis gingipains.

Infection and immunity ·Vol. 70 ·No. 5 ·2002-05-00 ·Pages 2512-8

Katz J, Yang QB, Zhang P, Potempa J, Travis J, Michalek SM, Balkovetz DF

Abstract

Porphyromonas gingivalis has been implicated as an etiologic agent of adult periodontitis. We have previously shown that P. gingivalis can degrade the epithelial cell-cell junction complexes, thus suggesting that this bacterium can invade the underlying connective tissues via a paracellular pathway. However, the precise mechanism(s) involved in this process has not been elucidated. The purpose of this study was to determine if the arginine- and lysine-specific gingipains of P. gingivalis (i.e., HRgpA and RgpB, and Kgp, respectively) were responsible for the degradation of E-cadherin, the cell-cell adhesion protein in the adherens junctions. In addition, we compared the degradative abilities of the whole gingipains HRgpA and Kgp to those of their catalytic domains alone. In these studies, immunoprecipitated E-cadherin as well as monolayers of polarized Madin-Darby canine kidney (MDCK) epithelial cell cultures were incubated with the gingipains and hydrolysis of E-cadherin was assessed by Western blot analysis. Incubation of P. gingivalis cells with immunoprecipitated E-cadherin resulted in degradation, whereas prior exposure of P. gingivalis cells to leupeptin and especially acetyl-Leu-Val-Lys-aldehyde (which are arginine- and lysine-specific inhibitors, respectively) reduced this activity. Furthermore, incubation of E-cadherin immunoprecipitates with the different gingipains resulted in an effective and similar hydrolysis of the protein. However, when monolayers of MDCK cells were exposed to the gingipains, Kgp was most effective in hydrolyzing the E-cadherin molecules in the adherens junction. Kgp was more effective than its catalytic domain in degrading E-cadherin at 500 nM but not at a lower concentration (250 nM). These results suggest that the hemagglutinin domain of Kgp plays a role in degradation and that there is a critical threshold concentration for this activity. Taken together, these results provide evidence that the gingipains, especially Kgp, are involved in the degradation of the adherens junction of epithelial cells, which may be important in the invasion of periodontal connective tissue by P. gingivalis.

MeSH Terms
Adhesins, Bacterial Animals Cadherins/metabolism Catalytic Domain Cell Line Cysteine Endopeptidases/pharmacology Dogs Epithelial Cells/metabolism Gingipain Cysteine Endopeptidases Hemagglutinins/pharmacology Hydrolysis Porphyromonas gingivalis/enzymology
Chemicals
Adhesins, Bacterial Cadherins Gingipain Cysteine Endopeptidases Hemagglutinins Cysteine Endopeptidases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Katz Jannet
Department of Oral Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA. jenny_katz@micro.microbio.uab.edu
Yang Qiu-Bo
Zhang Ping
Potempa Jan
Travis James
Michalek Suzanne M
Balkovetz Daniel F
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
Published
2002-05-00
Pages
2512-8
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC127922
Subset
IM
Grants
NIDCR NIH HHS · DE 08228 · United States
NIDCR NIH HHS · DE 10607 · United States
NIDCR NIH HHS · DE 13269 · United States
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