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Infection and Immunity, June 1999, p. 2986-2995, Vol. 67, No. 6
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Modulation of Major Histocompatibility Complex Protein Expression by Human Gamma Interferon Mediated by Cysteine Proteinase-Adhesin Polyproteins of Porphyromonas gingivalis

Peter L. W. Yun,1,* Arthur A. DeCarlo,2 and Neil Hunter1

Institute of Dental Research, Surry Hills, New South Wales 2010, Australia,1 and Departments of Periodontics and Oral Biology, University of Alabama at Birmingham, Birmingham, Alabama 352942

Received 4 December 1998/Returned for modification 13 January 1999/Accepted 4 March 1999

Cysteine proteinases have been emphasized in the virulence of Porphyromonas gingivalis in chronic periodontitis. These hydrolases may promote the degradation of extracellular matrix proteins and disrupt components of the immune system. In this study it was shown that purified Arg-gingipain and Lys-gingipain inhibited expression of class II major histocompatibility complex (MHC) proteins in response to the stimulation of endothelial cells with human gamma interferon (IFN-gamma ). Treatment with the cysteine proteinases resulted in a rapid shift in the apparent molecular size of IFN-gamma from 17 to 15 kDa, as shown by Western blot analysis, a response which also occurred in the presence of serum. Further, glycosylated natural IFN-gamma from human leukocytes and unglycosylated recombinant IFN-gamma from Escherichia coli were both digested by the cysteine proteinases. Immunoblot analysis indicated that cleavage within the carboxyl terminus of recombinant IFN-gamma correlated with the loss of induction of MHC class II expression as monitored by analytical flow cytometry. No hydrolysis of MHC class II molecules or human IFN-gamma receptor by these proteinases was detected by Western blot analysis. These findings suggest that P. gingivalis cysteine proteinases may alter the cytokine network at the point of infection through the cleavage of IFN-gamma . Degradation of IFN-gamma could have important consequences for the recruitment and activation of leukocytes and therefore may contribute significantly to the destruction of the periodontal attachment.

* Corresponding author. Mailing address: Institute of Dental Research, 2 Chalmers St., Surry Hills, NSW 2010, Australia. Phone: 61-2-929-33376. Fax: 61-2-929-33368. E-mail adddress: pyun{at}dentistry.usyd.edu.au

Infection and Immunity, June 1999, p. 2986-2995, Vol. 67, No. 6
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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