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Infection and Immunity, July 1999, p. 3248-3256, Vol. 67, No. 7
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Purification, Characterization, and Sequence Analysis of a Potential Virulence Factor from Porphyromonas gingivalis, Peptidylarginine Deiminase

Walker T. McGraw,1 Jan Potempa,2 David Farley,3 and James Travis1,*

Department of Biochemistry, University of Georgia, Athens, Georgia 30602,1 Department of Arthritis Biology, Novartis Pharmaceuticals, Summit, New Jersey 07901,3 and Institute of Molecular Biology, Jagiellonian University, Krakow, Poland2

Received 29 January 1999/Returned for modification 23 March 1999/Accepted 7 April 1999

The initiation and progression of adult-onset periodontitis has been associated with infection of the gingival sulcus by Porphyromonas gingivalis. This organism utilizes a multitude of virulence factors to evade host defenses as it establishes itself as one of the predominant pathogens in periodontal pockets. A feature common to many other oral pathogens is the production of ammonia due to its protective effect during acidic cleansing cycles in the mouth. Additionally, ammonia production by P. gingivalis has been proposed as a virulence factor due to its negative effects on neutrophil function. In this study, we describe the first purification of a peptidylarginine deiminase (PAD) from a prokaryote. PAD exhibits biochemical characteristics and properties that suggest that it may be a virulence agent. PAD deiminates the guanidino group of carboxyl-terminal arginine residues on a variety of peptides, including the vasoregulatory peptide-hormone bradykinin, to yield ammonia and a citrulline residue. The soluble protein has an apparent mass of 46 kDa, while the DNA sequence predicts a full-length protein of 61.7 kDa. PAD is optimally active at 55°C, stable at low pH, and shows the greatest activity above pH 9.0. Interestingly, in the presence of stabilizing factors, PAD is resistant to limited proteolysis and retains significant activity after short-term boiling. We propose that PAD, acting in concert with arginine-specific proteinases from P. gingivalis, promotes the growth of the pathogen in the periodontal pocket, initially by enhancing its survivability and then by assisting the organism in its circumvention of host humoral defenses.

* Corresponding author. Mailing address: Dept. of Biochemistry and Molecular Biology, The University of Georgia, Athens, GA 30602. Phone: (706) 542-1713. Fax: (706) 542-3719. E-mail: jtravis{at}arches.uga.edu.

Infection and Immunity, July 1999, p. 3248-3256, Vol. 67, No. 7
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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