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Purification, Characterization, and Sequence Analysis of a Potential Virulence Factor from Porphyromonas gingivalis , Peptidylarginine Deiminase
Open accessAbstract
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.
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“Citrullination of arginine occurs via the action of peptidyl arginine deiminase, an enzyme found in both humans and P gingivalis.211”
From The oral microbiome: Role of key organisms and complex networks in oral health and disease (2021) · cites this paper as [211]
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Metadata
- Authors
- McGraw, W. T., Potempa, J., Farley, D., & Travis, J.
- Affiliations
- University of Georgia (US)
- Jagiellonian University (PL)
- <!--label omitted: 3-->Department of Arthritis Biology, Novartis Pharmaceuticals, Summit, New Jersey 07901,3 and
- Venue
- Infection and Immunity
- Publisher
- American Society for Microbiology
- Published
- 1999-07
- Volume
- 67
- Issue
- 7
- Pages
- 3248-3256
- ISSN
- 0019-9567 (ISSN-L)
- 1098-5522
- PMC
- PMC116503
- OpenAlex
- W1943338444
- Cited by
- 378
- References
- 47
- Citations by year
- 2026: 9 · 2025: 13 · 2024: 12 · 2023: 15 · 2022: 19 · 2021: 15 · 2020: 16 · 2019: 30 · 2018: 24 · 2017: 37 · 2016: 26 · 2015: 28 · 2014: 22 · 2013: 27 · 2012: 20
- FWCI
- 1.60
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Infection and Immunity (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Dentistry › Periodontics › Oral microbiology and periodontitis research
- Health Sciences › Dentistry › Periodontics › Oral and gingival health research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
- Keywords
- Porphyromonas gingivalis, peptidylarginine deiminase, virulence factors, periodontitis, ammonia synthesis, bradykinin, citrullination, protein purification, protein stability, host defense evasion, periodontal pockets
- MeSH terms
- Protein-Arginine Deiminases, Protein-Arginine Deiminase Type 4, Amino Acid Sequence, Base Sequence, Enzyme Activation, Humans, Hydrolases, Molecular Sequence Data, Periodontitis, Virulence, Bacteroidaceae Infections, Porphyromonas gingivalis, Sequence Analysis
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