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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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PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease
Vossenaar, E. R., Zendman, A. J. W., VENROOIJ, W. J. V., & Pruijn, G. J. M. (2003) · BioEssays · doi:10.1002/bies.10357 · Cited by 986
“To date only a single prokaryotic enzyme that can citrullinate proteins has been identified, in Porphyromonas gingivalis.((8)) This enzyme (AAF06719), however, is not evolutionarily related to the vertebrate PAD enzymes, can convert both peptidylarginine and free L-arginine, is not dependent on Ca2þ and shares sequenc…”
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“While the association between periodontitis and RA development was recognized as early as the 19th century [11], recent studies have demonstrated that infections with the common periodontal bacterium Porphyromonas gingivalis can result in the induction of autoimmune responses via the citrullination of host peptides [2…”
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Wegner, N., Wait, R., Sroka, A., Eick, S., Nguyen, K.-A. T., Lundberg, K., Kinloch, A., Culshaw, S., Potempa, J., & Venables, P. J. (2010) · Arthritis & Rheumatism · doi:10.1002/art.27552 · Cited by 690
“The unique nature of the bacterial deiminase, along with its location on the cellsurface of the bacterium (26), provides a target for treatment designed to prevent this otherwise incurable disease.”
BackgroundInfluentialSelf-citation
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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