<i>Porphyromonas gingivalis</i>: Presence of a Species-specific Antigen which is Discriminatory in Chronic Inflammatory Adult Periodontal Disease

Duncan, Alexander; Carman, Robert J.; Harper, Fiona; Griffiths, Gareth; Curtis, Michael A.

doi:10.3402/mehd.v5i1.7762

Microbial Ecology in Health & Disease

1992

DOI: 10.3402/mehd.v5i1.7762

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Porphyromonas gingivalis: Presence of a Species-specific Antigen which is Discriminatory in Chronic Inflammatory Adult Periodontal Disease

Alexander Duncan

Robert J. Carman

Fiona Harper

et al.

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Cited by 3 publications

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“…Initially, the IgG antibody response to soluble and outer membrane preparations of this organism was determined in sera from a case-control study of adult periodontal disease, and a number of discriminatory surface antigens were identified (7). One of these antigens, with an M r of ϳ50,000, is readily released from the cell surfaces of all P. gingivalis strains examined to date but is absent from type and reference strains of other related oral and intestinal anaerobic bacteria (10) and thus satisfies some of the criteria needed for a model antigen.…”

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Characterization, genetic analysis, and expression of a protease antigen (PrpRI) of Porphyromonas gingivalis W50

et al. 1995

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Previous studies of the serum immunoglobulin G antibody response of periodontal patients have demonstrated significant reactivity to a cell surface or extracellular arginine-specific protease of Porphyromonas gingivalis which migrates as an ϳ50-kDa band on sodium dodecyl sulfate-polyacrylamide gels. In the present report, two forms of the enzyme (ArgI and ArgIA) with this electrophoretic behavior were isolated. ArgI is a heterodimer of ␣ and ␤ subunits, and ArgIA is a monomer composed of the catalytically active ␣ component alone. The gene encoding ArgI (prpR1 encoding protease polyprotein ArgI) was cloned from Sau3AI digests of P. gingivalis W50 DNA into pUC18. Sequence analysis demonstrated that the ␣ and ␤ components are contiguous on the initial translation product and are flanked by large N-and C-terminal extensions. prpR1 is 97.5% identical to the rgp-1 gene from P. gingivalis H66. prpR1 expression in Escherichia coli demonstrated the presence of an internal transcription-translation initiation site which could permit independent expression of different regions of the polyprotein. Immunochemical analysis of P. gingivalis mid-logarithmic-phase cultures suggested that the processing of PrpRI may be closely coupled to its synthesis, with only the final stages taking place at the cell surface. Southern hybridization studies demonstrated that the prpR1 gene is widely distributed in other P. gingivalis strains and that a second homologous locus to the ␣ component and at least two other homologous loci to the ␤ component are present on the P. gingivalis chromosome. These data indicate that the ArgI protease of P. gingivalis is a member of a family of sequence-related gene products which may share both functional and antigenic properties.

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confidence: 99%

Characterization, genetic analysis, and expression of a protease antigen (PrpRI) of Porphyromonas gingivalis W50

et al. 1995

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Identification of Photolabile Outer Membrane Proteins of Porphyromonas gingivalis

Bhatti

Nair

MacRobert

et al. 2001

Current Microbiology

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As the prevalence of antibiotic-resistant strains of bacteria increases, novel ways of treating infections need to be developed. This is particularly pertinent with respect to the periodontal diseases--the most common chronic bacterial infections of man. The use of a photosensitizer in combination with red light has been demonstrated to be effective in killing several human pathogens, including the oral bacterium, Porphyromonas gingivalis, a major pathogen in periodontitis. Killing was associated with alterations in the molecular masses of several outer membrane and plasma membrane proteins and these may be therapeutic targets for photodynamic therapy and other antimicrobial approaches. To identify these photolabile proteins, we have used a panel of monoclonal antibodies raised to whole P. gingivalis. A number of the antibodies recognized various photolabile proteins. Using a combination of Western blotting and protein sequencing the predominant photolabile proteins in P. gingivalis have been identified as the major secreted/cell surface proteases--Lys and Arg gingipain.

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Periodontal Diseases: Microbial Factors

1996

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Ann Periodontal 1996;1:879-925. Annals of PeriodontologyReview: Periodontai Diseases: Microbial Factors become clear over the past several years that A. actinomycetemcomitans can cause periodontai disease. There are a group of periodontai microorganisms for which such extensive and convincing data exist that they are considered to be etiologic agents in Periodontitis. These include A. actinomycetemcomitans, Bacteroides forsythus, and P. gingivalis. There have been, in fact, propos-

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Porphyromonas gingivalis: Presence of a Species-specific Antigen which is Discriminatory in Chronic Inflammatory Adult Periodontal Disease

Cited by 3 publications

References 19 publications

Characterization, genetic analysis, and expression of a protease antigen (PrpRI) of Porphyromonas gingivalis W50

Characterization, genetic analysis, and expression of a protease antigen (PrpRI) of Porphyromonas gingivalis W50

Identification of Photolabile Outer Membrane Proteins of Porphyromonas gingivalis

Periodontal Diseases: Microbial Factors

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