title: Analysis of cultivable Porphyromonas gingivalis with trypsin-like protease enzyme activity and serum antibodies in chronic adult periodontitis.
abstract: OBJECTIVE
  Trypsin-like protease (TLPase) enzyme produced by Porphyromonas gingivalis has been implicated as a virulence factor in the pathogenesis of periodontal disease. The aims of this study were to investigate the relationship between cultivable P. gingivalis, TLPase enzyme activity (BANA hydrolysis) and serum antibody levels against cell sonicate and a purified TLPase antigen from P. gingivalis W50.
  
  
  METHODS
  Sub-gingival plaque samples were cultured for levels of P. gingivalis together with a chairside analysis of TLPase enzyme activity (Perioscan) from periodontitis and gingivitis sites of adult periodontitis patients. A TLPase from P. gingivalis was purified by gel filtration and ion exchange chromatography from the vesicle fraction for use as a test antigen.
  
  
  RESULTS
  Elevated levels of P. gingivalis were found at periodontitis sites, however, there was no correlation with sub-gingival plaque TLPase enzyme activity. Adult periodontitis patients had higher levels of IgG and IgA against cell sonicate and TLPase antigens than did controls. Those patients who were P. gingivalis culture-positive demonstrated an elevated immune response against both cell sonicate and TLPase when compared to P. gingivalis culture-negative patients. Treatment resulted in an improvement of clinical indices and no cultivable P. gingivalis could be recovered from the treated sites and there was a concomitant decrease in IgG levels against the TLPase. There was no significant difference in BANA hydrolysis at gingivitis sites or periodontitis sites after treatment.
  
  
  CONCLUSIONS
  Further longitudinal studies are suggested to investigate the role of the TLPase in the response to treatment of chronic adult periodontitis patients.
authors.affiliation: Department of Adult Dental Care, Glasgow Dental School, United Kingdom.
authors.forename: A J
authors.initials: AJ
authors.lastname: Smith
authors.forename: W G
authors.initials: WG
authors.lastname: Wade
authors.forename: J
authors.initials: J
authors.lastname: Greenman
authors.forename: M
authors.initials: M
authors.lastname: Addy
mesh_terms: D000328:Adult; D000907:Antibodies, Bacterial / Q000097:blood / Q000276:immunology; D000942:Antigens, Bacterial / Q000276:immunology; D001426:Bacterial Proteins; D001587:Benzoylarginine-2-Naphthylamide; D016009:Chi-Square Distribution; D002908:Chronic Disease; D003430:Cross-Sectional Studies; D003546:Cysteine Endopeptidases; D003773:Dental Plaque / Q000201:enzymology / Q000382:microbiology; D005260:Female; D005891:Gingivitis / Q000201:enzymology / Q000276:immunology / Q000382:microbiology; D006801:Humans; D007070:Immunoglobulin A / Q000097:blood; D007074:Immunoglobulin G / Q000097:blood; D007075:Immunoglobulin M / Q000097:blood; D008297:Male; D010512:Periodontal Index; D010518:Periodontitis / Q000201:enzymology / Q000276:immunology / Q000382:microbiology*; D016966:Porphyromonas gingivalis / Q000201:enzymology* / Q000276:immunology / Q000472:pathogenicity; D018709:Statistics, Nonparametric; D014357:Trypsin / Q000032:analysis* / Q000378:metabolism
chemical_list: D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D007070:Immunoglobulin A; D007074:Immunoglobulin G; D007075:Immunoglobulin M; D001587:Benzoylarginine-2-Naphthylamide; D014357:Trypsin; D003546:Cysteine Endopeptidases; C078912:prtT protein, Porphyromonas gingivalis