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Infection and Immunity, March 2004, p. 1374-1382, Vol. 72, No. 3
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.3.1374-1382.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Humoral Responses to Porphyromonas gingivalis Gingipain Adhesin Domains in Subjects with Chronic Periodontitis

Ky-Anh Nguyen,1,2* Arthur A. DeCarlo,2,3 Mayuri Paramaesvaran,1 Charles A. Collyer,4 David B. Langley,4 and Neil Hunter1

Institute of Dental Research, Westmead Centre for Oral Health,1 United Dental Hospital,2 School of Molecular and Microbial Biosciences, University of Sydney, Sydney, New South Wales, Australia,4 NSU Dental, Nova Southeastern University, Ft. Lauderdale, Florida3

Received 22 July 2003/ Returned for modification 9 September 2003/ Accepted 26 November 2003

The gingipains have been implicated in the pathogenicity of Porphyromonas gingivalis, a major etiologic agent of chronic periodontitis. Mature gingipains often present as a membrane-bound glycosylated proteinase-adhesin complex comprising multiple adhesin domains (HA1 to -4) and a catalytic domain. Using recombinant adhesin domains, we were able to show that patients with chronic periodontitis produce significantly more immunoglobulin G reactive with gingipain domains than a corresponding group with healthy periodontium. Titers were predominantly directed toward the carbohydrate epitopes shared between the gingipains and the lipopolysaccharide of P. gingivalis with little recognition of the peptide backbone of the catalytic domains. Distribution of titers to peptide epitopes of the adhesin domains was as follows: HA4 {approx} HA1 > HA3 >> HA2. No correlation was observed between markers of disease severity and titers to individual adhesins within the disease group. Posttreatment titers showed no change or a decrease in titers for the majority of patients except for titers to the HA2 domain which showed marked increases in a few responding patients. Since the HA2 domain is important in hemoglobin binding and acquisition of essential porphyrin, boosting titers of antibodies to this domain may have the potential to control the growth of this organism.

* Corresponding author. Mailing address: Institute of Dental Research, Westmead Centre for Oral Health, P.O. Box 533, Wentworthville, NSW 2145, Australia. Phone: (61) 2-9845-8764. Fax: (61) 2-9845-7599. E-mail: kyanhn{at}dental.wsahs.nsw.gov.au.

Editor: V. J. DiRita

Infection and Immunity, March 2004, p. 1374-1382, Vol. 72, No. 3
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.3.1374-1382.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Tam, V., O'Brien-Simpson, N. M., Pathirana, R. D., Frazer, L. T., Reynolds, E. C. (2008). Characterization of T Cell Responses to the RgpA-Kgp Proteinase-Adhesin Complexes of Porphyromonas gingivalis in BALB/c Mice. J. Immunol. 181: 4150-4158 [Abstract] [Full Text]  


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