The relationship of serum IgG antibody titers to periodontal pathogens to indicators of the host response in crevicular fluid

Abstract

Lamster IB, Celenti R and Ebersole JL: The relationship of serum IgG antibody titers to periodontal pathogens to indicators of the host response in crevicular fluid. J Clin Periodontol 1990: 17: 419^25. Abstract. In this study, the relationship of indicators of the local host response in gingival crevicular fluid (GCF) to the serum antibody titer to periodontal pathogens was examined. 15 patients with chronic adult periodontitis were studied, GCF was collected and analyzed for the total amount of IgG, IgM, the lysosomal enzyme B-glucuronidase (BG) and a-2-macroglobuIin (a2M). At the same examination, serum from these patients was collected, and enzyme-linked immunosorbent assays used to determine the serum IgG antibody titer to a panel of 17 periodontal pathogens (Actinobaeillus aelinomycetemcomitans (3 strains), Bacterotdcs gingivalis (4), Eikenella corrodens (2), Wolinella reeta. Bacteroides intermedius (3), Fusobacterium nucleatum, and 3 Capnoeytophaga species). Using Spearman rank order correlation analysis, correlation coefficients were calculated to relate the 4 indicators of host response in GCF to the serum IgG antibody titer to each of the 17 micro-organisms. The mean correlation between total IgG in GCF and the serum IgG antibody titer was positive (r= +0.30), and statistically significant correlations between total IgG in GCF and serum IgG antibody titer were observed for one strain of B. intermedius and C. oehraeea. A weaker positive correlation was observed for IgM {r = 0,\%). In contrast, the mean correlation between total BG in GCF and the serum antibody titer was negative (r = -0.34). Statistically significant negative correlations were observed for all 3 strains of A. actinomycetemcomitans. one strain of E. corrodens and W. recta. The mean correlation for a2M was r= -0.06. These data suggest that elevated BG activity in GCF, believed to be a marker for lysosomal enzyme released from polymorphonuclear leukocytes in the crevicular environment, may be associated with a reduced serum IgG antibody response to suspected periodontal pathogens. Furthermore, these findings imply that the development of a serum IgG antibody response to suspected periodontal pathogens is consistent with a protective host response.

Host‐derived diagnostic markers for periodontitis: do they exist in gingival crevice fluid?

“…(94) showed a predictive value of > 80% for beta‐glucuronidase in relation to clinical attachment loss. Interestingly, this enzyme showed a negative correlation with serum antibody titers to several periodontal pathogens, indicating that higher antibody titers protect against periodontal breakdown (92). However, later studies have concluded that, in general, beta‐glucuronidase is strongly related to the severity and the inflammatory state of periodontal disease and is thus not per se predictive (53, 174).…”

Immunoglobulin G subclass antibody profiles in Porphyromonas gingivalis‐associated aggressive and chronic periodontitis patients

“…We previously reported that Porphyromonas gingivalis , which is one of the periodontopathic bacteria, was frequently detected in aggressive periodontitis (AgP) and chronic periodontitis (CP) patients in the Japanese population (47). While immunoglobulin G (IgG) is a major immunoglobulin of human serum, the IgG antibody response to P. gingivalis antigens has been considered beneficial for the control of P. gingivalis ‐mediated periodontitis (5, 12, 13, 24, 41). However, no clear correlation has been shown between IgG antibody levels and severity of disease (3).…”

Porphyromonas gingivalis induction of mediator and cytokine secretion by human gingival fibroblasts

“…Various investigators have attempted to correlate these molecules with initiation, risk and progression of periodontal disease. Among the molecules of interest are prostaglandin E 2 , interleukin‐1β, IL‐6, IL‐8, leukotriene B 4 , thromboxane B 2 , tumor necrosis factor α, monocyte chemoattractant protein‐1 and various other enzymes and acute phase proteins ( 1, 29, 31).…”