Human serum precipitins to human dental plaque and oral bacteria

doi:10.1016/0003-9969(81)90080-7

Archives of Oral Biology

Volume 26, Issue 2, 1981, Pages 117-122

https://doi.org/10.1016/0003-9969(81)90080-7 Get rights and content

Abstract

Naturally occurring precipitins with 2 different specificities were found in 45 per cent of human sera from male and female subjects whose average age was 24.6 yr. One specificity was for a factor from Actinomyces species and strains (A⁺) and the other for a factor from streptococci, staphylococci and lactobacilli (S⁺). Serologically identical factors were found in soluble extracts of dental plaque. The S, but not the A factor, was rendered inactive by treatment with mild alkali. The serum precipitins, uncharged at pH 8.2, were four times less reactive after IgG had been removed with Staphylococcal Protein A.

References (39)

D.A. Berkenbilt et al.
Development of antibodies to cariogenic streptococci in children
J. Am. dent. Ass.
(1971)
P. Grabar et al.
A method for combining the electrophoretic and immunochemical properties in the study of a mixture of proteins. Application to blood serum
Biochim. biophys. Acta
(1953)
A.E. Kennedy et al.
Antibodies to cariogenic streptococci in humans
Archs oral Biol.
(1968)
M. Levine et al.
Variation in the cytotoxic activities of human dental plaque
Archs oral Biol.
(1978)
W.H. Bowen
Relevance of caries vaccine investigations in rodents, primates and humans: critical assessment
D. Bratthall
Serological studies on Sptococcus mutans
Odont. Revy
(1970)
S.J. Challacombe et al.
Serum and salivary antibodies to cariogenic bacteria in man
J. dent. Res.
(1976)
H.R. Cooper et al.
Lipid-free glycerol teichoic acids with potent membranebinding activity
Infect. Immun.
(1978)
J.J. Ferretti et al.
Susceptibility of Streptococcus mutans to antimicrobial agents
Antimicrob. Ag. Chemother.
(1976)
A. Forsgren et al.
Many bacterial species bind human Ig D
J. Immun.
(1979)

A. Grubb

Analysis of the immunochemical relationship between antigens by electrophoresis in agarose gels containing antibodies

Scand. J. clin. Lab. Invest.

(1972)

C.V. Holdeman et al.

J. Huis in't Veld et al.

Antibodies against Streptococcus mutans and glucosyl transferases in caries-free and caries active military recruits

Adv. exp. Med. Biol.

(1977)

R. Joseph et al.

Synthesis and excretion of glycerol teichoic acid during growth of two streptococcal species

Infect. Immun.

(1975)

P.H. Klesius et al.

Human antibody response tc group A streptococcal teichoic acid

Can. J. Microbiol.

(1974)

K.W. Knox et al.

Immunologica properties of teichoic acids

Bact. Rev.

(1973)

J. Kroll

Tandem-crossed immuno electrophoresis

Scand. J. Immun.

(1973)

G. Kronvail et al.

Differences in anti-protein A activity among IgG subgroups

J. Immun.

(1969)

C.B. Laurell

Electroimmuno assay

Scand. J. clin. Lab. Invest.

(1972)

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Analysis of the specificity of natural human antibody reactive to Actinomyces
1986, Molecular Immunology
The specificity of a frequently-occurring precipitin response to soluble antigens from cell-walls and culture filtrates of A. viscosus ATCC 19246 was examined. After precipitation with isopropanol (50–75% v/v), antigen fractions of different charge and molecular weight were isolated by ion exchange and gel filtration. When heated in mineral acid or alkali above 0.15 M, each of the purified antigens lost precipitating activity, but now inhibited the precipitin reaction between serum and exogenous unheated antigen. The inhibitor was isolated over Biogel P30 and characterized as a peptide fragment (mol. wt about 2kd) containing approximately 50 moles of ornithine and 6–12 moles, respectively, of aspartate, serine, threonine, glutamate, glycine, alanine and histidine per 100 moles amino acids. The inhibitor was totally destroyed by heating for 1.0 hr in 2.0 M HC1. Variability in the number of fragments and differences in the non-antigenic portions probably accounted for the complexity of the antigens. Ornithine, putrescine, N-acetyl putrescine and various sugars had little or no effect on the precipitin reaction with intact antigen at high concentrations (200 mM), whereas the fragment inhibited completely at 0.4 mM. This indicates that neither ornithine nor its side-chain amides are exclusively recognized by antibody. However, ornithine may be part of a larger sequence and/or important in forming the configuration recognized by the human antibodies.
Human serum precipitins to oral bacteria related to dental caries
1984, Archives of Oral Biology
Adults aged 20–38 years were classified by a postive (+) or negative (−) precipitating serum antibody response to d-alanyl glycerol teichoic acid (S), or an antigen from Actinomyces spp. (A). Culture filtrates of Streptococcus mutans and Actinomyces viscosus were used to detect the respective specific antibodies by immunoelectrophoresis and immunodiffusion when present in serum at a concentration of more than 0.05 mg/ml. Among subjects who had grown up in fluoridated areas, A⁺ subjects exhibited significantly fewer decayed, missing and filled teeth or teeth surfaces compared to A⁻ subjects (p < 0.02). For the whole population examined, caries severity increased with age and decreased with length of residence in a fluoridated area (p < 0.01). When classified by A and S antibody response, only S⁻ subjects showed a significant increase in caries score with age (p < 0.02) and only A⁺ S⁺ subjects a significant decrease in score with length of exposure to fluoridated water (p < 0.05). It is concluded that the severity of caries in relation to age and fluoride exposure may differ in subjects with the different antibody specificities.
Natural antibodies in man to a protein antigen from the bacterium Streptococcus mutans related to dental caries experience
1984, Archives of Oral Biology
Serum antibodies to a cell-wall protein antigen derived from Streptococcus mutans (SA I/II) were examined, in 108 subjects by a solid-phase radioimmunoassay. As a control, antibodies to lipoteichoic acid and to Strep. mutans whole cells were examined and the relationship to dental caries of isotype-specific antibodies to both antigens determined. Serum-IgG antibodies to SA I/II and to Strep. mutans were significantly greater in subjects of low caries experience than in subjects of high caries experience, whereas serum-IgG antibodies to LTA showed no relationship. Serum-IgM antibodies to SA I/II were depressed in subjects with carious lesions, whereas IgM antibodies to Strep. mutans in the same subjects were raised. IgA antibodies against any antigen were not related to caries.
Serum antibodies of each isotype to SA I/II were generally positively-correlated with antibodies to LTA but inhibition experiments demonstrated specificity of antibodies for each antigen. The relationship between antibodies to SA I/II and dental caries are consistent with those reported with antibodies to whole cells of Strep. mutans and suggest that high-serum IgG antibodies to SA I/II may be associated with protection against dental caries in man.
Naturally occurring human serum precipitins specific for d-alanyl esters of glycerol teichoic acid
1982, Molecular Immunology
An antigen common to various oral bacteria and to which precipitating IgG is present in about 30% of young adult human sera was obtained from culture filtrates of Streptococcus mutans GS-5 and detected by electroimmunoassay as described elsewhere. The antigen was isolated by gel filtration, affinity chromatography with Sephacryl and finally passed through a strong anion exchange gel (AGMPI) to give a major peak (S₁) and a long tail (S₂ and S₃). These three preparations, yielding about 10% of the starting antigen activity, were composed of protein, fatty acids, sugar, glycerol and phosphate. Glycerol and phosphate accounted for 26% of the dry weight of the S₁-preparation and in all preparations were in an approximately 1:1 molar ratio typical of glycerol teichoic acid. The S₁-fraction had a greater sugar and fatty acid content and a different amino acid composition compared to the S₂- and S₃-preparations which were similar in these respects. On exposure to pH 8.0 buffer, the precipitin activity disappeared and this was accompanied by a loss of alanine. Shorter exposure to the pH 8.0 buffer caused a slightly increased electrophoretic mobility compared to non-alkali-exposed antigen and a lesser loss of alanine. Hapten precipitin inhibition assays indicated that d-alanine and d-alanyl ethyl ester inhibited the reaction much more effectively than l-alanyl ethyl ester, l-alanine, or d- or l-glutamine. These human sera are thus specific for d-alanyl esters of glycerol teichoic acid. Two possible structures bearing the antigenic determinant are described.
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2021, Journal of Clinical Medicine
The family Actinomycetaceae
2014, The Prokaryotes: Actinobacteria

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Human serum precipitins to human dental plaque and oral bacteria

Abstract

J. Am. dent. Ass.

Biochim. biophys. Acta

Archs oral Biol.

Archs oral Biol.

Relevance of caries vaccine investigations in rodents, primates and humans: critical assessment

Serological studies on Sptococcus mutans

Odont. Revy

Serum and salivary antibodies to cariogenic bacteria in man

J. dent. Res.

Lipid-free glycerol teichoic acids with potent membranebinding activity

Infect. Immun.

Susceptibility of Streptococcus mutans to antimicrobial agents

Antimicrob. Ag. Chemother.

Many bacterial species bind human Ig D

J. Immun.

Analysis of the immunochemical relationship between antigens by electrophoresis in agarose gels containing antibodies

Scand. J. clin. Lab. Invest.

Antibodies against Streptococcus mutans and glucosyl transferases in caries-free and caries active military recruits

Adv. exp. Med. Biol.

Synthesis and excretion of glycerol teichoic acid during growth of two streptococcal species

Infect. Immun.

Human antibody response tc group A streptococcal teichoic acid

Can. J. Microbiol.

Immunologica properties of teichoic acids

Bact. Rev.

Tandem-crossed immuno electrophoresis

Scand. J. Immun.

Differences in anti-protein A activity among IgG subgroups

J. Immun.

Electroimmuno assay

Scand. J. clin. Lab. Invest.