Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0031099 (periodontitis)
 12,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Campylobacter rectus is one of the predominant bacteria in the lesions of human periodontitis. The surface antigens of the bacterium contain several components which may play significant roles in colonization and pathogenesis. A high-molecular-weight protein was selectively isolated from the cell surface of C. rectus by acid extraction and purified by DEAE Sepharose. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed that the extracted protein was 150 kDa. The protein was not found in Campylobacter curvus ATCC 35224 or Wolinella succinogenes ATCC 29543. Lipopolysaccharide (LPS) was extracted from various C. rectus strains by the hot phenol-water method. SDS-PAGE patterns revealed that C. rectus LPS was the smooth type in nature. Monoclonal antibodies against C. rectus were generated by the fusion of SP2/0 myeloma cells with splenocytes from BALB/c mice immunized with whole cells of C. rectus ATCC 33238 strain. An Immunoglobulin G1 monoclonal antibody reacted with the high-molecular-weight proteins from 4 of 9 C. rectus strains, indicating that the 150 kDa protein exhibits antigenic heterogeneity. Immunoelectron microscopic study revealed that the monoclonal antibody recognized the S-layer of C. rectus cells. An IgM monoclonal antibody reacted with LPSs from C. rectus strains at molecular weights between approximately 20.0 kDa and 24.0 kDa. The monoclonal antibody did not react with any other LPSs from C. curvus ATCC 35224 or W. succinogenes ATCC 29543. The reactivities of this monoclonal antibody indicate that it recognizes an O-specific side chain epitope of C. rectus LPS. Sera from patients with adult periodontitis showed strong reactivity with the 150 kDa protein antigen and LPS from C. rectus strains. As determined by immunoblotting analysis, sera from periodontally healthy individuals, however, showed little or no reactivity. The levels of serum IgG antibodies of patients with periodontitis to the protein antigen and LPS were statistically significantly higher than those of periodontally healthy individuals, as assessed by an enzyme-linked immunosorbent assay.
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PMID:Analysis of cell surface antigens of Campylobacter rectus. 130 24

A high-molecular-weight (approximately 150,000) protein was selectively isolated by acid extraction from the cell surface of Wolinella recta and purified by negative adsorption on DEAE-cellulose and gel filtration. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed that this protein was found in W. recta but not in other Wolinella species, such as W. curva and W. succinogenes. Sera from patients with periodontitis reacted strongly with this protein antigen, whereas sera from healthy donors showed little or no reactivity, as determined by immunoblotting analysis. In serum, titers of immunoglobulin G antibodies to the protein antigen were significantly higher in patients with periodontitis than in periodontally healthy donors, as detected by an enzyme-linked immunosorbent assay.
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PMID:Cell surface protein antigen from Wolinella recta ATCC 33238T. 275 98

A protein was extracted from whole cells of Prevotella intermedia ATCC 25611 with sodium lauroylsarcosine and purified by chromatography on a DEAE-Sepharose fast-flow column. The The apparent molecular weight of the protein was 55,000. A mouse polyclonal antibody specific for the protein recognized the cell surface structure of P. intermedia and also reacted with proteins in lysates of other black-pigmented anaerobic bacteria, such as Porphyromonas endodontalis and Prevotella melaninogenica, but not with those in lysates of Porphyromonas gingivalis or with the purified fimbriae of P. gingivalis 381. The N-terminal sequence of the 55-kDa protein showed only low homology with the cell surface proteins of any black-pigmented bacteria reported to date. The level of immunoglobulin G antibody to the antigen was higher in the sera of patients with periodontitis than in the sera of healthy volunteers. The protein induced interleukin-1 alpha, -1 beta, -6, and -8 and tumor necrosis factor alpha in human peripheral blood mononuclear cell cultures and interleukin-1 beta and -6 in human umbilical vascular endothelial cell and gingival fibroblast cultures. The protein induced interleukin-6 and tumor necrosis factor alpha activities in peritoneal macrophages from C3H/HeJ as well as from C3H/HeN mice and also induced cytokine activities in the sera of both strains of mice primed with muramyldipeptide.
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PMID:Immunobiological activities of a 55-kilodalton cell surface protein of Prevotella intermedia ATCC 25611. 818 71

Oral Actinobacillus actinomycetemcomitans strains have been classified into five serotypes. The aim of this study was to determine the compositions of A. actinomycetemcomitans serotype d- and e- specific antigens. The serodistribution of clinical isolates from the patients with periodontitis were also investigated. Serotype-specific polysaccharide antigens of A. actinomycetemcomitans IDH 781 (serotype d) and OMZ 534 (serotype e) were extracted from whole cells by autoclaving. The extracts were purified by chromatography on DEAE-Sepharose CL-6B and Sephacryl S-300HR columns. The serotype d antigen was composed of rhamnose (17.1%), mannose (45.5%), galactose (2.0%) and glucose (35.5%). On the other hand, the serotype e antigen was composed of rhamnose (23.9%), mannose (29.1%), galactose (11.0%), glucose (13.5%) and unidentified sugar (22.5%). Immunodiffusion tests revealed that the purified polysaccharide antigen form a single precipitin line with the corresponding rabbit antiserum. A total of 157 A. actinomycetemcomitans clinical isolates from diseased sites of 39 patients with periodontitis were serotyped by using serotype-specific rabbit antisera against A. actinomycetemcomitans serotype a, b, c, d and e strains. In the immunodiffusion assay, the autoclaved extracts of 42, 12, 34, 8 and 41 A. actinomycetemcomitans clinical isolates reacted with serotype a, b, c, d and e antisera, respectively. These findings indicate that the extraction of serotype antigens by autoclaving is useful and definite for the serotyping of A. actinomycetemcomitans clinical isolates.
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PMID:[Purification of serotype d-- and e--specific antigens from Actinobacillus actinomycetemcomitans and seroclassification of clinical isolates from periodontal patients]. 872 65