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PubMed1983

Microcapsule agglutination test for Treponema pallidum antibodies. A new serodiagnostic test for syphilis.

For the serodiagnosis of syphilis a quantitative passive agglutination (MCA-TP) test for antibodies to Treponema pallidum was performed with chemically stable microcapsules with no antigenic activity instead of with conventional sheep erythrocytes. The microcapsules were easily sensitised with the antigen of sonicated Treponema pallidum by treatment with glutaraldehyde. Compared with the Treponema pallidum haemagglutination test (TPHA) the MCA-TP test was superior for detecting cases of primary syphilis. Furthermore, the decrease in antibody titre during treatment was more evident in this test than in the FTA-ABS or the TPHA tests. The MCA-TP test performed on IgM and IgG gel-filtered fractions of sera from patients with syphilis proved that the sensitised microcapsule antigen reacted sharply with the IgM antibodies specific to syphilis.

Agglutination Tests↗

PubMed1983

Estimation of the local production of antibodies to Treponema pallidum in the central nervous system of patients with neurosyphilis.

In 76% of 149 patients with neurosyphilis local production of treponema-specific IgG antibodies in the central nervous system (CNS) was determined by estimating the cerebrospinal fluid (CSF)-to-serum ratio of TPHA-IgG titre per mg total IgG. With this formula synthesis of treponema-specific IgG antibodies in the CNS could be detected independently of the function of the blood-CSF barrier. A selective increase of total IgG in the CSF was not found in all cases. Forty-three patients with adequately treated or spontaneously resolved syphilis without clinical evidence of involvement of the CNS by Treponema pallidum served as controls.

Albumins↗

PubMed1987

Interactions between Treponema bryantii and cellulolytic bacteria in the in vitro degradation of straw cellulose.

To assess the contribution of individual bacterial species to the overall process of cellulose digestion in the rumen, cellulolytic bacteria (Bacteroides succinogenes and Ruminococcus albus) were tested as pure cultures and as cocultures with noncellulolytic Treponema bryantii. In studies of in vitro barley straw digestion, Treponema cocultures surpassed pure cultures of the cellulolytic organisms in dry matter disappearance, volatile fatty acid generation, and in the production of succinic acid, lactic acid, and ethanol. Morphological examination, by electron microscopy, showed that cells of T. bryantii associate with the plant cell wall materials in straw, but that cellulose digestion occurs only when these organisms are present with cellulolytic species such as B. succinogenes. These results show that cellulolytic bacteria interact with noncellulolytic Treponema to promote the digestion of cellulosic materials.

Animals↗

PubMed2006

[Expression and purification of membrane immunogens of Treponema pallidum in Pichia pastoris].

Genes of Treponema pallidum subsp. pallidum three membrane antigens (47kDa, 17kDa and 15kDa) were amplified by PCR with the template of the genomic DNA of Nichols strain and cloned into plasmid pPICZ B, the recombinant plasmids of pTP47, pTP17 and pTP15 were transformed into Pichia pastoris GS115. Recombinant antigens were expressed by the methanol induction and confirmed by the Western blot assay. Fusion antigens with 6 x His tag were purified using Ni-NTA agarose, and purified fusion protein yields were 4.8mg/L, 6.6mg/L and 25mg/L of cell culture for His-TP15, His-TP17 and His-TP47, respectively. Purity of all three antigens were more than 96% by SDS-PAGE assay. Particularly, His-TP17 was more about 6kDa molecular weight than that of expected probably because of glycosylation in Pichia pastoris. At last, these recombinant antigens were evaluated by ELISA assay with serum from syphilis patient and healthy blood donors, all three antigens showed strong sensitivity and specificity. So three membrane antigens of Treponema pallidum were expressed and purified fused with 6 x His tag in Pichia pastoris for the first time. The immunoreactivity results showed that all of which can be applied to diagnosis of Treponema pallidum, especially to diagnosis method based on combined two or three antigens.

Antigens, Bacterial↗

PubMed1988

Ultrastructural and electrophoretic analysis of Treponema hyodysenteriae axial filaments.

Axial filaments of Treponema hyodysenteriae were purified and examined by transmission electron microscopy. The size and fine structure of the filaments were similar to those of Treponema zuelzerae and Treponema phagedenis biotype reiterii. Filaments were dissociated by heat and 2-mercaptoethanol and examined by polyacrylamide-gel electrophoresis. Six protein bands were evident, with approximate molecular weights of 39,000, 29,000, 27,000, 22,000, 21,000, and 18,500 daltons. All the proteins reacted with T hyodysenteriae and T innocens rabbit antisera, using the immunoblot technique.

Animals↗

PubMedDate not supplied

[Extraction of the soluble protein fraction from Treponema Reiter for use as antigen in syphilis serodiagnosis].

The present paper reports on two methods for extraction of the protein antigen from Treponema Reiter and shows the chemical and immunochemical characteristics of the extracts. Serologic testing of 1810 sera from syphilitic patients in various stages of the disease, from healthy subjects and from subjects with a false positive reaction to lipoid antigens, showed the value of the Reiter antigen to be equal to the cardiolipin antigens and those prepared from pathogenic Treponema. It is recommended to associate this antigen, in view of its qualities, to the cardiolipin tests used in the serodiagnosis of syphilis, especially in the laboratories that do not currently apply other treponema tests.

Antigens↗

PubMed1963

MORPHOLOGY OF TREPONEMA MICRODENTIUM AS REVEALED BY ELECTRON MICROSCOPY OF ULTRATHIN SECTIONS.

Listgarten, M. A. (Harvard School of Dental Medicine and Forsyth Dental Infirmary, Boston, Mass.), W. J. Loesche, and S. S. Socransky. Morphology of Treponema microdentium as revealed by electron microscopy of ultrathin sections. J. Bacteriol. 85:932-939. 1963.-Broth cultures of a strain of Treponema microdentium were harvested on Millipore filters, fixed in osmic acid, and sectioned for electron microscopy. The sections revealed that the spirochetes had an axial filament, made up of two fibrils approximately 150 A in diameter, which was situated between an external envelope approximately 140 A in thickness and a protoplasmic cylinder. The protoplasmic cylinder had a cross-sectional diameter of 100 to 200 mmu, and was surrounded by a double "membrane" consisting of two 40-A electron-dense structures separated by a 45-A space. Cross-sections of spirochetal "granules" revealed that the limiting membrane was continuous with the outer envelope of the spirochetes, and surrounded the protoplasmic cylinder and axial filament.

Cross-Sectional Studies↗

PubMed1964

DEPENDENCY OF TREPONEMA MICRODENTIUM ON OTHER ORAL ORGANISMS FOR ISOBUTYRATE, POLYAMINES, AND A CONTROLLED OXIDATION-REDUCTION POTENTIAL.

Socransky, S. S. (Forsyth Dental Center, Boston, Mass.), W. J. Loesche, C. Hubersak, and J. B. Macdonald. Dependency of Treponema microdentium on other oral organisms for isobutyrate, polyamines, and a controlled oxidation-reduction potential. J. Bacteriol. 88:200-209. 1964.-Strains of Treponema microdentium can be cultivated on a variety of autoclaved commercially available media in the presence of other oral organisms. Organisms supporting growth in these circumstances include a facultative diphtheroid accompanied by either a strain of Fusobacterium or a motile gram-negative anaerobic rod. Culture filtrates and lysates of these "supporting organisms" failed to substitute for growing organisms. Measurement of the oxidation-reduction potential of the test system demonstrated that the spirochetes grew in a narrow range of Eh (optimum, -190 mv). The supporting organisms could be replaced by their filtrates when the Eh of the medium was poised in this range by a combination of reducing agents. Both filtrates contained a heat-labile factor required by the spirochete, which could be replaced by 5 mug/ml of cocarboxylase. Isobutyric acid, which could be detected in the fusiform filtrate, and putrescine which could be detected in the diphtheroid filtrate, replaced the spirochete's remaining filtrate requirement. Maximal growth occurred when any of the following were incorporated into the medium: 2 mug/ml of sodium isobutyrate; 250 mug/ml of putrescine dihydrochloride; 200 mug/ml of spermidine phosphosphate, or 150 mug/ml of spermine tetrahydrochloride.

Amines↗

PubMed1992

A CAMP-like phenomenon in Serpulina (Treponema) spp.

A CAMP-like phenomenon was observed in 40 Serpulina (Treponema) isolates from the intestines of pigs, dogs, mice and rats. The strains examined included reference strains of the serotypes 1-4 of Serpulina (Treponema) hyodysenteriae and Serpulina (Treponema) innocens. The possible pathogenic importance of this phenomenon is discussed.

Animals↗

PubMed2004

A CDP-choline pathway for phosphatidylcholine biosynthesis in Treponema denticola.

The genomes of Treponema denticola and Treponema pallidum contain a gene, licCA, which is predicted to encode a fusion protein containing choline kinase and CTP:phosphocholine cytidylyltransferase activities. Because both organisms have been reported to contain phosphatidylcholine, this raises the possibility that they use a CDP-choline pathway for the biosynthesis of phosphatidylcholine. This report shows that phosphatidylcholine is a major phospholipid in T. denticola, accounting for 35-40% of total phospholipid. This organism readily incorporated [14C]choline into phosphatidylcholine, indicating the presence of a choline-dependent biosynthetic pathway. The licCA gene was cloned, and recombinant LicCA had choline kinase and CTP:phosphocholine cytidylyltransferase activity. The licCA gene was disrupted in T. denticola by erythromycin cassette mutagenesis, resulting in a viable mutant. This disruption completely blocked incorporation of either [14C]choline or 32Pi into phosphatidylcholine. The rate of production of another phospholipid in T. denticola, phosphatidylethanolamine, was elevated considerably in the licCA mutant, suggesting that the elevated level of this lipid compensated for the loss of phosphatidylcholine in the membranes. Thus it appears that T. denticola does contain a licCA-dependent CDP-choline pathway for phosphatidylcholine biosynthesis.

Amino Acid Sequence↗

PubMed2004

Comparison of the genome of the oral pathogen Treponema denticola with other spirochete genomes.

We present the complete 2,843,201-bp genome sequence of Treponema denticola (ATCC 35405) an oral spirochete associated with periodontal disease. Analysis of the T. denticola genome reveals factors mediating coaggregation, cell signaling, stress protection, and other competitive and cooperative measures, consistent with its pathogenic nature and lifestyle within the mixed-species environment of subgingival dental plaque. Comparisons with previously sequenced spirochete genomes revealed specific factors contributing to differences and similarities in spirochete physiology as well as pathogenic potential. The T. denticola genome is considerably larger in size than the genome of the related syphilis-causing spirochete Treponema pallidum. The differences in gene content appear to be attributable to a combination of three phenomena: genome reduction, lineage-specific expansions, and horizontal gene transfer. Genes lost due to reductive evolution appear to be largely involved in metabolism and transport, whereas some of the genes that have arisen due to lineage-specific expansions are implicated in various pathogenic interactions, and genes acquired via horizontal gene transfer are largely phage-related or of unknown function.

ATP-Binding Cassette Transporters↗

PubMed1984

Monoclonal antibody with hemagglutination, immobilization, and neutralization activities defines an immunodominant, 47,000 mol wt, surface-exposed immunogen of Treponema pallidum (Nichols).

Radioimmunoprecipitation (RIP) analyses performed on 125I-surface-labeled Treponema pallidum cells using various immune sera revealed the presence of six major surface antigens (immunogens) with apparent molecular weights of 47 K, 36 K, 34 K, 32 K, 29 K, and 13 K. Among these, the 47 K surface antigen was most abundant. Radioimmunoprecipitation assays using 125I-labeled T. phagedenis biotype Reiter or immunoblot analyses using the same strain, failed to reveal the presence of the 47 K mol wt antigen in the representative nonpathogenic treponeme. Preabsorption of anti-T. pallidum immune rabbit serum (IRS) with the Reiter organism did not remove anti-T. pallidum antibodies from immune serum that reacted with the 47 K mol wt immunogen or other immunogens of T. pallidum present in the characteristic antigenic profile. Monoclonal antibodies (mAb) directed specifically against the 47 K mol wt immunogen of T. pallidum also failed to react with an analogous 47 K mol wt component in Treponema phagedenis biotype Reiter, further suggesting the unique presence of this antigen in pathogenic treponemes. The presence of the 47 K mol wt surface immunogen in pathogenic treponemes other than T. pallidum subspecies pallidum was also observed (43). Anti-47 K immunogen mAb was nonreactive against rabbit IgG or IgM. mAb directed specifically against the 47 K mol wt immunogen of T. pallidum was examined for strategic functional activities. It was found to be reactive in the microhemagglutination assay for T. pallidum antibodies, the T. pallidum immobilization test, and was found to be capable of significant blockage of attachment of virulent T. pallidum to host cells in tissue culture. Additional significant biological activity for the anti-47 K mol wt immunogen mAb was revealed through results of the in vitro-in vivo neutralization test of Bishop and Miller, in which a 99% or 100% neutralizing activity was demonstrated. The combined data of this study suggest that the 47 K mol wt immunogen of T. pallidum represents an abundant, immunodominant, surface-exposed immunogen possessing potential biological importance in the pathogenesis and immunology of T. pallidum infection. These studies serve to establish the first functionally defined immunogen for T. pallidum, which may represent the major immunogen of the organism.

Animals↗

PubMedDate not supplied

Purified flagella from Treponema phagedenis biotype Reiter does not induce protective immunity against experimental syphilis in rabbits.

Thirteen rabbits were immunized three times at weekly intervals with 50 micrograms of flagella purified from Treponema phagedenis biotype Reiter. Fourteen rabbits were inoculated in the same way with a placebo preparation. Rabbits immunized with the flagella developed an immune response to the flagella but showed no statistically significant prolongation of incubation time or diminution of lesion severity when challenged intradermally with 4 X 10(3) Treponema pallidum organisms.

Animals↗

PubMed1998

Identification and sequence analysis of Treponema pallidum tprJ, a member of a polymorphic multigene family.

TnphoA mutagenesis was used to identify genes encoding exported proteins in a genomic DNA library of Treponema pallidum, the syphilis agent. The nucleotide sequence of an open reading frame (tprJ) that encodes a 755-amino acid protein with a predicted molecular mass of 81.1 kDa was determined. The deduced amino acid sequence of TprJ has homology to the major surface protein of Treponema denticola, a periodontal pathogen. Southern hybridization and genomic DNA sequence analysis indicate that tprJ is a member of a polymorphic multigene family. RT-PCR data showed that tprJ is expressed in treponemes during syphilitic infection. A putative tprJ gene was sequenced from T. pertenue, the closely related yaws agent. The deduced amino acid sequence of T. pertenue TprJ is 87.3% identical to that of T. pallidum TprJ. This is the first report of significant sequence differences within homologous genes of T. pallidum and T. pertenue.

Amino Acid Sequence↗

PubMed1999

Molecular characterization of a flagellar (fla) operon in the oral spirochete Treponema denticola ATCC 35405.

A Treponema denticola 9.6-kb motility locus containing 11 genes was identified, sequenced and analyzed. The genes were designated tap1, flgD, flgE, orf4, motA, motB, fliL, fliM, fliY, orf10 and fliP. The order of these genes is identical to that of the corresponding region of the Treponema pallidum fla operon. Seven of the deduced Fla proteins share significant homology with both Escherichia coli and Bacillus subtilis proteins associated with flagellar structure and function. Reverse transcription-PCR analysis indicated that the T. denticola fla genes are transcribed as a single unit. A putative sigma(28)-like promoter, virtually identical to the T. pallidum fla promoter, was identified upstream of tap1. These results showed that the T. denticola and T. pallidum fla operons are highly conserved, supporting the proposed phylogenetic relatedness of these spirochetes.

Bacterial Proteins↗

PubMed1976

Ultrastructure of cells of Treponema pertenue obtained from experimentally infected hamsters.

Cells of Treponema pertenue Gauthier obtained by elution from skin lesions and lymph nodes of experimentally infected hamsters were studied in the electron microscope by means of negative staining. The cells were also examined in thin secions of skin biopsies and lymph nodes. Fimbriae were observed on the negatively stained cells. Until now fimbriae have not been demonstrated on negatively stained cells of other species of Treponema, but at present only one straon of T. pertenue has been studied in our laboratory. Otherwise, the ultrastructure of the T. pertenue cells was found to be very similar, if not identical to, the substructural details observed in cells of T. pallidum and T. cuniculi. In thin sections of skin biopsies, treponemes were observed in the intercellular spaces between cells of the stratum basale and the stratum spinosum layers of the epidermis.

Animals↗

PubMed1972

Evaluation of the qualitative and automated quantitative microhemagglutination assay for antibodies to Treponema pallidum.

Qualitative and quantitative microhemagglutination assays for antibodies to Treponema pallidum (MHA-TP) were performed on 314 syphilitic and 597 presumably nonsyphilitic sera, and the results were compared with those of the fluorescent treponemal antibody-absorbed (FTA-ABS), the Treponema pallidum immobilization (TPI), and the Veneral Disease Research Laboratory (VDRL) tests. MHA-TP sensitivity was similar to that of the other tests in all stages of syphilis except primary syphilis, in which MHA-TP reactivity was only 64% compared with 82% in the FTA-ABS test, 73% in the VDRL test, and 67% in the TPI test. MHA-TP specificity was satisfactory and comparable to that of the other treponemal tests. Quantitation of the MHA-TP test was automated by use of Autotiter II equipment. Titers tended to become elevated later in the course of syphilis and to remain elevated longer than did VDRL titers. Reproducibility of the quantitative MHA-TP test was satisfactory, with duplicate tests agreeing within one doubling dilution on 97.5% of 351 reactive sera. Poor reproducibility was obtained with sera giving minimal reactions in the qualitative test, and such sera should be routinely retested. The MHA-TP is less time-consuming and costly than the FTA-ABS test and could be used in conjunction with the VDRL or another reagin test for syphilis to eliminate a large number of the FTA-ABS tests now required.

Antibodies↗

PubMed1998

Flagellins, but not endoflagellar sheath proteins, of Treponema pallidum and of pathogen-related oral spirochetes are glycosylated.

Glycosylation of the flagellar core proteins (FlaBs) was detected in Treponema pallidum Nichols and in the type or reference strains of seven oral Treponema species. In several nonmotile strains of oral treponemes, the FlaBs were undetectable by both antibody and glycan staining. In contrast, a spontaneous low-motility variant of T. vincenti poundi-related strain RitzA, OMZ 305A, lacked the flagellar sheath protein (FlaA) and the two glycan-staining FlaB bands of the wild type, but antibody labeling revealed a novel FlaB band with a lower relative molecular weight. A ca. 38-kDa component of isolated endoflagella of T. vincentii OMZ 800 was identified on Western blots as FlaA by monoclonal antibody (MAb) H9-2, which specifically labels the 37-kDa FlaA protein of T. pallidum. Glycan and H9-2 labeling patterns similar to those of T. pallidum were observed in whole-cell extracts of T. medium G7201 and of 10 strains classified as T. vincentii and as two T. vincentii-related taxons. These four groups were thus identified as cultivable pathogen (T. pallidum)-related oral spirochetes as defined by labeling with MAb H9-2. No H9-2 MAb-reactive component could be detected in T. amylovorum, T. denticola, T. maltophilum, T. pectinovorum, and the three subspecies of T. socranskii.

Flagellin↗