Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “TREPONEMA”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 37 records · Page 2Linked to original sources
PubMed2005

Occurrence of two newly named oral treponemes - Treponema parvum and Treponema putidum - in primary endodontic infections.

BACKGROUND/AIMS: Recent evidence from molecular genetic studies has revealed that oral Treponema species are involved in infections of endodontic origin. This study assessed the occurrence of two newly named oral treponemes - Treponema parvum and Treponema putidum - in primary endodontic infections using a culture-independent identification technique. METHODS: Genomic DNA was isolated directly from clinical samples, and a 16S rRNA gene-based nested polymerase chain reaction (PCR) assay was used to determine the presence of T. parvum and T. putidum. Species-specific primer pairs were developed by aligning closely related 16S rRNA gene sequences. The specificity for each primer pair was validated by running PCR against a panel of oral bacteria and by sequence analysis of PCR products from positive clinical samples. RESULTS: T. parvum was detected in 52% of the root canals associated with chronic apical periodontitis, in 20% of the cases diagnosed as acute apical periodontitis, and in no abscessed case. In general, T. parvum was detected in 26% of the samples from primary endodontic infections. T. putidum was found in only one case of acute apical periodontitis (2% of the total number of cases investigated). CONCLUSIONS: The devised nested PCR protocol was able to identify both T. parvum and T. putidum directly in clinical samples and demonstrated that these two treponemes can take part in endodontic infections.

DNA, Bacterial↗
PubMed2004

Description of Treponema azotonutricium sp. nov. and Treponema primitia sp. nov., the first spirochetes isolated from termite guts.

Long after their original discovery, termite gut spirochetes were recently isolated in pure culture for the first time. They revealed metabolic capabilities hitherto unknown in the Spirochaetes division of the Bacteria, i.e., H(2) plus CO(2) acetogenesis (J. R. Leadbetter, T. M. Schmidt, J. R. Graber, and J. A. Breznak, Science 283:686-689, 1999) and dinitrogen fixation (T. G. Lilburn, K. S. Kim, N. E. Ostrom, K. R. Byzek, J. R. Leadbetter, and J. A. Breznak, Science 292:2495-2498, 2001). However, application of specific epithets to the strains isolated (Treponema strains ZAS-1, ZAS-2, and ZAS-9) was postponed pending a more complete characterization of their phenotypic properties. Here we describe the major properties of strain ZAS-9, which is readily distinguished from strains ZAS-1 and ZAS-2 by its shorter mean cell wavelength or body pitch (1.1 versus 2.3 micro m), by its nonhomoacetogenic fermentation of carbohydrates to acetate, ethanol, H(2), and CO(2), and by 7 to 8% dissimilarity between its 16S rRNA sequence and those of ZAS-1 and ZAS-2. Strain ZAS-9 is proposed as the type strain of the new species, Treponema azotonutricium. Strains ZAS-1 and ZAS-2, which are H(2)-consuming, CO(2)-reducing homoacetogens, are proposed here to be two strains of the new species Treponema primitia. Apart from the salient differences mentioned above, the genomes of all three strains were similar in size (3,461 to 3,901 kb), in G+C content (50.0 to 51.0 mol%), and in possession of 2 copies of the gene encoding 16S rRNA (rrs). For comparison, the genome of the free-living spirochete Spirochaeta aurantia strain J1 was analyzed by the same methods and found to have a size of 3,719 kb, to contain 65.6 mol% G+C, and also to possess 2 copies of the rrs gene.

Animals↗
PubMed1982

Fatty acid requirement of Treponema denticola and Treponema vincentii.

Treponema denticola and Treponema vincentii were cultured in a medium supplemented with either 0.2 or 0.4% (w/v) alpha globulin in place of serum. The active factor(s) in alpha globulin was stable at pH 7.0 to autoclaving and was nondialyzable. Extraction of lipids from alpha globulin showed that both protein and lipid, supplied by the alpha globulin, were required for maximal growth of these two oral treponemes. The lipid component was investigated by adding sodium salts of long-chain fatty acids to the basal medium supplemented with 0.4% delipified alpha globulin. The lipid component of alpha globulin was replaced by either oleic acid (cis-18:1(9)) or by elaidic acid (trans- 18:1 (9)0. No other saturated or unsaturated fatty acid tested could support good growth. Tween 80 (polysorbitan monooleate) was the only Tween compound able to support maximal growth of T. denticola. The cellular lipids of T. denticola, grown with oleate in broth supplemented with 0.4% delipified alpha globulin, were extracted and analyzed by gas chromatography. The principle fatty acids were myristic, pentadecanoic, and palmitic acids. Lesser amounts of oleic acid, eicosadienoic acid, and an unidentified fatty acid (retention time, 88 min) were also detected. Treponema denticola appears to be capable of limited synthesis of cellular fatty acids such as myristic, pentadecanoic, and palmitic acids from oleic acid.

Alpha-Globulins↗
PubMed1991

Identification of Treponema hyodysenteriae and Treponema innocens using two four-hour identification systems.

Two 4-hour identification systems, the RapID-ANAII (Innovative Diagnostic Systems) and the ANI card (Vitek Systems), were used to identify isolates of Treponema hyodysenteriae and T. innocens. Twenty-one isolates of T. innocens and 53 isolates of T. hyodysenteriae were tested with both systems. With the ANI system, alpha-galactosidase was the only test that differentiated the two species. With the RapID-ANAII system, alpha-galactosidase and indole tests allowed differentiation of the two species. Treponema hyodysenteriae was alpha-galactosidase negative and indole positive, whereas T. innocens produces the opposite reactions. Three isolates were alpha-galactosidase negative and indole negative. These isolates represent a group intermediate between the two officially described species. The two species of swine Treponema can be identified by commercial identification kits and a third group of isolates intermediate between the two species was identified.

Animals↗
PubMed1990

Immune response to Treponema pertenue and Treponema pallidum Nichols in patients with yaws.

Human sera from African patients with acute yaws were analysed by Western blot (WB) against antigens of Treponema pallidum Nichols and two Treponema pertenue isolates. The Western blot patterns were remarkably similar from one patient to another, and strains of both subspecies exhibited exactly the same banding pattern. Sera from yaws patients failed to detect at least one antigen in T. pertenue which was absent from T. pallidum.

Acute Disease↗
PubMed1992

Organization of the ribosomal RNA genes in Treponema phagedenis and Treponema pallidum.

The genomic DNA fragment which contains ribosomal RNA (rRNA) genes for Treponema phagedenis was cloned into bacteriophage vector lambda EMBL3. A restriction map of the fragment was constructed and the organization of the rRNA genes was determined. The fragment contained at least one copy of the 16S, 23S and 5S sequences and the genes are arranged in the order 16S-23S-5S. Southern hybridization using radiolabeled rRNA gene probes to genomic DNA from T. phagedenis strain Reiter and T. pallidum strain Nichols showed that these organisms have two radioactive fragments which hybridize to the probes in their genome. These results suggest that both pathogenic and non-pathogenic strains of Treponema may carry at least two sets of rRNA genes on their chromosomes.

Cloning, Molecular↗
PubMed1994

Identification of lactoferrin-binding proteins from Treponema pallidum subspecies pallidum and Treponema denticola.

Lactoferrin-binding or -associated proteins were identified in Treponema pallidum subspecies pallidum and Treponema denticola by affinity column chromatography using human lactoferrin and detergent-solubilized, radiolabelled spirochaetes. Two discrete polypeptides of T. pallidum with masses of 45 and 40 kDa and a broad band from 29-34 kDa exhibited association with human apo- and partially ferrated lactoferrin. T. denticola produced two proteins that associated with a lactoferrin affinity matrix (50 and 35 kDa). T. pallidum and T. denticola did not associate with soluble, human transferrin in parallel experiments. Soluble human lactoferrin competed with all lactoferrin-associated proteins from T. pallidum and T. denticola in competitive-binding assays. However, the T. denticola proteins dissociated from a lactoferrin-affinity matrix in the presence of differing concentrations of unlabelled, soluble lactoferrin competitor. Treatment with phospholipase D altered migration of the diffuse 29-34 kDa band of T. pallidum suggesting that the polypeptide was lipid-modified. Each of the lactoferrin-binding proteins from T. pallidum and T. denticola reacted with pooled rabbit syphilitic antisera. The lactoferrin-binding proteins of T. pallidum reacted with human sera from patients at all stages of syphilis. In addition, a monoclonal antibody generated against the 45 kDa polypeptide of T. pallidum crossreacted with the 29-34 kDa protein.

Antibodies, Bacterial↗
PubMed1983

Comparison of major protein antigens and protein profiles of Treponema pallidum and Treponema pertenue.

The protein profiles of Treponema pallidum and Treponema pertenue, the causative agents of syphilis and yaws, respectively, were compared by one- and two-dimensional gel electrophoresis. One-dimensional gels showed essentially no differences in the protein patterns of these treponemes. On two-dimensional gels most radiolabeled protein species were shared; however, variations were noticed in several minor protein species. Antigenic comparison by radioimmunoprecipitation and Western blotting also demonstrated similarities between these spirochetes. However, lactoperoxidase-catalyzed iodination of T. pallidum and T. pertenue suggested differences in their surface proteins.

Animals↗
PubMed1983

Molecular basis of immunological cross-reactivity between Treponema pallidum and Treponema pertenue.

Protein antigens of Treponema pallidum, Nichols strain, and Treponema pertenue, Gauthier strain, were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting techniques. Treponemal proteins were solubilized in 1% sodium dodecyl sulfate, electrophoresed on 12.5% polyacrylamide gels, and either stained with Coomassie brilliant blue or electrophoretically transferred to nitrocellulose paper. These antigen blots were incubated with sera from rabbits infected with either T. pallidum or T. pertenue and 125I-labeled staphylococcal protein A and exposed to X-ray film for visualization of antigenic molecules. Protein profiles of each organism separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and stained with Coomassie brilliant blue showed no distinguishable differences. Antigenic profiles as determined by Western blots were similar with two exceptions. A 39,500-dalton band was present on T. pertenue but absent from T. pallidum, and a 19,000-dalton band was present on T. pallidum but absent from T. pertenue (although two additional antigenic bands at 21,000 and 18,000 daltons were seen on T. pertenue). Because these differences were detected by using antisera raised against either T. pallidum or T. pertenue, these molecules must contain some antigenic determinants in common despite their differences in molecular weight.

Antigens, Bacterial↗
PubMed1986

Antigenic interrelationship between endoflagella of Treponema phagedenis biotype Reiter and Treponema pallidum (Nichols): molecular characterization of endoflagellar proteins.

Purified endoflagella from nonpathogenic Treponema phagedenis biotype Reiter were characterized biochemically and compared antigenically with the endoflagellar proteins of Treponema pallidum. T. phagedenis biotype Reiter endoflagella were dissociated into constituent polypeptides by incubation under conditions which disrupt noncovalent bonds. Chymotrypsin peptide maps of T. phagedenis biotype Reiter endoflagellar proteins revealed that the 37- and 33-kilodalton (kDa) major components shared significant homology with the 27- and 30-kDa minor components, respectively. The peptide maps also suggested that the major components shared a lesser degree of structural similarity with each other. These relationships were confirmed by Western blots of T. phagedenis biotype Reiter endoflagellar proteins employing antibodies that were purified against the individual endoflagellar polypeptides. Western blots of T. pallidum with the purified antibodies also demonstrated strong cross-reactivity between the T. phagedenis biotype Reiter endoflagellar proteins and T. pallidum proteins of identical or similar molecular weights. A unique Western blotting technique that we called epitope bridging was used to determine that the 37-kDa subunit contains most of the external epitopes on T. phagedenis biotype Reiter endoflagella. Immunoelectron microscopy with human syphilitic serum and rabbit T. phagedenis biotype Reiter endoflagellar antiserum confirmed the presence of cross-reactive epitopes on the surface of intact T. phagedenis and T. pallidum endoflagella.

Animals↗
PubMed1994

Isolation of the outer membranes from Treponema pallidum and Treponema vincentii.

The outer membranes from Treponema pallidum subsp. pallidum and Treponema vincentii were isolated by a novel method. Purified outer membranes from T. pallidum and T. vincentii following sucrose gradient centrifugation banded at 7 and 31% (wt/wt) sucrose, respectively. Freeze fracture electron microscopy of purified membrane vesicles from T. pallidum and T. vincentii revealed an extremely low density of protein particles; the particle density of T. pallidum was approximately six times less than that of T. vincentii. The great majority of T. vincentii lipopolysaccharide was found in the outer membrane preparation. The T. vincentii outer membrane also contained proteins of 55 and 65 kDa. 125I-penicillin V labeling demonstrated that t. pallidum penicillin-binding proteins were found exclusively with the protoplasmic cylinders and were not detectable with purified outer membrane material, indicating the absence of inner membrane contamination. Isolated T. pallidum outer membrane was devoid of the 19-kDa 4D protein and the normally abundant 47-kDa lipoprotein known to be associated with the cytoplasmic membrane; only trace amounts of the periplasmic endoflagella were detected. Proteins associated with the T. pallidum outer membrane were identified by one- and two-dimensional electrophoretic analysis using gold staining and immunoblotting. Small amounts of strongly antigenic 17- and 45-kDa proteins were detected and shown to correspond to previously identified lipoproteins which are found principally with the cytoplasmic membrane. Less antigenic proteins of 65, 31 (acidic pI), 31 (basic pI), and 28 kDa were identified. Compared with whole-organism preparations, the 65- and the more basic 31-kDa proteins were found to be highly enriched in the outer membrane preparation, indicating that they may represent the T. pallidum rare outer membrane proteins. Reconstitution of solubilized T. pallidum outer membrane into lipid bilayer membranes revealed porin activity with two estimated channel diameters of 0.35 and 0.68 nm based on the measured single-channel conductances in 1 M KCl of 0.40 and 0.76 nS, respectively.

Animals↗
PubMed1996

Organization, transcription, and expression of the 5' region of the fla operon of Treponema phagedenis and Treponema pallidum.

A locus encoding polypeptides associated with flagellar structure and function was identified, sequenced, and characterized in Treponema phagedenis and Treponema pallidum. This locus includes homologs of the FlgD, FlgE, MotA, MOB, FliL, and FliM polypeptides found in Salmonella typhimurium and Bacillus subtilis. These polypeptides are extensively conserved between the two treponemes. Several additional polypeptides or unknown function, including Tapl, located upstream of FlgD, and ORF4, located between FlgE and MotA, were also identified. Transcription analysis using RNA PCR indicated that these genes are likely transcribed as part of a single operon and comprise the 5' region of the treponemal fla operon. Primer extension analysis identified a putative promoter, preceding T. phagedenis tap1 in a region of divergent transcription. Pfla resembles the class II or class III motility-related promoters of S. typhimurium. FlgE and Tap1 were further characterized. Western blotting (immunoblotting) indicated that T. pallidum FlgE exhibited an unusual polypeptide ladder that was similar but not identical to that of T. phagedenis. Triton X-114 phase partitioning of T. phagedenis cells coupled with Western blotting revealed that Tap1 was located in the aqueous phase. Computer analysis indicated that Tap1 had no significant membrane spanning regions, suggesting that it resides primarily in the cytoplasm. The organization and expression of this operon are similar in both treponemes but different from those of previously described motility-related operons. These results indicate that despite extensive amino acid sequence conservation, the expression of spirochete flagellar polypeptides is different from that in other bacteria.

Amino Acid Sequence↗
PubMed1977

Immunofluorescent staining of Treponema pallidum and Treponema pertenue in tissues fixed by formalin and embedded in paraffin wax.

The main problems in identifying Treponema pallidum in tissues are optical definition contrast, and specificity. In general, fluorochrome staining provides optical definition and contrast superior to that obtained by ordinary tinctorial staining, and in theory improved resolution. Specificity is lacking however, as with other stains. In contrast, immunofluorescence should combine the optical advantages of fluorochrome staining with the immunological advantages of specificity. Since the validity of such staining depends in part upon the integrity of the antigenic components of the micro-organisms, it is customary to avoid such drastic procedures as are involved in routine fixation and paraffin embedding. The manipulation, however, of unfixed cryostat material, in contrast with that of paraffin sections suffers from two disadvantages--namely, friability and infectivity. Published and unpublished work has shown antigenic stability in T. pallidum to a variety of procedures, both physical and chemical. Consideration of these facts led in this work to successful immunofluorescent staining after routine formalin fixation and paraffin embedding of tissues infected with T. pallidum or Treponema pertenue. Optical definition and contrast, were superior to that obtained with silver methods, but it was not possible to differentiate between these two organisms. Nevertheless immunofluorescence applied as described to paraffin sections should supply a convenient safe, and sensitive means of reappraising the histopathology of treponemal disease in patients, necropsy material, and experimental animals.

Animals↗
PubMed2005

Prostaglandin E(2) is a main mediator in receptor activator of nuclear factor-kappaB ligand-dependent osteoclastogenesis induced by Porphyromonas gingivalis, Treponema denticola, and Treponema socranskii.

BACKGROUND: Periodontitis is an inflammatory disease that often leads to destruction of alveolar bone; a number of bacteria in subgingival plaque are associated with bone destruction in periodontitis. To understand the mechanism of how periodontopathogens induce osteoclastogenesis, we determined which mediators are involved in the osteoclastogenesis. METHODS: We investigated effects of sonicates from three periodontopathic bacteria, Porphyromonas gingivalis, Treponema denticola, and Treponema socranskii, on osteoclast formation in a co-culture system of mouse calvaria-derived osteoblasts and bone marrow cells. The osteoclast formation was determined by tartrate resistant acid phosphatase (TRAP) staining. The expression of the receptor activator of nuclear factor-kappa B ligand (RANKL), prostaglandin E(2) (PGE(2)) and osteoprotegerin (OPG) in mouse calvaria-derived osteoblasts was determined by immunoassay. RESULTS: Each bacterial sonicate induced the osteoclast formation in the co-culture system. These bacterial sonicates increased the expression of RANKL and PGE(2), and decreased the expression of OPG in osteoblasts. The addition of OPG, an inhibitor of RANKL, in the co-culture completely suppressed the osteoclastogenesis that was stimulated by each bacterial sonicate. Indomethacin, which is an inhibitor of PGE(2) synthesis, reduced more than 88% of the osteoclast formation induced by each bacterial sonicate. Indomethacin inhibited more than 80% of RANKL expression in osteoblasts induced by T. denticola and T. socranskii, and 59% by P. gingivalis. Indomethacin completely recovered the depression of OPG expression in osteoblasts by T. denticola and T. socranskii to the level of the untreated osteoblasts. Indomethacin recovered the reduction of OPG expression by P. gingivalis to 67%. CONCLUSION: These findings suggest that the osteoclastogenesis by P. gingivalis, T. denticola, and T. socranskii is mediated by a RANKL-dependent pathway and that PGE(2) is a main factor in the pathway by the enhancing of RANKL expression and the depression of osteoprotegerin, a RANKL inhibitor.

Acid Phosphatase↗
PubMed1986

Correlation of treponemicidal activity in normal human serum with the presence of IgG antibody directed against polypeptides of Treponema phagedenis biotype Reiter and Treponema pallidum, Nichols strain.

Normal human serum (NHS) was shown to have complement-dependent treponemicidal activity against both Treponema pallidum and Treponema phagedenis biotype Reiter (TPR) by employing in vitro-in vivo neutralization and TPR plaque assays, respectively. The molecular basis of NHS treponemicidal activity was studied by immunoblot analysis in conjunction with treponemicidal assays. Five major T. pallidum polypeptide bands (47kDa, 35kDa, 33kDa doublet, and 30 kDa) and three major TPR polypeptide bands (47kDa and 33kDa doublet) bound IgG present in NHS. Absorption of NHS with TPR completely removed both TPR and T. pallidum treponemicidal activity; corresponding immunoblots demonstrated a significant removal of IgG antibody against all three TPR polypeptide bands as well as four T. pallidum polypeptide bands (30kDa, 33kDa doublet, and 35kDa). In contrast, T. pallidum absorption of NHS was found to remove treponemicidal activity against T. pallidum but not TPR; corresponding Western blots showed the complete removal of IgG antibody against all but one T. pallidum polypeptide band (47kDa) but no detectable loss in IgG antibody against the TPR polypeptides. These results suggest that antibody in NHS generated against nonpathogenic, indigenous treponemes is responsible for the T. pallidum treponemicidal activity. Furthermore, the treponemicidal activity against T. pallidum correlated with the presence of IgG antibody against T. pallidum polypeptides of 30kDa, 35kDa, and a 33kDa doublet.

Antibodies, Bacterial↗
PubMed1989

Treponema pallidum subspecies pallidum (Nichols) and Treponema pallidum subspecies pertenue (CDC 2575) differ in at least one nucleotide: comparison of two homologous antigens.

In an attempt to identify antigenic differences between Treponema pallidum subsp. pallidum (T. pallidum) and Treponema pallidum subsp. pertenue (T. pertenue) a gene bank of T. pertenue was constructed in lambda vector EMBL3. Clones carrying the T. pertenue gene encoding a 190 kDa protein, TyF1, were selected and the DNA was expressed in E. coli. TyF1 was shown to be closely related, but slightly different from the previously cloned T. pallidum antigen TpF1. TyF1 and TpF1 are high molecular weight antigens of about 190 kDa, which dissociate into 19 kDa subunits after heat treatment in presence of SDS. The difference between the two proteins is most obvious after treatment with proteinase K, which yields a 115 kDa component from TyF1 and a 95 kDa component from TpF1, as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The structural genes encoding TyF1 and TpF1 were sequenced and the predicted amino acid sequences differed in a single amino acid residue at position 40, which is arginine in TyF1 and glutamine in TpF1. Similarities TyF1 and TpF1 with the previously described 4D antigen are discussed. The antibody response to TyF1 and TpF1 seems higher in syphilis patients than in yaws patients. The possibility of using the difference between these T. pallidum and the T. Pertenue antigens for serological discrimination of syphilis and yaws is discussed.

Antigens, Bacterial↗
PubMed1977

Selective response of lymphocytes from Treponema pallidum-infected rabbits to mitogens and Treponema reiteri.

The in vitro response of peripheral blood lymphocytes from rabbit infected with Treponema pallidum was examined using various mitogens and avirulent Treponema reiteri. For the first 4 weeks after treponemal infection, the response of lymphocytes from syphilitic rabbits to phytohemagglutinin and pokeweed mitogen was markedly reduced in comparison to uninfected controls. Lymphocytes from both groups of rabbits responded normally to class-specific immunoglobulin anti-sera (anti-immunoglobulin M and anti-immunoglobulin G) and T. reiteri.

Animals↗