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PubMed1966

Immunity in experimental syphilis. IV. Serological reactivity of antigens extracted from gamm-irradiated Treponema pallidum and Treponema reiteri.

Miller, James N. (University of California School of Medicine, Los Angeles), J. H. De Bruijn, and J. H. Bekker. Immunity in experimental syphilis. IV. Serological reactivity of antigens extracted from gamma-irradiated Treponema pallidum and Treponema reiteri. J. Bacteriol. 91:583-587. 1966.-Ultrasonic lysate preparations extracted from virulent Treponema pallidum, Nichols strain, suspensions exposed to 652,800 R of gamma-irradiation exhibited a loss in the serological reactivity of their heat-labile antigens; the heat-stable components of both the lysate and residue antigens were unaffected. The activity of heat-stable, cardiolipin T. pallidum complement-fixing antigen obtained from similarly irradiated organisms was also unaltered. gamma-Irradiation of the cultivable Treponema reiteri with dosages as high as 6,500,000 R failed to alter serologically either the heat-labile or heat-stable component of its lipopolysaccharide-protein (Reiter protein) antigen. The reactivity of the lipopolysaccharide portion of the Reiter protein complex with an antiserum to T. pallidum Nichols indicates previously unsuspected antigenic differences between the rabbit-adapted Nichols strain of the organism and so-called "wild" human strains of T. pallidum in which this antigen is generally absent.

Animals↗

PubMed1996

Characterization of the cytoplasmic filament protein gene (cfpA) of Treponema pallidum subsp. pallidum.

Treponema pallidum and other members of the genera Treponema, Spirochaeta, and Leptonema contain multiple cytoplasmic filaments that run the length of the organism just underneath the cytoplasmic membrane. These cytoplasmic filaments have a ribbon-like profile and consist of a major cytoplasmic filament protein subunit (CfpA, formerly called TpN83) with a relative molecular weight of approximately 80,000. Degenerate DNA primers based on N-terminal and CNBr cleavage fragment amino acid sequences of T. pallidum subsp. pallidum (Nichols) CfpA were utilized to amplify a fragment of the encoding gene (cfpA). A 6.8-kb EcoRI fragment containing all but the 5' end of cfpA was identified by hybridization with the resulting PCR product and cloned into Lambda ZAP II. The 5' region was obtained by inverse PCR, and the complete gene sequence was determined. The cfpA sequence contained a 2,034-nucleotide coding region, a putative promoter with consensus sequences (5'-TTTACA-3' for -35 and 5'-TACAAT-3' for -10) similar to the sigma70 recognition sequence of Escherichia coli and other organisms, and a putative ribosome-binding site (5'-AGGAG-3'). The deduced amino acid sequence of CfpA indicated a protein of 678 residues with a calculated molecular mass of 78.5 kDa and an estimated pI of 6.15. No significant homology to known proteins or structural motifs was found among known prokaryotic or eukaryotic sequences. Expression of a LacZ-CfpA fusion protein in E. coli was detrimental to survival and growth of the host strain and resulted in the formation of short, irregular filaments suggestive of partial self-assembly of CfpA. The cytoplasmic filaments of T. pallidum and other spirochetes appear to represent a unique form of prokaryotic intracytoplasmic inclusions.

Amino Acid Sequence↗

PubMed1979

Mucopolysaccharidase of Treponema pallidum.

Treponema pallidum (Nichols strain) exhibited mucopolysaccharidase activity. Acidic mucopolysaccharides were broken down more rapidly by viable treponemes than by heat-inactivated treponemes or membrane filtrates of treponemal suspensions. Ouchterlony immunodiffusion demonstrated the occurrence of antibodies to the hyaluronidase-like enzyme within syphilitic sera. After intratesticular inoculation of 2 x 10(7) to 6 x 10(7) treponemes, these anti-mucopolysaccharidase antibodies were detected between 9 and 35 days postinoculation. In addition, acidic mucopolysaccharides were present in the serum of infected animals 9 and 16 days postinoculation. Immune serum that contained antibodies to the mucopolysaccharidase restricted treponemal breakdown of acidic mucopolysaccharides. It has been previously demonstrated that immune rabbit serum contains a factor that blocks attachment of T. pallidum (Nichols strain) to cultured mammalian cells. This factor was effectively absorbed by prior incubation with bovine hyaluronidase. It is postulated that T. pallidum attaches to acidic mucopolysaccharides on the surface of cultured cells through the mucopolysaccharidase enzyme at the surface of the organisms. These findings are discussed in terms of the histopathogenesis of T. pallidum with applications to the healing immune response.

Glycosaminoglycans↗

PubMed1972

Shape of Treponema pallidum.

Treponema pallidum was found to be not helical, but a flat wave twisted into one to five different planes per cell.

Bacteriological Techniques↗

PubMed1979

Glucose incorporation by Treponema pallidum.

Treponema pallidum incorporated glucose into trichloroacetic acid-precipitable material. The amount of incorporation was proportional to the number of treponemes and was estimated to equal 3% of the glucose oxidized.

Carbohydrates↗

PubMed1981

Distribution of glucose incorporated into macromolecular material by treponema pallidum.

Treponema pallidum was observed to incorporate glucose carbons into lipids, ribonucleic acid, deoxyribonucleic acid, and protein. Only the glycerol portions of phosphatidylcholine and phosphatidylglycerol contained glucose-derived carbons. Incorporation of exogenous choline into phosphatidylcholine was detected. Glucose was incorporated into only the pentoses of nucleic acids. About 50% of the glucose incorporated into protein was present in only one amino acid, aspartate. Evidence suggests that aspartate synthesis could follow the conversion of phosphoenolpyruvate to oxalacetic acid by a guanosine 5'-diphosphate-dependent phosphoenolpyruvate carboxykinase.

Animals↗

PubMed1982

Electrophysiological dysfunction and cellular disruption of sensory neurones during incubation with Treponema pallidum.

Treponema pallidum (Nichols strain) was incubated with cultured nerve cells derived from dorsal root ganglia of rat embryos. The electrophysiological response of these neuronal cells was then investigated. Cells exposed to 2 X 10(8) treponemes/ml responded abnormally after 13 hours and failed to respond after 18 hours. In contrast, control preparations exposed to heat-inactivated treponemes or to culture medium responded normally after 72 hours. Extended incubation with viable treponemes resulted in various degrees of nerve cell disruption as shown by scanning electron microscopy. With some cells holes in the cytoplasmic membrane were detected; with others a coagulated matrix of apparent nuclear material and remnants of cytoskeletal elements indicated more severe destruction. These findings may explain the painless nature of many of the clinical manifestations of syphilis as well as the severe damage to central nervous system tissue in tertiary and congenital syphilis.

Action Potentials↗

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

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↗

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↗

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↗

PubMed1990

Antigenic cross-reactivity between Borrelia burgdorferi, Borrelia recurrentis, Treponema pallidum, and Treponema phagedenis.

The antigenic cross-reactivity between different Borrelia and Treponema species was determined by the indirect immunofluorescence antibody test and sodium dodecyl sulphate-polyacrylamide gel electrophoresis followed by immunoblotting. The protein profiles of Borrelia burgdorferi, Borrelia recurrentis, Treponema pallidum, and Treponema phagedenis revealed essential differences. Using immunoblotting, rabbit immune sera to B. burgdorferi and B. recurrentis exhibited strong cross-reactivities to heterologous borrelial antigens and, to a lesser extent, to treponemal antigens. Immune sera to T. pallidum and T. phagedenis reacted with heterologous treponemal antigens, but exhibited lesser cross-reactivities to borrelial antigens. Five B. burgdorferi and seven T. pallidum major antigens were not cross-reacting with antisera raised against T. pallidum and B. burgdorferi, respectively. However, absorption of the investigated antisera with a T. phagedenis ultrasonicate eliminated cross-reacting borrelial and treponemal antibodies.

Absorption↗

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↗

PubMed1980

Genetic relationship between Treponema pallidum and Treponema pertenue, two noncultivable human pathogens.

Genetic relationships among two strains of Treponema pallidum (Nichols and KKJ) and a strain of T. pertenue were determined by measuring the degree of deoxyribonucleic acid sequence homology. The results in indicated that these three virulent, noncultivable treponemes were genetically indistinguishable. Like T. pallidum (Nichols), T. pertenue (Gauthier) had no detectable deoxyribonucleic acid sequence homology with T. phagedenis (biotype Reiter), T. refringens (biotype Noguchi), or with salmon sperm.

Base Sequence↗

PubMed1979

Comparative behavior of virulent strains of Treponema pallidum and Treponema pertenue in gradient cultures of various mammalian cells.

Two strains of virulent Treponema pallidum and two of virulent T. pertenue were investigated for their ability to attach to and survive in gradient cultures of five different mammalian cells under aerobic conditions. The strains of T. pallidum studied were the high-rabbit-passage Nichols and the low-rabbit-passage KKJ. The former was known to readily attach to cottontail rabbit epithelial cells (Sf1Ep) and to survive in the virulent state for up to 21 days. We therefore compared attachment of the other virulent treponemes with that of T. pallidum (Nichols). The KKJ strain of T. pallidum behaved in a fashion similar to T. pallidum (Nichols) in all of the cultures. Both strains exhibited preferential attachment to cells of Sf1Ep and those derived from the ear of a nude athymic (nu/nu) mouse. In these cultures, we observed a consistent three- to fivefold increase in attached treponemes up to 12 days after initial inoculation. The strains of T. pertenue were the human-derived Gauthier and cynocephalus-derived FB. These two strains of T. pertenue also attached to cells of all five types of cultures, but in smaller numbers than were seen with T. pallidum and equally to all of the cultures. Neither preferential attachment to Sf1Ep and nude mouse ear cells nor increased attachment with time was seen.

Animals↗

PubMed1985

Identification of glycosylated protein antigens of Treponema pallidum and Treponema phagedenis.

Comparison of autoradiographies of intrinsically [35S] methionine and [14C] glucosamine labeled Treponema pallidum (Nichols strain) after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed four glycosylated proteins with molecular weights 30,500, 33,000, 35,000, and 59,000. T. phagedenis (biotype Reiter) was comparatively investigated and showed only two glycosylated proteins with molecular weights 33,000 and 34,000. The at the first time in treponemes identified glycosylated proteins could be precipitated with homologous human antibodies and characterized as antigens. By comparison with 125I surface labeling of T. pallidum and T. phagedenis it is suggested that the glycosylated protein antigens are localized on the surface of these treponemes.

Antigens, Bacterial↗

PubMed1988

Antigenic relatedness and N-terminal sequence homology define two classes of periplasmic flagellar proteins of Treponema pallidum subsp. pallidum and Treponema phagedenis.

The periplasmic flagella of many spirochetes contain multiple proteins. In this study, two-dimensional electrophoresis, Western blotting (immunoblotting), immunoperoxidase staining, and N-terminal amino acid sequence analysis were used to characterize the individual periplasmic flagellar proteins of Treponema pallidum subsp. pallidum (Nichols strain) and T. phagedenis Kazan 5. Purified T. pallidum periplasmic flagella contained six proteins (Mrs = 37,000, 34,500, 33,000, 30,000, 29,000, and 27,000), whereas T. phagedenis periplasmic flagella contained a major 39,000-Mr protein and a group of two major and two minor 33,000- to 34,000-Mr polypeptide species; 37,000- and 30,000-Mr proteins were also present in some T. phagedenis preparations. Immunoblotting with monospecific antisera and monoclonal antibodies and N-terminal sequence analysis indicated that the major periplasmic flagellar proteins were divided into two distinct classes, designated class A and class B. Class A proteins consisted of the 37-kilodalton (kDa) protein of T. pallidum and the 39-kDa polypeptide of T. phagedenis; class B included the T. pallidum 34.5-, 33-, and 30-kDa proteins and the four 33- and 34-kDa polypeptide species of T. phagedenis. The proteins within each class were immunologically cross-reactive and possessed similar N-terminal sequences (67 to 95% homology); no cross-reactivity or sequence homology was evident between the two classes. Anti-class A or anti-class B antibodies did not react with the 29- or 27-kDa polypeptides of T. pallidum or the 37- and 30-kDa T. phagedenis proteins, indicating that these proteins are antigenically unrelated to the class A and class B proteins. The lack of complete N-terminal sequence homology among the major periplasmic flagellar proteins of each organism indicates that they are most likely encoded by separate structural genes. Furthermore, the N-terminal sequences of T. phagedenis and T. pallidum periplasmic flagellar proteins are highly conserved, despite the genetic dissimilarity of these two species.

Amino Acid Sequence↗