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S C Holt

Publications and source records attributed to S C Holt.

At least 19 recordsLinked to original sources
PubMed1997

Purification and characterization of Campylobacter rectus surface layer proteins.

Campylobacter rectus is a putative periodontopathogen which expresses a proteinaceous surface layer (S-layer) external to the outer membrane. S-layers are considered to play a protective role for the microorganism in hostile environments. The S-layer proteins from six different C. rectus strains (five human isolates and a nonhuman primate [NHP] isolate) were isolated, purified, and characterized. The S-layer proteins of these strains varied in molecular mass (ca. 150 to 166 kDa) as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. They all reacted with monospecific rabbit antiserum to the purified S-layer of C. rectus 314, but a quantitative enzyme-linked immunosorbent assay demonstrated a strong antigenic relationship among the five human strains, while the NHP strain, 6250, showed weaker reactivity. Amino acid composition analysis showed that the S-layers of four C. rectus strains contained large proportions of acidic amino acids (13 to 27%) and that >34% of the amino acid residues were hydrophobic. Amino acid sequence analysis of six S-layer proteins revealed that the first 15 amino-terminal amino acids were identical and showed seven residues of identity with the amino-terminal sequence of the Campylobacter fetus S-layer protein SapA1. CNBr peptide profiles of the S-layer proteins from C. rectus 314, ATCC 33238, and 6250 confirmed that the S-layer proteins from the human strains were similar to each other and somewhat different from that of the NHP isolate (strain 6250). However, the S-layer proteins from the two human isolates do show some structural heterogeneity. For example, there was a 17-kDa fragment unique to the C. rectus 314 S-layer. The amino-terminal sequence of this peptide had homology with the C. rectus 51-kDa porin and was composed of nearly 50% hydrophobic residues. Thus, the S-layer protein from C. rectus has structural heterogeneity among different human strains and immunoheterogeneity with the NHP strain.

Amino Acid Sequence↗
PubMed1996

Trypsin-like protease activity of Porphyromonas gingivalis as a potential virulence factor in a murine lesion model.

Porphyromonas gingivalis possesses a large number of enzymatic activities which might be important in the virulence of this putative periodontopathogen. The purpose of this study was to examine these enzymatic activities in vivo in a murine model to assess their role in soft tissue destruction. Whole cells of P. gingivalis strains whether grown on blood agar plates or in broth exhibited high levels of alkaline phosphatase (ALPase), a trypsin-like protease (TLPase), acid phosphatase (ACPase), N-acetyl beta-glucosaminidase (Na beta-Gase) enzymes and collagenolytic activities. P. gingivalis W50 treated with 2 mM Na-P-tosyl-L-lysine chloromethyl ketone (TLCK)/phenylmethylsulfonyl fluoride (PMSF) prior to subcutaneous infection of mice failed to induce a phlegmonous abscess and lethality characteristic of animals challenged with untreated P. gingivalis. Comparison of wild type P. gingivalis strain 3079.03 with its protease-deficient (TLPase-negative) mutant NG4B19 revealed the mutant to be avirulent (no lesion and no death) in this model. P. gingivalis BEI and SW5 mutants (parent W50), which partially lacked TLPase enzyme activity produced only localized lesions, and no death. Thus, the TLPase enzyme appears to be correlated with the lesion type (spreading or localized), lesion size, and death in this mouse abscess model. Therefore, the enzymatic activities of P. gingivalis and specifically the TLPase enzyme could play an important role in periodontal disease by enhancing bacterial spread and degrading gingival tissues.

Acetylglucosaminidase↗
PubMed1996

Isolation and characterization of a hemin-binding cell envelope protein from Porphyromonas gingivalis.

A 30 kDa (heated 24 kDa) hemin-binding protein whose expression is both hemin and iron regulated was identified and purified in Porphyromonas gingivalis 381. A strong hemin-binding function was found by LDS-PAGE and TMBZ staining when cells were grown under hemin (iron)-limited conditions. N-terminal amino acid sequence analysis of CNBr-digested 24 kDa hemin binding protein revealed that this protein belongs to a new, so far undescribed hemin-binding class of proteins.

Amino Acid Sequence↗
PubMed1996

Lipopolysaccharide isolated from Porphyromonas gingivalis grown in hemin-limited chemostat conditions has a reduced capacity for human neutrophil priming.

One way prokaryotes respond to environmental stresses is by modifying selected outer membrane components. Iron, in the form of hemin, has been shown to be a significant regulator of Porphyromonas gingivalis growth and virulence and of the expression of outer membrane proteins and lipopoly saccharide. Since lipopoly saccharide has profound effects on host immune cells, this study compared the effect of hemin-restricted and hemin-normal P. gingivalis growth conditions on lipopolysaccharide priming of N-formylmethionyl-leucyl-phenylalanine-induced superoxide generation by human neutrophils. P. gingivalis was grown in a chemostat under normal (5 micrograms hemin/ml) and hemin-restricted (0.08 microgram hemin/ml) conditions. Purified lipopolysaccharide from both P. gingivalis normal and hemin-limited environments increased N-formylmethionyl-leucyl-phenylalanine-induced superoxide release by neutrophils in a dose-dependent manner. Lipopolysaccharide isolated from the hemin-normal conditions was a significantly more potent neutrophil priming agent than the lipopolysaccharide isolated from hemin-restricted conditions. Addition of normal human serum enhanced the priming effect of both lipopolysaccharide preparations; this effect, however, was more evident with the hemin-normal lipopolysaccharide. Further, this enhancing effect of serum was partly reduced in the presence of antibodies raised against the serum lipopolysaccharide-binding protein. The differences in the biological activity of the two lipopolysaccharide preparations could be associated with structural differences detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. These results indicate that hemin availability affects regulation of an aspect of P. gingivalis virulence, lipopolysaccharide-human neutrophils priming. The reduced capacity for neutrophil priming by hemin-restricted lipopolysaccharide appears to be related to lipopolysaccharide-neutrophil interactions and not to serum factors Targeting bacterial cell-surface components involved in hemin transport might be effective therapy for P. gingivalis-associated periodontal diseases.

Culture Media, Serum-Free↗
PubMed1996

Characteristics of systemic antibody responses of nonhuman primates following active immunization with Porphyromonas gingivalis, Prevotella intermedia and Bacteroides fragilis.

Periodontal disease is an infectious disease manifested by the progressive change of a healthy resident commensal microbiota to a pathogenic one characterized by a specific microbiota. Thus, the prospect for the use of selected bacteria or their antigens as a vaccine to interfere with the microbial changes and resulting progression of periodontal tissue destruction has been proposed. As a first step in examining the use of bacterial antigens as immunogens in periodontitis, this study characterized the humoral immune response in Macaca fascicularis after systemic immunization with intact Porphyromonas gingivalis, Prevotella intermedia and Bacteroides fragilis. Parental immunization of the nonhuman primate with the intact bacteria resulted in the production of specific and significantly elevated levels of antibodies to P. gingivalis and P. intermedia, with the predominant isotype being immunoglobulin G (IgG). In contrast, the principal response to the nonoral, intestinal bacterium, B. fragilis, was of the IgM isotype. Immunization increased IgG, IgM, and IgA antibody by 14-227 fold to P. gingivalis and 8-108 fold to P. intermedia. The level of serum IgA antibody increased (77-227 fold). The kinetics of the antibody response post-immunization and post-ligation differed with respect to each of the bacteria tested. IgG antibody to P. gingivalis increased through week 16 of the experiment and remained elevated above baseline through week 32. The IgG antibody level to P. intermedia peaked at 4 weeks following the third immunization and decreased post-ligation to near baseline levels by week 16. Characterization of the immune response after active immunization in the nonhuman primate has demonstrated a substantial and specific increase in antibody response which was sustained for several weeks. The insights obtained from these studies should help optimize the potential for immunologic interference with progressing periodontitis.

Analysis of Variance↗
PubMed1996

Mixed infection with Porphyromonas gingivalis and Fusobacterium nucleatum in a murine lesion model: potential synergistic effects on virulence.

These studies determined the characteristics of tissue destruction in a murine abscess model elicited by mixed infection with the periodontopathogens Fusobacterium nucleatum and Porphyromonas gingivalis. The interbacterial effects of this synergism, the kinetics of the relationship of the bacterial interaction, and the characteristics of the bacteria required for the tissue destruction were studied. Infection of mice with P. gingivalis and F. nucleatum strains elicited lesions of various sizes as a function of infective dose. Primary infection with F. nucleatum plus P. gingivalis at various ratios (i.e., <1:1) resulted in a significantly greater lesion size (P < 0.001) compared with that resulting from primary infection with P. gingivalis alone. At F. nucleatum/P. gingivalis ratios of > or = 1:1, spreading lesion formation and progression were significantly (P < 0.001) decreased, suggesting that bacterial interaction (i.e., coaggregation) may have inhibited the spread of the P. gingivalis infection to a site distant from the initial injection. Infection with F. nucleatum and P. gingivalis simultaneously (at different sites) or F. nucleatum administered within 4 h prior to or 1 h following P. gingivalis infection significantly enhanced the ability of P. gingivalis to form large phlegmonous lesions. Chemical inhibition of the P. gingivalis trypsin-like protease activity or the use of a trypsin-negative P. gingivalis strain abrogated tissue destruction either alone or in combination with F. nucleatum. Therefore, it was possible to examine aspects of virulence of these pathogens in a murine lesion model by either altering bacterial ratios, manipulating the time of infection, or targeting vital bacterial virulence factors.

Animals↗
PubMed1996

Yolk sac number, size and morphologic features in monochorionic monoamniotic twin pregnancy.

OBJECTIVE: To determine the relation between three characteristics of the yolk sac (number, size and morphologic features) and outcome in monochorionic monoamniotic twin pregnancy. METHODS: The authors reviewed data for the four sets of monochorionic monoamniotic twins detected by first-trimester ultrasonography between January 1990 and June 1994 at their institution. Data analysed included yolk sac number, size and morphologic features, as well as the outcome of the pregnancy. RESULTS: In all four sets of twins, only one yolk sac was identified. In one case the yolk sac was irregular in contour, and in two it was abnormally large. Two of the four mothers delivered healthy twins at 34 weeks gestational age, one had conjoined twins ( and underwent elective termination of the pregnancy), and one had a twin ectopic pregnancy (and underwent salpingectomy). CONCLUSION: A single yolk sac in cases of monochorionic monoamniotic twins may be a normal finding.

Adult↗
PubMed1995

Cell envelope and cell wall immunization of Macaca fascicularis: effect on the progression of ligature-induced periodontitis.

The nonhuman primate, Macaca fascicularis, was used to study the role of immunization with selected members of the periodontopathic microbiota in the longitudinal progression of ligature-induced periodontitis. Animals were immunized with cell envelope antigens prepared from Porphyromonas gingivalis and Prevotella intermedia, and a mixture prepared from Fusobacterium nucleatum, Campylobacter rectus, and Actinomyces viscosus. Serum immunoglobulin G (IgG), IgM and IgA isotype antibodies increased significantly in all immunization groups and were specific for each of the immunogens. P. gingivalis and P. intermedia immunization resulted in a stabilization of the proportions of these species throughout most of the experiment. The high P. gingivalis antibody titer resulted in low P. gingivalis numbers being recovered. P. gingivalis immunization, while lowering recoverable viable P. gingivalis, resulted in significantly increased levels of Prevotella loescheii, Prevotella buccae, Bacteroides macacae and Prevotella melaninogenica compared with preligation and preimmunization levels. Actinobacillus actinomycetemcomitans, Capnocytophaga spp. and Eikenella spp. remained at preligation levels postimmunization. Campylobacter spp. increased significantly during the course of the experiment in all groups, whereas the levels of Fusobacterium spp. decreased. Plaque indices and bleeding on probing showed significant increases in all groups following ligation, with the placebo group showing the greatest increase. Pocket depth measurements revealed that , whereas the placebo animals showed an approximate 5% increase, the P. gingivalis- and P. intermedia-immunized groups showed nearly a 20% increase in pocket depth. Attachment level measurements showed significantly greater attachment loss in the P. gingivalis- and P. intermedia-immunized groups, and the F. nucleatum + C. rectus + A. viscosus immunization appeared to prevent significant changes in pocket depth/attachment level loss. Radiographic measurement of bone loss by computer-assisted densitometric image analysis revealed that the placebo group lost bone throughout the experiment. P. gingivalis- and P. intermedia-immunized groups showed an exacerbated loss of bone density and the group immunized with F. nucleatum + C. rectus + A. viscosus exhibited significantly lower amounts of bone loss when analyzed by computer-assisted densitometric image analysis, compared with the other immunized groups. Although immunization with P. gingivalis and P. intermedia cell envelope antigens had an effect on their emergence in the complex microbiota of the developing periodontal pocket, this immunization also resulted in greater bone loss than immunization with F. nucleatum + C. rectus + A. viscosus, suggesting that, whereas selective members of the putative periodontopathic microbiota may play a direct role in periodontal tissue destruction, the complexity of the subgingival microbiota dictates that considerable scrutiny is required to select useful immunogens that can elicit functional protection from periodontal tissue destruction induced by oral microorganisms that already colonize or infect the host.

Actinomyces viscosus↗
PubMed1995

Comparative virulence of periodontopathogens in a mouse abscess model.

OBJECTIVE(S): This report compares the virulence of selected strains of P. gingivalis, A. actinomycetemcomitans, C. rectus, F. nucleatum and T. denticola in a murine model as a measure of pathogenic potential of these oral microorganisms. The characteristics of the tissue destruction associated with these monoinfections were then related to a potential model for bacterial synergism in progressing periodontitis. DESIGN AND METHODS: All bacterial strains were grown to mid-logarithmic to early stationary growth phase, harvested and used at various doses to challenge BALB/c normal and BALB/c dexamethasone (DEX) treated mice to mimic a neutrophil dysfunction. The characteristics of tissue destruction, and overt tissue destructive capacity of these species were examined as a function of challenge dose and time. OUTCOME MEASURES: The mice were examined for an interval of approximately 15 days post-challenge and the presence/absence of lesions, localized or generalized nature of the lesion (including size in mm2), and lethality of the infection were assessed. RESULTS: Comparison of the virulence of the various P. gingivalis strains related to lethality and lesion size associated with destruction of the connective tissue, indicated a virulence capacity of P. gingivalis strains 53977>W50 = T22>3079>33277>381. C. rectus elicited localized necrotic lesions which were limited to the epithelial layers of the skin. The size of the lesions also indicated a graded difference in virulence, such that C. rectus strains 234>576>>33238. A. actinomycetemcomitans caused the formation of classic localized abscesses with a PMN infiltrate and inflammatory exudates. Although each of the A. actinomycetemcomitans strains exhibited a similar virulence pattern in this murine model, A. actinomycetemcomitans serotype b representative strains were potentially more pathogenic with a virulence capacity of 3113D-N = 3975A>JP2 > or = Y4>29523>33384. Both C. rectus and A. actinomycetemcomitans strains showed clear evidence that recent clinical isolates were more virulent than laboratory strains. Challenge with F. nucleatum resulted in tissue destructive responses which were different from those observed with the other strains used in this study. A rapid onset of dose-dependent lesion development, related to the formation of either closed abscesses or open lesions, was observed with F. nucleatum. Tissue involvement was also greater at lower F. nucleatum doses when compared to the other bacteria. F. nucleatum challenge of DEX-treated mice resulted in a shift to open lesions. T. denticola appeared to be more tissue invasive than the other species examined in this study. Challenge of mice with T. denticola resulted in involvement of multiple tissues, including epithelial and connective tissues, as well as appearing to invade muscle layers and deeper tissues. In addition to invading deeper tissues, the resulting lesions took considerably longer to resolve. In the DEX-treated mice (neutrophil depleted), P. gingivalis, C. rectus, and A. actinomycetemcomitans were significantly more virulent. In contrast, while DEX treatment altered the characteristics of lesions caused by F. nucleatum, the extent of lesions produced by F. nucleatum and T. denticola was not substantially enhanced. CONCLUSIONS: The results obtained from this study suggest that different microorganisms have the ability to provide individual pathologies which may act in an additive/synergistic fashion contributing to the tissue destruction noted in periodontitis.

Abscess↗
PubMed1995

The 46-kilodalton-hemolysin gene from Treponema denticola encodes a novel hemolysin homologous to aminotransferases.

The 46-kDa hemolysin produced by Treponema denticola may be involved in the etiology of periodontitis. In order to initiate a genetic analysis of the role of this protein in disease, its gene has been cloned. Synthetic oligonucleotides, designed on the basis of the previously reported amino-terminal amino acid sequence of the 45-kDa hemolysin, were used as primers in a PCR to amplify part of the hemolysin (hly) gene. This PCR product was then used to clone the entire hly gene from libraries of T. denticola genomic DNA. Constructs containing the entire cloned region on plasmids in Escherichia coli produced both hemolysis and hemoxidation activities either on sheep blood agar plates or in liquid assays. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot (immunoblot) analysis revealed that the constructs synthesized a protein with molecular size of about 46 kDa which was reactive with anti-T. denticola hemolysin. Nucleotide sequence analysis indicated that the largest open reading frame could encode a protein with a calculated molecular size of 46.2 kDa. The first 31 amino acids encoded by this open reading frame were identical to the experimentally determined amino-terminal sequence of the 45-kDa hemolysin. These results indicate that the entire hly gene has been cloned. The deduced amino acid sequence of the T. denticola hly gene is homologous (23 to 37% identity) to those of proteins that are members of a family of pyridoxal-phosphate-dependent aminotransferases. This suggests that the 46-kDa hemolysin may be related to an aminotransferase and have a novel mechanism of hemolysis. However, the functional aspects of this relationship remain to be investigated.

Amino Acid Sequence↗
PubMed1994

Characterization of hemolysis and hemoxidation activities by Treponema denticola.

This study determined the presence of two hemolytic activities in the oral treponeme, Treponema denticola, strains ATCC 35404 (TD-4), ATCC 33520, GM-1, and MS25. These activities, referred to as hemolytic and hemoxidative (HeA, HeO, respectively), were found to be both secreted into the extracellular environment, and cell associated. The extracellular activity was associated with small molecules with relative molecular weights of < 1000 Da, and its activity was cysteine independent; the cell-associated HeA and HeO activities were associated with a molecular weight fraction > 10 kDa, and were cysteine dependent. The HeO activity of the fractionated material observed was due to the oxidation of hemoglobin to methemoglobin, and preceded the HeA lysis of the RBCs by approximately 2 h. Heating at 80 degrees C and treatment with proteinase K resulted in the complete destruction of these activities in the fraction > 10 kDa, while lipase at high concentration (800 micrograms/ml) reduced the HeA and HeO activities in the extracellular fraction by approximately 50%. Proteinase inhibitors had a variable effect on HeA and HeO activities in both extracellular and cell-associated fractions. Scanning and transmission electron microscopy revealed a progressive destruction of the RBC membrane, with membrane protrusions formed early in the interaction, which progressed to irregular holes in the membrane, and the complete loss of membrane integrity.

Erythrocytes↗
PubMed1994

Purification and characterization of a 45 kDa hemolysin from Treponema denticola ATCC 35404.

A 45 kDa polypeptide capable of erythrocyte (RBC) lysis and hemoglobin oxidation was isolated from Treponema denticola, ATCC 35404 (TD-4) after sequential ammonium sulfate (2.8-3.6 M) precipitation and preparative electrophoresis. The purified polypeptide produced a single protein band on PAGE at a relative molecular weight of 45 kDa in the presence and absence of SDS. The polypeptide was sensitive to proteinase K and pronase, and heating at 80 degrees C. The protease inhibitors, PMSF, TLCK and benzamidine had no inhibitory affect on activity. It was non heat-modifiable, and lost all hemolytic and hemoxidative function in SDS. Cysteine and other sulfhydryl-containing compounds were required for hemolytic and hemoxidative activities. The isoelectric point of the polypeptide was 5.3 and N'-terminal sequence analysis indicated it to belong to a new, so far undescribed group of peptides possessing hemoxidation and hemolytic activities. Functionally, it was capable of rapid hemoxidation of sheep and human erythrocytes (hemoglobin to methemoglobin) coupled to erythrocyte lysis, or hemolysis.

Amino Acid Sequence↗
PubMed1994

Effect of iron regulation on expression and hemin-binding function of outer-sheath proteins from Treponema denticola.

The effect of the iron-chelating compounds EDDA and BPD on polypeptide regulation in the putative oral pathogen Treponema denticola was studied. SDS-PAGE analysis of the T. denticola strains grown in the presence of EDDA or BPD, i.e. iron-limiting environmental conditions, revealed the expression of 44 and 43 kDa polypeptides in the outer sheath, a 73 kDa polypeptide in the cell membrane, and a 16 kDa polypeptide in the soluble cell fraction. The hemin-binding activity of purified outer sheaths from T. denticola TD-4 grown in the presence of 6.4 mM EDDA was significantly greater than that observed in control (absence of EDDA) outer sheaths. Both activities were inhibited by proteinase K. SDS-PAGE, LDS-PAGE and TMBZ staining revealed the 44 and 43 kDa outer-sheath polypeptides to be expressed by T. denticola strains GM-1. MS-25, ATCC 33520 and ATCC 33404 (TD-4), strains which possessed strong hemin-binding activity. The 44 kDa hemin-binding polypeptide was purified by 1% CHAPS solubilization, HPLC, and SDS-preparative electrophoresis. N'-terminal sequence analysis indicated the purified 44 kDa polypeptide to belong to a new, undescribed group of polypeptides possessing hemin-binding activity.

2,2'-Dipyridyl↗
PubMed1994

Cloning and expression of hemolysin genes from Treponema denticola strains ATCC 35404 (TD-4) and human clinical isolate GM-1 in Escherichia coli.

The oral spirochete, Treponema denticola is a putative etiologic agent in adult periodontitis, and acute necrotizing ulcerative gingivitis. In vitro, the oral treponeme produces several factors including proteases, hemolysins, hemin-binding proteins, which could potentially be involved in the virulence of this spirochete. Our laboratory has been investigating the pathobiology of T. denticola, and has demonstrated the production of several hemolysins by T. denticola. In this report two hemolysin genes from T. denticola strains ATCC 35404 (TD-4) and GM-1 were isolated by screening genomic DNA libraries of T. denticola on sheep blood agar plates. Physical maps of the insert fragments were not identical. Southern blot analyses suggested some degree of homology in the nucleotide sequence. Maxicell analyses of [35S]-methionine-labeled polypeptides from the recombinant plasmids have suggested the synthesis of an approximately 62.5 kDa polypeptide. Biochemical characterization of the T. denticola hemolysin genes indicated the activity to be inhibited by Mg2+, Ca2+ and Zn2+ but not by EDTA. Dithiothreitol and glutathione moderately enhanced the hemolytic activity of the recombinant plasmids. Iron partially inhibited the hemolytic activities. Addition of 2-2' bipyridyl moderately enhanced the activities, possibly by iron limitation. These results suggest the isolation of an identical hemolysin gene from T. denticola strains TD-4 and GM-1.

Animals↗
PubMed1994

Coaggregation between bacterial species.

Bacterial coaggregation, or interbacterial adherence, is one mechanism involved in the development of bacterial biofilms that are found on surfaces in nature. Assays used to measure coaggregation rely on the interaction of bacterial cells in suspension or attachment of one species to a second species that has been fixed to a solid substrate. Both semiquantitative and quantitative assays are described. These methods have also been used to determine the nature of the adherence and molecules involved in mediating the interaction, to characterize potential inhibitors, to isolate the bacterial adhesins and receptors, and to isolate adherence-deficient mutant strains. Each of the assay systems offers different advantages, with significant variations in sensitivity. Selection of a particular assay system should depend on the goals of the study to be performed.

Actinomyces↗
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↗