The Eighth C. L. Oakley Lecture: Pathogenicity and immunobiology of Treponema pallidum

Penn, Charles W.

doi:10.1099/00222615-24-1-1

Cited by 11 publications

(5 citation statements)

References 6 publications

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“…2), similar to cytoplasmic filament subunit proteins described by Masuda and Kawata (25) for T. phagedenis and several other spirochetes. The single-and two-dimensional gel migration characteristics of this protein are very similar to those of the T. pallidum polypeptide previously described as TpN83, which comprises 3 to 5% of the total cellular protein of T. pallidum (29,32). Other bands present in the T. phagedenis cytoplasmic filament preparation may represent degraded or otherwise modified forms of the 80-kDa protein (32), flagellar basal body or basal plate constituents, or other polypeptides associated with the cytoplasmic filaments.…”

Section: Resultsmentioning

confidence: 54%

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

You¹,

Elmore²,

Colton³

et al. 1996

J Bacteriol

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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 ϳ80,000. 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 70 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.Spirochetes possess a number of unusual structural features, including helical or flat plane-wave shape and periplasmic flagella that tightly entwine the cell body and are encased by the outer membrane (13-16, 19, 31, 41). T. pallidum differs from other spirochetes in that it contains relatively few intramembranous protein particles in its outer membrane, as determined by freeze-fracture electron microscopy (33, 40). Seven of eight Treponema species examined, some Spirochaeta species, and Leptonema illini have also been shown to contain cytoplasmic filaments (also called cytoplasmic tubules and cytoplasmic fibrils) (14). Cytoplasmic filaments are ribbon-like structures 7.0 to 7.5 nm wide that run the length of the organism (5, 13-16, 19, 25, 31, 41). An array of 4 to 6 filaments lie in close apposition to the inner membrane and are always localized directly underneath the corresponding group of periplasmic flagella. The function of the cytoplasmic filaments is unknown. Their location indicates that they may be involved in cell motility, although other functions related to helical morphology or cell division are also possible (5).Masuda and Kawata (25) purified the cytoplasmic filaments of Treponema denticola TD-2, Treponema phagedenis biotypes Reiter and Kazan, three Treponema sp. strains (E-21,...

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Section: Resultsmentioning

confidence: 54%

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

You¹,

Elmore²,

Colton³

et al. 1996

J Bacteriol

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“…The T. pallidum outer membrane particles appear to be uniform in size, leading to the hypothesis that there are only a few different protein species in the outer membrane (180,234). It is thought that a low concentration of surface-exposed protein antigens may permit T. pallidum to evade the immune response, thereby contributing to its pathogenesis (25,43,160,164,180,198,233,234). Physiology T. pallidum is an obligate parasite of humans and is one of the few bacteria that are pathogenic to humans and have not been cultured continuously in vitro.…”

Section: Structurementioning

confidence: 99%

“…Surface radioiodination has yielded highly variable results and seems to be unreliable in identifying surface-localized proteins (3, 135,153,161). Treatment of T. pallidum with Triton X-100 or Triton X-114 appears to selectively solubilize the outer membrane (34,47,160,161,165,174,178…”

Section: Tpnl2dmentioning

confidence: 99%

Polypeptides of Treponema pallidum: progress toward understanding their structural, functional, and immunologic roles. Treponema Pallidum Polypeptide Research Group.

Norris

1993

Microbiological Reviews

116

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confidence: 99%

“…Freeze fracture electron microscopy has revealed that the outer membranes of pathogenic spirochetes contain amounts of integral membrane protein that are 1 to 2 orders of magnitude less than those of gram-negative bacteria (45,54,55). This striking feature has been suggested to be a key factor in the pathogenicity of these organisms by contributing to their ability to evade the host immune response and to establish chronic infection (11,15,38,45,54,55).The outer membrane of T. pallidum has an extremely low content of membrane-spanning protein (45, 55), a finding which has explained the surface antigenic inertness (18,20,25,40,43) of this spirochete and its relative resistance to bactericidal antibody (9,20,32,33,43). Freeze fracture electron microscopy has shown that the T. pallidum rare outer membrane protein (TROMP) molecules have surface-exposed antigenic sites, evidenced by immune-serum-mediated aggregation of TROMP molecules (11).…”

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confidence: 99%

Isolation of the outer membranes from Treponema pallidum and Treponema vincentii

et al. 1994

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The outer membranes from Treponema pallidum subsp. pa~idum and Treponema vincentii were isolated by a novel method. Purified outer membranes from T. palidum 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 extremel 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. 1251-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 pl), 31 (basic pl), 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. paUidum 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 KCI of 0.40 and 0.76 nS, respectively.The outer membranes of spirochetes, including that of Treponema pallidum subsp. pallidum, the agent of syphilis, are fragile compared with those of typical gram-negative bacteria (17,22,24,39,42,49). Spirochetal outer membranes bleb from the underlying protoplasmic cylinder under relatively mild conditions, including dilute detergents and hypotonic environments (24). Freeze fracture electron microscopy has revealed that the outer membranes of pathogenic spirochetes contain amounts of integral membrane protein that are 1 to 2 orders of magnitude less than those of gram-negative bacteria (45,54,55). This striking feature has been suggested to be a key factor in the pathogenicity of these organisms by contributing to their ability to evade the host immune response and to establish chronic infection (11,15,38,45,54,55).The outer membrane of T. pallidum has an extremely low content of membrane-spanning protein (45, 55), a finding...

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The Eighth C. L. Oakley Lecture: Pathogenicity and immunobiology of Treponema pallidum

Cited by 11 publications

References 6 publications

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

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

Polypeptides of Treponema pallidum: progress toward understanding their structural, functional, and immunologic roles. Treponema Pallidum Polypeptide Research Group.

Isolation of the outer membranes from Treponema pallidum and Treponema vincentii

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