Treponema pallidum Major Sheath Protein Homologue Tpr K Is a Target of Opsonic Antibody and the Protective Immune Response

@article{CenturinLara1999TreponemaPM,
  title={Treponema pallidum Major Sheath Protein Homologue Tpr K Is a Target of Opsonic Antibody and the Protective Immune Response},
  author={Arturo Centuri{\'o}n-Lara and Christa Castro and Lynn K. Barrett and Caroline E. Cameron and Maryam Mostowfi and Wesley C. Van Voorhis and Sheila A. Lukehart},
  journal={The Journal of Experimental Medicine},
  year={1999},
  volume={189},
  pages={647 - 656}
}
We have identified a family of genes that code for targets for opsonic antibody and protective immunity in T. pallidum subspecies pallidum using two different approaches, subtraction hybridization and differential immunologic screening of a T. pallidum genomic library. Both approaches led to the identification of a polymorphic multicopy gene family with predicted amino acid homology to the major sheath protein of Treponema denticola. One of the members of this gene family, tpr K, codes for a… 

Figures and Tables from this paper

The Tprk Protein of Treponema pallidum Is Periplasmic and Is Not a Target of Opsonic Antibody or Protective Immunity
TLDR
Results challenge the notion that TprK will be a component of an efficacious syphilis vaccine, as it is conclusively demonstrated that native TPRK is entirely periplasmic.
Opsonic potential, protective capacity, and sequence conservation of the Treponema pallidum subspecies pallidum Tp92.
TLDR
It is demonstrated that Tp92 is an invariant, immunoprotective antigen that may be present on the surface of T. pallidum and may represent a potential vaccine candidate for syphilis.
Evaluation of the Protective Ability of the Treponema pallidum subsp. pallidum Tp0126 OmpW Homolog in the Rabbit Model of Syphilis
TLDR
The humoral and cellular responses to Tp 0126 during experimental and natural syphilis and the ability of Tp0126 to confer protection against syphilis in immunized rabbits are investigated and initial results pointed to a housekeeping function for this protein.
Systematic cloning of Treponema pallidum open reading frames for protein expression and antigen discovery.
TLDR
The potential of the T. pallidum clone set for antigen discovery and, more generally, for advancing the biology of this enigmatic spirochete is demonstrated.
Gene Organization and Transcriptional Analysis of the tprJ, tprI, tprG, and tprF Loci in Treponema pallidum Strains Nichols and Sea 81-4
ABSTRACT The tpr gene family of Treponema pallidum subsp. pallidum, the causative agent of syphilis, has recently become the focus of intensive investigation. TprF and TprI sequences are highly
Comparative Genomics and Full-Length TprK Profiling of Treponema pallidum subsp. pallidum Reinfection
TLDR
The results are consistent with an immunodominant-evasion model in which the diversity of TprK explains the ability of T. pallidum to successfully reinfect individuals, even when they have been infected with the organism multiple times.
Segregation of B and T Cell Epitopes of Treponema pallidum Repeat Protein K to Variable and Conserved Regions During Experimental Syphilis Infection1
TLDR
Abs from rabbits immunized with recombinant TprK recognized conserved and variable regions, suggesting that the conserved regions are inherently as immunogenic as the variable regions.
B-cell epitope mapping of TprC and TprD variants of Treponema pallidum subspecies
TLDR
This study identified B-cell epitopes across the full-length TprC and TprD variants using the Geysan pepscan mapping approach with antisera from rabbits infected with syphilis, yaws, and bejel strains and from animals immunized with refolded recombinant TPRC proteins from three syphilis strains.
Treponema pallidum, the stealth pathogen, changes, but how?
TLDR
It is suggested that T.’pallidum has appropriated a paradigmatic global regulator of metabolic processes in heterotrophic bacteria to further its capacity for immune evasion in its obligate human host.
...
...

References

SHOWING 1-10 OF 53 REFERENCES
Identification and sequence analysis of Treponema pallidum tprJ, a member of a polymorphic multigene family.
TLDR
Southern hybridization and genomic DNA sequence analysis indicate that tprJ is a member of a polymorphic multigeneFamily, the first report of significant sequence differences within homologous genes of T. pallidum and T. pertenue.
Identification of Treponema pallidum subspecies pallidum genes encoding signal peptides and membrane‐spanning sequences using a novel alkaline phosphatase expression vector
TLDR
A novel expression vector which confers the utility of TnphoA transposition is developed which includes an inducible tac promoter, a polylinker with multiple cloning sites in three reading frames, and an alkaline phosphatase (AP) gene lacking the signal sequence‐encoding region.
Recombinant Treponema pallidum rare outer membrane protein 1 (Tromp1) expressed in Escherichia coli has porin activity and surface antigenic exposure
TLDR
These findings demonstrate that rTromp1 can be targeted to the E. coli outer membrane, where it has both porin activity and surface antigenic exposure.
Treponema pallidum and the quest for outer membrane proteins
TLDR
It is now believed that the T. pallidum outer membrane (OM) contains a paucity of poorly immunogenic transmembrane proteins (‘rare outer membrane proteins’) and that its highly immunogentc proteins are lipoproteins anchored predominantly to the periplasmic leaflet of the cytoplasmic membrane.
Sequence analysis and recombinant expression of a 28-kilodalton Treponema pallidum subsp. pallidum rare outer membrane protein (Tromp2)
TLDR
It is demonstrated that Tromp2 is a membrane-spanning outer membrane protein, the second such protein to be identified for T. pallidum.
Identification of the Treponema pallidum subsp. pallidum glycerophosphodiester phosphodiesterase homologue.
TLDR
An immunoreactive clone containing an open reading frame encoding a 356 residue protein was identified as a homologue of glycerophosphodiester phosphodiesterase, a glycerol metabolizing enzyme previously identified in Haemophilus influenzae, Escherichia coli, Bacillus subtilis and Borrelia hermsii.
Sequence analysis, expression, and binding activity of recombinant major outer sheath protein (Msp) of Treponema denticola
TLDR
Northern (RNA) blot analysis showing the msp transcript to be approximately 1.7 kb was consistent with the identification of a promoter consensus sequence located optimally upstream of msp and a transcription termination signal found downstream of the stop codon, lending further support to the hypothesis that Msp mediates the extracellular matrix binding activity of T. denticola.
Identification of homologs for thioredoxin, peptidyl prolyl cis-trans isomerase, and glycerophosphodiester phosphodiesterase in outer membrane fractions from Treponema pallidum, the syphilis spirochete
TLDR
Describing candidate rare outer membrane (OM) proteins with apparent molecular masses of 19, 27, 38, and 38.5 kDa provides fresh insights into a poorly understood aspect of treponemal physiology and raises important issues regarding the use of OM preparations for identifying rare OM proteins of T. pallidum.
The outer membrane, not a coat of host proteins, limits antigenicity of virulent Treponema pallidum
TLDR
A new model is proposed for T. pallidum ultrastructure in which the outer membrane contains a small number of transmembrane proteins and the major membrane immunogens are anchored by lipids to the periplasmic leaflet of the cytoplasmic membrane.
Demonstration of rare protein in the outer membrane of Treponema pallidum subsp. pallidum by freeze-fracture analysis
TLDR
The unique molecular architecture of the OM of T. pallidum can explain the puzzling in vitro properties of the surface of the organism and may reflect a specific adaptation by which treponemes evade the host immune response.
...
...