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Treponema denticola outer sheath protein (Msp) inhibits the binding step of collagen phagocytosis in fibroblasts

Andre Paes Batista da Silva

Treponema denticola outer sheath protein (Msp) inhibits the binding step of collagen phagocytosis in fibroblasts

by Andre Paes Batista da Silva

  • 313 Want to read
  • 19 Currently reading

Published in 2003 .
Written in English


Edition Notes

Statementby André Paes Batista da Silva.
The Physical Object
Paginationvii, 120 leaves :
Number of Pages120
ID Numbers
Open LibraryOL20775494M
ISBN 100612842452

The proteolytic, chemotactic and flagellar proteins of T. denticola promote the migration of the bacterium through connective tissues (Grenier et al., ; Lux et al., ), thereby facilitating direct contact of host cells with the shed bacterial outer sheath. The major outer sheath protein (Msp) of T. denticola (NCBI accession number. The Treponema denticola outer membrane lipoprotein-protease complex (dentilisin) contributes to periodontal disease by degrading extracellular matrix components and disrupting intercellular host signaling pathways. We recently demonstrated that prcB, located upstream of and cotranscribed with prcA and prtP, encodes a kDa lipoprotein that interacts with PrtP and is .

Chemical and biological activities of a kilodalton outer sheath protein from Treponema denticola strains. J Bacteriol Google Scholar | Crossref | Medline | ISI. PF usually reside within the periplasmic space of T. denticola as they wrap around the cell cylinder or may protrude from the cell within an intact outer membrane sheath (28, 34, 54). Early 20th century accounts of PF protrusions were reported by Noguchi with cultures of various Treponema species (55, 56).

Treponema denticola is considered an important oral pathogen in the development and progression of periodontal diseases. In the present study, the mechanisms of recognition and activation of murine macrophages by T. denticola and its major outer sheath protein (MSP) and lipooligosaccharide (LOS or glycolipid) were investigated. T. denticola cells and the MSP . Treponema pallidum, the syphilis spirochaete, has a remarkable ability to evade the humoral and cellular responses it elicits in infected hosts. Although formerly .


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Treponema denticola outer sheath protein (Msp) inhibits the binding step of collagen phagocytosis in fibroblasts by Andre Paes Batista da Silva Download PDF EPUB FB2

Coaggregation of Treponema denticola with Porphyromonas gingivalis and Fusobacterium nucleatum is mediated by the major outer sheath protein of Treponema denticola. FEMS Microbiol Lett59– /jx Simonson L. G Cited by: Protein and proteolytic patterns of the vesicles were found to be very similar to those of isolated T.

denticola outer sheaths. They were enriched with the major outer sheath polypeptides (molecular sizes, to kDa) and with outer sheath proteases of 91, and by: The major outer sheath protein (Msp) of Treponema denticola perturbs actin dynamics in fibroblasts by inducing actin reorganization, including subcortical actin filament assembly, leading to defective calcium flux, diminished integrin engagement of collagen, and retarded cell migration.

Yet, its mechanisms of action are unknown. We challenged Rat-2 fibroblasts with enriched Cited by: outer-sheath protein with pore-forming properties; A number of studies have observed an increase of T.

denticola in patients with orthodontic appliances, particularly the fixed type. Oral Cancer. Treponema Denticola is a potential etiological bacterial agent for oral : Bacteria. Coagreggation of Treponema denticola with either Porphyromonas gingivalis or Fusobacterium nucleatum was characterized and the role of the major outer sheath protein (MSP) in the coaggregation process of these bacteria was evaluated.

The MSP of T. denticola was found to be able to bind to P. gingivalis and F. nucleatum cells and this binding could be Cited by: Outer sheath vesicles. Factor H binding protein. Immunomodulation factors. These virulence factors are discussed as follows, Major sheath protein (Msp) The major outer sheath protein (Msp) is a primary virulence determinant in T.

denticola. It is the principal immunogenic surface antigen that forms oligomeric protein complexes in the outer. Msp, a member of the Tpr (T. pallidum repeat) protein family, is the most abundant protein in the T. denticola outer membrane (or sheath) and is one of the most-studied T.

denticola proteins. It is a β-barrel, integral outer sheath protein that acts as a porin and has surface-exposed loops that are able to bind to a variety of host proteins. Bacterial strains and growth conditions. denticola strains ATCC (TD4), ATCCand GM-1, and T.

denticola mutants K1 (lacking the outer sheath dentilisin protease) and MHE (lacking the major outer sheath protein [MSP]) (), were grown in GM-1 medium in a Bactron anaerobic (85% N 2, 10% H 2, and 5% CO 2) environmental chamber (Sheldon Manufacturing.

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 protein that is predicted to have a cleavable signal peptide and be located in the outer membrane of the bacterium.

The finding that Treponema pallidum, the syphilis spirochete, contains 12 orthologs of the Treponema denticola outer membrane major sheath protein has engendered speculation that members of this T.

pallidum repeat (Tpr) family may be similarly surface exposed. In this regard, the TprK protein was reported to be a target of opsonic antibody and protective immunity and. Treponema denticola is a major etiologic agent of chronic periodontitis.

On the outer sheath of T. denticola, several proteins, such as the major outer sheath protein and dentilisin were detected, and among them, a 95 kDa protein which has not yet been characterized. The aim of this study was to characterize the function of this 95 kDa protein containing gene cluster.

Immunofluorescent analysis of T. denticola embedded with agarose gel droplets showed that the labeling pattern of the intact Treponema is much weaker than that of the Treponema treated with % Triton X which is sufficient to permeabilize the outer sheath.

This result suggested that only minor parts of the Msp are exposed on the outer sheath. Treponema (T.) denticola is one of the key etiological agents in the development of major outer sheath protein (Msp) of T. denticola has been shown to mediate pathogenesis and to facilitate adhesion of T.

denticola to mucosal surfaces. This study aimed to find short polypeptides in the amino acid sequence of Msp which may be. Treponema denticola, one of several recognized periodontal pathogens, is a model organism for studying Treponema physiology and host-microbe interactions.

Its major surface protein Msp (or MOSP) comprises an oligomeric outer membrane-associated complex that binds fibronectin, has cytotoxic pore-forming activity, and disrupts several intracellular responses.

The T. denticola Msp protein was shown to be an outer membrane porin, with binding properties to host cell surface proteins [4,5,12]. Further it was reported that the Msp protein forms a hexagonal array in the outer sheath, however, this could.

This study examined the distribution of the major outer sheath proteins (MOSP) in several Treponema denticola strains andreports the isolation ofakDaprotein fromthe outer sheath ofhumanclinical isolate T.

denticola GM The outer sheath was isolated by freeze-thaw procedures, and the distribution of outer sheath proteins wasexamined. Rosen G, Genzler T, Sela MN () Coaggregation of Treponema denticola with Porphyromonas gingivalis and Fusobacterium nucleatum is mediated by the major outer sheath protein of Treponema denticola.

FEMS Microbiol Lett. Welcome to Knowledge genie!. Bringing the latest insights and key developments in medical education to Physicians and the medical community. This chapter reviews current progress in applying Treponema denticola genome information to the research areas and suggests some topics that have yet to be addressed adequately by the research community.

A group of seven genes was identified by homology with TP, a fibronectin-binding protein of T. pallidum. While five of these proteins showed at least some.

The major outer sheath protein (Msp) is a primary virulence determinant in Treponema denticola, as well as the parental ortholog for the Treponema pallidum repeat (Tpr) family in the syphilis spirochete.

The Conserved Domain Database (CDD) server revealed that Msp contains two conserved domains, major outer sheath protein N (MOSP N) and MOSP C, spanning.

The recent discovery that the Treponema pallidum genome encodes 12 orthologs of the Treponema denticola major sheath protein (Msp) prompted us to reexamine the cellular location and topology of the T. denticola polypeptide. Experiments initially were conducted to ascertain whether Msp forms an array on or within the T.

denticola outer membrane.The major outer sheath protein of Treponema denticola inhibits the binding step of collagen phagocytosis in fibroblasts. Cell Microbiol ; Jobin MC, Virdee I, McCulloch CA, Ellen RP.

Activation of MAPK in fibroblasts by Treponema denticola major outer sheath protein. Biochem Biophys Res Commun ;Abstract. The pore-forming major surface protein (Msp) and the chymotrypsin-like protease (CTLP) of Treponema denticola ATCC have been implicated in periodontal pathogenicity.

Allelic replacement mutations were constructed at two sites in the msp gene and at one site in the CTLP locus. All mutant strains lacked the Msp hexagonal array outer membrane ultrastructure.