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AB43055

Recombinant Treponema pallidum p47 protein

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(1 Publication)

Recombinant Treponema pallidum p47 protein is a Treponema pallidum subsp. pallidum str. Nichols Fragment protein, expressed in Escherichia coli, with >90%, suitable for ELISA, WB.

View Alternative Names

Putative DD-carboxypeptidase TP_0574, 47 kDa lipoprotein, 47 kDa membrane antigen, 47-kilodalton major integral membrane immunogen, Tp47, Tpp47, TP_0574

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

ELISA, WB

applications

Biologically active

No

Accession

P29723

Animal free

No

Carrier free

No

Species

Treponema pallidum subsp. pallidum str. Nichols

Storage buffer

pH: 8 Constituents: 48% Urea, 0.158% Tris HCl, 0.0292% EDTA, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P29723","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The Treponema pallidum p47 protein also known as Tp47 functions as a protease integral to the bacterium Treponema pallidum which causes syphilis. It has a molecular mass of approximately 47 kDa. This protein expresses in the outer membrane of the bacterium playing a pivotal role in modulating host-pathogen interactions. Through its proteolytic activity Tp47 influences the bacterium's ability to evade the host's immune response facilitating chronic infection.
Biological function summary

Tp47 engages in processes assisting the bacterium to persist in its human host. This protein does not individually perform functions; it is a part of multi-protein complexes allowing the bacterium to interact with the human immune system. These interactions alter immune responses giving the bacterium a better chance of escaping detection or destruction by host defenses. Tp47's interactions with other proteins in these complexes set the stage for more varied effects on the host's physiological systems.

Pathways

Tp47 interacts with several key pathways in the host's immune system. These include the complement cascade pathway where Tp47's activity can impact the bacterium's chances of survival by interfering with complement-mediated lysis. Additionally researchers associate Tp47 with the oxidative burst process which plays a role in phagocytosis. Another protein TpN47 is related to the Tp47 activity through its role in these pathways assisting in masking the bacterium from immune cells.

Tp47 has a significant association with syphilis a chronic systemic infection. This protein's role in evading immune surveillance makes it a target for studying persistent treponemal infections. Additionally Tp47 connects to neurodegenerative pathways due to tertiary syphilis's potential impact on the nervous system. Understanding Tp47's interactions with proteins like TpN47 in these contexts can advance therapeutic strategies against sequelae of syphilis including neurological complications.

Specifications

Form

Liquid

Additional notes

Inclusion bodies.

General info

Function

A possible D,D-carboxypeptidase, that releases amino acids sequentially from a proteins C-terminus (PubMed : 12196546, PubMed : 7972112). Has zinc-dependent carboxypeptidase activity on synthetic depsipeptide substrates (PubMed : 7972112). May serve to decrease cross-linking of peptidoglycan, promoting the highly sinusous motility of this spirochaete (Probable). Overexpression of the whole protein in E.coli leads to aberrant cell morphology and extrusion of the cytoplasm, while overexpression of a construct with the first 62 resides of the protein fused to PhoA does have this effect, suggesting the whole protein, not the lipoprotein moiety, is toxic (PubMed : 7972112). Binds penicillin (PubMed : 2647634, PubMed : 7972112). Penicillin binding is covalent, does not require lipidation, and is zinc-dependent (PubMed : 12196546, PubMed : 7972112). While this protein has beta-lactamase activity in vitro, that is probably not its role in vivo, as T.pallidum is very sensitive to penicillin antibiotics (PubMed : 12196546).. A pathogen-specific membrane antigen (PubMed : 1372297, PubMed : 2642466). Most abundant of the membrane lipoproteins, only found in pathogenic treponemes, suggesting that it is an important structural moiety in the cell envelope of virulent treponemal subspecies. A lipopeptide corresponding to the first 6 mature residues induces host (human and mouse) cytokine release by monocyte cell lines via TLR2 and CD14; nonlipidated protein does not stimulate host cells (PubMed : 10426995). Stimulates host (human) dendritic cell maturation to become MHC class II-positive antigen presenting cells via TLR2, which depends on lipidation; nonlipidated protein does not stimulate maturation (PubMed : 11160304).

Post-translational modifications

The N-terminus is blocked (PubMed:2642466). Present as a doublet of low abundance 48 kDa and high abundance 47 kDa proteins (PubMed:1372297, PubMed:2647634, PubMed:2668192). The longer form is probably due to readthrough of the stop codon; the extra amino acids at the C-terminus would be X-Lys-Arg-Gly-Val-Leu-Ser-Arg-Val-Ser, a peptide antibody against this sequence detects only the 48 kDa form (PubMed:2668192).

Product protocols

Target data

A possible D,D-carboxypeptidase, that releases amino acids sequentially from a proteins C-terminus (PubMed : 12196546, PubMed : 7972112). Has zinc-dependent carboxypeptidase activity on synthetic depsipeptide substrates (PubMed : 7972112). May serve to decrease cross-linking of peptidoglycan, promoting the highly sinusous motility of this spirochaete (Probable). Overexpression of the whole protein in E.coli leads to aberrant cell morphology and extrusion of the cytoplasm, while overexpression of a construct with the first 62 resides of the protein fused to PhoA does have this effect, suggesting the whole protein, not the lipoprotein moiety, is toxic (PubMed : 7972112). Binds penicillin (PubMed : 2647634, PubMed : 7972112). Penicillin binding is covalent, does not require lipidation, and is zinc-dependent (PubMed : 12196546, PubMed : 7972112). While this protein has beta-lactamase activity in vitro, that is probably not its role in vivo, as T.pallidum is very sensitive to penicillin antibiotics (PubMed : 12196546).. A pathogen-specific membrane antigen (PubMed : 1372297, PubMed : 2642466). Most abundant of the membrane lipoproteins, only found in pathogenic treponemes, suggesting that it is an important structural moiety in the cell envelope of virulent treponemal subspecies. A lipopeptide corresponding to the first 6 mature residues induces host (human and mouse) cytokine release by monocyte cell lines via TLR2 and CD14; nonlipidated protein does not stimulate host cells (PubMed : 10426995). Stimulates host (human) dendritic cell maturation to become MHC class II-positive antigen presenting cells via TLR2, which depends on lipidation; nonlipidated protein does not stimulate maturation (PubMed : 11160304).
See full target information TP_0574

Additional targets

Treponema pallidum p47

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

International journal of environmental research and public health 19: PubMed36498280

2022

Development of a Cyclic Voltammetry-Based Method for the Detection of Antigens and Antibodies as a Novel Strategy for Syphilis Diagnosis.

Applications

Unspecified application

Species

Unspecified reactive species

Gabriel M C Barros,Dionísio D A Carvalho,Agnaldo S Cruz,Ellen K L Morais,Ana Isabela L Sales-Moioli,Talita K B Pinto,Melise C D Almeida,Ignacio Sanchez-Gendriz,Felipe Fernandes,Ingridy M P Barbalho,João P Q Santos,Jorge M O Henriques,César A D Teixeira,Paulo Gil,Lúcio Gama,Angélica E Miranda,Karilany D Coutinho,Leonardo J Galvão-Lima,Ricardo A M Valentim
View all publications

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