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
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
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).
Target data
Additional targets
Publications (1)
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International journal of environmental research and public health 19: PubMed36498280
2022
Applications
Unspecified application
Species
Unspecified reactive species
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