Difference between revisions of "Part:BBa K3009021"

Latest revision as of 13:48, 21 October 2019

FPR2-receptor with mCherry

The human N-formyl peptide receptor 2 (FPR2) is a G-protein coupled receptor (GPCR) which is expressed on immune cell lineages like neutrophils and T-cells. Amongst other peptides, FPR2 senses the Staphylococcus aureus toxin PSMɑ3. It was proposed by Cheung et al (2014) that the PSMɑ3 FPR2 receptor interaction supposedly occurs via the formylated N- or the C-terminus of the peptide.[1] In response to receptor activation FPR2 elicits a signaling cascade depending on calcium ions as second messengers. Ultimately, this leads to immune cell activation, secretion of inflammatory cytokines and chemotaxis resulting in an inflammatory outcome. Neutrophil chemotaxis is triggered by PSM interaction with the FPR2 receptor [2] leading to an aggravation of the inflammation related symptoms in Staphylococcus aureus infection.

We provide here a BioBrick that can be used in signaling studies and the cellular detection of several small formylated amyloidogenic peptides. Commercially available peptide with inhibitory (WRWW4) and activating (WKYMVm) effect on FPR2 to test receptor activity without using a toxin.

The presence of FPR2 on transfected cells can be analyzed by fluorescence microscopy and flow cytometry via the attached mCherry reporter.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
INCOMPATIBLE WITH RFC[21]
Illegal BamHI site found at 1063
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K3009021 short</partinfo>
-The human formyl peptide receptor 2 (FPR2) is a G-protein coupeled receptor which is physiologically expressed on immune cell lineages like neutrophils and T-cells. Amongst other peptides the FPR2 senses the staphylococcus aureus toxin PSMa3. It was suggested by Cheung et al 2014 that the binding mechanism relies on the formylated N-terminus of the peptide as well as on the C-terminus. In response to receptor activation FPR2 elicits a signalling cascade depending on calcium ions as second messengers. Ultimately this leads to immune cell activation, secretion of inflammatory cytokines and chemotaxis. All of this is connected with an inflammatory outcome in vivo. The neutrophil activation by FPR2 is therefore an important mechanism of its toxicity because it leads to an aggravation of the inflammation related symptoms in Staphylococcus aureus infection
+The human N-formyl peptide receptor 2 (FPR2) is a G-protein coupled receptor (GPCR) which is expressed on immune cell lineages like neutrophils and T-cells. Amongst other peptides, FPR2 senses the <i>Staphylococcus aureus</i> toxin PSMɑ3. It was proposed by Cheung et al (2014) that the PSMɑ3 FPR2 receptor interaction supposedly occurs via the formylated N- or the C-terminus of the peptide.[1] In response to receptor activation FPR2 elicits a signaling cascade depending on calcium ions as second messengers. Ultimately, this leads to immune cell activation, secretion of inflammatory cytokines and chemotaxis resulting in an inflammatory outcome. Neutrophil chemotaxis is triggered by PSM interaction with the FPR2 receptor [2] leading to an aggravation of the inflammation related symptoms in <i>Staphylococcus aureus</i> infection.
-This Biobrick can be used in signalling studies or the cellular detection of several small formylated amyloidogenic peptides. As a controls two peptides with  inhibitry (WRWW4) and activating (WKYMVm) effect on FPR2 are availabe.
+We provide here a BioBrick that can be used in signaling studies and the cellular detection of several small formylated amyloidogenic peptides. Commercially available peptide with inhibitory (WRWW4) and activating (WKYMVm) effect on FPR2 to test receptor activity without using a toxin.
+The presence of FPR2 on transfected cells can be analyzed by fluorescence microscopy and flow cytometry via the attached mCherry reporter.
-The presence of FPR2 in transfected cells can be checked by flurescence microscopy and FACS. If no anti FPR2 antibody is available a high resolution microscope can even help to determine if FPR2 is located at the membrane, relying on the mCherry reporter.
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