Difference between revisions of "Part:BBa K3582002"
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It is also the most common target of the PfEMP1 proteins of the malaria parasite, Plasmodium falciparum, tethering parasite-infected erythrocytes to endothelial receptors. The scavenger receptor, CD36 binds to many classes of CIDRa domain (CIDRa2-6). It is also the host receptor most commonly found to interact with parasite isolates from patients and with laboratory-adapted parasite strains. Interestingly, approximately 84% of PfEMP1 proteins contain domains predicted to bind to CD36, making this the most common adhesion phenotype. The increase in the frequency of CD36 binding shows that it is advantageous to the parasite, allowing the avoidance of splenic clearance. CD36 binding may also benefit the parasite by providing a mechanism to reduce dendritic cell-mediated T-cell activation, hampering the capacity of the host immune system to clear the infection. So, in order to study these interactions between CD36 and PfEMP1 CIDR domain, we plan to synthesize the CD36 interaction protein using this biobrick and purify it using the grafted strep II tag.
 
It is also the most common target of the PfEMP1 proteins of the malaria parasite, Plasmodium falciparum, tethering parasite-infected erythrocytes to endothelial receptors. The scavenger receptor, CD36 binds to many classes of CIDRa domain (CIDRa2-6). It is also the host receptor most commonly found to interact with parasite isolates from patients and with laboratory-adapted parasite strains. Interestingly, approximately 84% of PfEMP1 proteins contain domains predicted to bind to CD36, making this the most common adhesion phenotype. The increase in the frequency of CD36 binding shows that it is advantageous to the parasite, allowing the avoidance of splenic clearance. CD36 binding may also benefit the parasite by providing a mechanism to reduce dendritic cell-mediated T-cell activation, hampering the capacity of the host immune system to clear the infection. So, in order to study these interactions between CD36 and PfEMP1 CIDR domain, we plan to synthesize the CD36 interaction protein using this biobrick and purify it using the grafted strep II tag.
  
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[[Image:Inhibitory sequence 2.png|900px|thumb|center|Figure 1. Structure of CD36 human platelet glycoprotein modelled using Chimera (PDB:5LGD-Fu-Lien Hsieh1 et al.)]]
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[[Image:CD36 BBa K3582002.png|750px|thumb|center|Figure 1. Structure of CD36 human platelet glycoprotein modelled using Chimera (PDB:5LGD-Fu-Lien Hsieh1 et al.)]]
  
  

Revision as of 15:04, 18 October 2020


CD36 (HUMAN PLATELET GLYCOPROTEIN 4)

CD36 is a scavenger receptor play a crucial role in fatty acid metabolism, innate immunity and angiogenesis. This glycoprotein molecule s popularly known for its versatile nature as it targets a broad range of ligands. Several ligands are that are a potential target of CD36 include thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides. Their multivalent nature allows them to engage multiple receptors that play an important role in signal transduction and forming complexes. CD36 is found to be a major player in the following processes:

  • 1]Angiogenesis
  • 2]Inflammatory response
  • 3]Fatty acid metabolism
  • 4]Proximal absorption of dietary fatty acids and cholesterol
  • 5]Activation of signal pathways via MAPK1/3 (ERK1/2), TICAM1, MYD88 etc

It is also the most common target of the PfEMP1 proteins of the malaria parasite, Plasmodium falciparum, tethering parasite-infected erythrocytes to endothelial receptors. The scavenger receptor, CD36 binds to many classes of CIDRa domain (CIDRa2-6). It is also the host receptor most commonly found to interact with parasite isolates from patients and with laboratory-adapted parasite strains. Interestingly, approximately 84% of PfEMP1 proteins contain domains predicted to bind to CD36, making this the most common adhesion phenotype. The increase in the frequency of CD36 binding shows that it is advantageous to the parasite, allowing the avoidance of splenic clearance. CD36 binding may also benefit the parasite by providing a mechanism to reduce dendritic cell-mediated T-cell activation, hampering the capacity of the host immune system to clear the infection. So, in order to study these interactions between CD36 and PfEMP1 CIDR domain, we plan to synthesize the CD36 interaction protein using this biobrick and purify it using the grafted strep II tag.

Figure 1. Structure of CD36 human platelet glycoprotein modelled using Chimera (PDB:5LGD-Fu-Lien Hsieh1 et al.)


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 169
    Illegal AgeI site found at 1129
    Illegal AgeI site found at 1255
    Illegal AgeI site found at 1303
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 1418

References

  • 1] The structural basis for CD36 binding by the malaria parasite.

Fu-Lien Hsieh1, Louise Turner2, Jani Reddy Bolla3, Carol V. Robinson3, Thomas Lavstsen2 & Matthew K. Higgins1