Difference between revisions of "Part:BBa K3582001"
 
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Plasmodium species of parasite uses a set of adhesive proteins, called the PfEMP1, which are expressed on the surfaces of infected red blood cells, causing them to bind to blood vessels and tissues. The PfEMP1 are among the few parasite proteins constantly exposed to the host immune system during the blood phase of the parasite life cycle. Due to increasing selective pressure, this group of proteins have expanded into a complex protein family, with around 60 members in each parasite genome and a system of antigenic variation that allows parasites to switch which PfEMP1 they expose to the immune system. Antibodies that bind PfEMP1 are found in people from malaria-endemic regions and correlate with immunity from severe disease.
 
Plasmodium species of parasite uses a set of adhesive proteins, called the PfEMP1, which are expressed on the surfaces of infected red blood cells, causing them to bind to blood vessels and tissues. The PfEMP1 are among the few parasite proteins constantly exposed to the host immune system during the blood phase of the parasite life cycle. Due to increasing selective pressure, this group of proteins have expanded into a complex protein family, with around 60 members in each parasite genome and a system of antigenic variation that allows parasites to switch which PfEMP1 they expose to the immune system. Antibodies that bind PfEMP1 are found in people from malaria-endemic regions and correlate with immunity from severe disease.
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For the facilitation of endothelial binding, PfEMP1 proteins contain huge extracellular ectodomains consisting of 2–10 copies of two domain types, the Duffy-binding like (DBL) and cysteine-rich interdomain region (CIDR) domains. Interestingly, it is found that these domains are extremely variable in sequence, yet they share a conserved architecture and can be classified into different subgroups based on the sequence.
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For the facilitation of endothelial binding, PfEMP1 proteins contain huge extracellular ectodomains consisting of 2–10 copies of two domain types, the Duffy-binding like (DBL) and cysteine-rich interdomain region (CIDR) domains. Interestingly, it is found that these domains are extremely variable in sequence, yet they share a conserved architecture and can be classified into different subgroups based on the sequence.The CIDRa2 domains have a hydrophobic pocket that binds to a protruding phenylalanine residue from CD36. This biobrick allows us to synthesize the CIDRa Domain of MC variant of PfEMP1 protein to study the interaction. A strep II tag is inserted in the end for ease of purification.
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A zoomed view of the binding interfaces that mediate the CIDRa2: CD36 interaction. The CIDRa2 domains have a hydrophobic pocket that binds to a protruding phenylalanine residue from CD36. This biobrick allows us to synthesize the CIDRa Domain of MC variant of PfEMP1 protein to study the interaction. A strep II tag is inserted in the end for ease of purification
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[[Image:1 BBa K3582001.png|250px|thumb|center|Figure 1.A zoomed view of the binding interfaces that mediate the CIDRa2: CD36 interaction.(PDB:5LGD-Fu-Lien Hsieh1 et al.) ]]
  
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[[Image:Inhibitory sequence 2.png|900px|thumb|center|Figure 1. DNA sequence of the inhibitory peptide sequence 2 with its translation output.]]
 
  
  
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[[Image:2 BBa K3582001.png|400px|thumb|center|Figure 2.Structure of the CIDRa domain from MCvar1 PfEMP1 visualized using Chimera ]]
  
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[[Image:Is22 BBa K3582013.png|400px|thumb|center|Figure 1.Interacting regions of the PfEMP1 CIDRa domain and the inhibitory peptide sequence 2 shown here in protein ribbon model.]]
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[[Image:5 BBa K3582002.gif|500px|thumb|center|Figure 1. Structure of CD36(Red) interacting with CIDRa domain of MCvar1 PfEMP1 protein(Blue).]]
  
  
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
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===References===
 
===References===
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*1] The structural basis for CD36 binding by the malaria parasite.
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* 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
 
Fu-Lien Hsieh1, Louise Turner2, Jani Reddy Bolla3, Carol V. Robinson3, Thomas Lavstsen2 & Matthew K. Higgins1
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*2]https://sci-hub.st/10.1002/ange.201406563
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* Gardner, M. J. et al. Genome sequence of the human malaria parasite Plasmodium falciparum. Nature 419, 498–511 (2002).
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* Chan, J. A. et al. Targets of antibodies against Plasmodium falciparum-infected erythrocytes in malaria immunity. J. Clin. Invest. 122, 3227–3238 (2012).
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===Functional Parameters===
 
===Functional Parameters===
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<partinfo>BBa_K3582013 parameters</partinfo>
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<partinfo>BBa_K3582001 parameters</partinfo>
 
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Latest revision as of 03:44, 28 October 2020

The CIDRa domain from MCvar1 PfEMP1

Plasmodium species of parasite uses a set of adhesive proteins, called the PfEMP1, which are expressed on the surfaces of infected red blood cells, causing them to bind to blood vessels and tissues. The PfEMP1 are among the few parasite proteins constantly exposed to the host immune system during the blood phase of the parasite life cycle. Due to increasing selective pressure, this group of proteins have expanded into a complex protein family, with around 60 members in each parasite genome and a system of antigenic variation that allows parasites to switch which PfEMP1 they expose to the immune system. Antibodies that bind PfEMP1 are found in people from malaria-endemic regions and correlate with immunity from severe disease. For the facilitation of endothelial binding, PfEMP1 proteins contain huge extracellular ectodomains consisting of 2–10 copies of two domain types, the Duffy-binding like (DBL) and cysteine-rich interdomain region (CIDR) domains. Interestingly, it is found that these domains are extremely variable in sequence, yet they share a conserved architecture and can be classified into different subgroups based on the sequence.The CIDRa2 domains have a hydrophobic pocket that binds to a protruding phenylalanine residue from CD36. This biobrick allows us to synthesize the CIDRa Domain of MC variant of PfEMP1 protein to study the interaction. A strep II tag is inserted in the end for ease of purification.

Figure 1.A zoomed view of the binding interfaces that mediate the CIDRa2: CD36 interaction.(PDB:5LGD-Fu-Lien Hsieh1 et al.)


Figure 2.Structure of the CIDRa domain from MCvar1 PfEMP1 visualized using Chimera
Figure 1. Structure of CD36(Red) interacting with CIDRa domain of MCvar1 PfEMP1 protein(Blue).


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
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]

References

  • 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

  • Gardner, M. J. et al. Genome sequence of the human malaria parasite Plasmodium falciparum. Nature 419, 498–511 (2002).
  • Chan, J. A. et al. Targets of antibodies against Plasmodium falciparum-infected erythrocytes in malaria immunity. J. Clin. Invest. 122, 3227–3238 (2012).