Difference between revisions of "Part:BBa K4040019"

(Experimental results)
(A Broad-spectrum neutralizing antibody)
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==Experimental results==
 
==Experimental results==
 
===A Broad-spectrum neutralizing antibody===
 
===A Broad-spectrum neutralizing antibody===
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  <li style="display: inline-block;"> [[File:T--NMU_China--CR3022bindstoRBD.jpeg|thumb|none|250px|<b>Figure 1:</b> Crystal structure of SARS-CoV receptor binding domain in complex with human antibody CR3022. The structure has been resolved <html><a href="#1">[1]</a></html> available in PDB with 7JN5 accession number 7JN5.]] </li>
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===Binding to RBD on the spike protein===
 
===Binding to RBD on the spike protein===
  

Revision as of 02:27, 28 September 2021


CR3022 scFv 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 NgoMIV site found at 352
    Illegal NgoMIV site found at 688
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 568

Usage and Biology

CR3022 is a SARS-CoV neutralizing antibody to a highly conserved epitope on the receptor-binding domain (RBD) on the spike protein that is able to cross-react with SARS-CoV-2. A single-chain variable fragment (scFv) is not actually a fragment of an antibody, but instead is a fusion protein of the variable regions of the heavy (VH) and light chains (VL) of immunoglobulins, connected with a short linker peptide of ten to about 25 amino acids. The linker is usually rich in glycine for flexibility, as well as serine or threonine for solubility, and can either connect the N-terminus of the VH with the C-terminus of the VL or vice versa. This protein retains the specificity of the original immunoglobulin, despite the removal of the constant regions and the introduction of the linker. These molecules were created to facilitate phage display, where it is highly convenient to express the antigen-binding domain as a single peptide. As an alternative, scFv can be created directly from subcloned heavy and light chains derived from a hybridoma. ScFvs have many uses, e.g., flow cytometry, immunohistochemistry, and as antigen-binding domains of artificial T cell receptors (chimeric antigen receptor). CR3022 scFv is an scFv protein derived from the antibody CR3022.

Experimental results

A Broad-spectrum neutralizing antibody

  • Figure 1: Crystal structure of SARS-CoV receptor binding domain in complex with human antibody CR3022. The structure has been resolved [1] available in PDB with 7JN5 accession number 7JN5.
  • Binding to RBD on the spike protein

    Used for a CAR