Difference between revisions of "Part:BBa K5310001:Design"

(→‎Source)
(→‎Design Notes)
 
Line 7: Line 7:
  
 
===Design Notes===
 
===Design Notes===
 +
This part is a domain of myelin oligodendrocyte glycoprotein (MOG). MOG is a protein expressed by oligodendrocytes that contributes to the myelin sheaths that seal the neurons. Due to this localization, it is a primary target antigen involved in immune-mediated demyelination.
 
This MOG domain is designed for experiments that would be proof of concept for Multiple Sclerosis therapeutic or diagnostic projects. Attention to detail is needed when selecting or modifying this sequence, also when selecting antibodies for experimental validation. For example, domain 35-55 has a single amino acid variation between human MOG and murine MOG. It has been shown by Mayer, M. et al, 2014 that MS patient sera had reduced binding or did not recognise the variant MOG domain because of the single point difference in Proline 42. Future improvements to the part could identify single point changes that improved autoantibody binding, for either diagnostic purposes or for the signalling purpose of our chimeric autoantibody receptor.
 
This MOG domain is designed for experiments that would be proof of concept for Multiple Sclerosis therapeutic or diagnostic projects. Attention to detail is needed when selecting or modifying this sequence, also when selecting antibodies for experimental validation. For example, domain 35-55 has a single amino acid variation between human MOG and murine MOG. It has been shown by Mayer, M. et al, 2014 that MS patient sera had reduced binding or did not recognise the variant MOG domain because of the single point difference in Proline 42. Future improvements to the part could identify single point changes that improved autoantibody binding, for either diagnostic purposes or for the signalling purpose of our chimeric autoantibody receptor.
−
 
−
 
  
 
===Source===
 
===Source===

Latest revision as of 12:34, 26 September 2024


MOG immunodominant sequence (aa 35-55)


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]


Design Notes

This part is a domain of myelin oligodendrocyte glycoprotein (MOG). MOG is a protein expressed by oligodendrocytes that contributes to the myelin sheaths that seal the neurons. Due to this localization, it is a primary target antigen involved in immune-mediated demyelination. This MOG domain is designed for experiments that would be proof of concept for Multiple Sclerosis therapeutic or diagnostic projects. Attention to detail is needed when selecting or modifying this sequence, also when selecting antibodies for experimental validation. For example, domain 35-55 has a single amino acid variation between human MOG and murine MOG. It has been shown by Mayer, M. et al, 2014 that MS patient sera had reduced binding or did not recognise the variant MOG domain because of the single point difference in Proline 42. Future improvements to the part could identify single point changes that improved autoantibody binding, for either diagnostic purposes or for the signalling purpose of our chimeric autoantibody receptor.

Source

The sequence of the human myelin oligodendrocyte glycoprotein (MOG) was retrieved from NCBI (https://www.ncbi.nlm.nih.gov/gene/4340). We selected the coding sequence of amino acids 35-55 of the protein and codon-optimised it for expression in human primary cell lines.

References

1. Androutsou Maria-Eleni, Tapeinou Anthi, Vlamis-Gardikas Alexios, Tselios Theodore, Myelin Oligodendrocyte Glycoprotein and Multiple Sclerosis, Medicinal Chemistry; Volume 14, Issue 2, Year 2018, . DOI: 10.2174/1573406413666170906123204

2.Nuzzo, D., & Picone, P. (2021). Multiple Sclerosis: Focus on Extracellular and Artificial Vesicles, Nanoparticles as Potential Therapeutic Approaches. International Journal of Molecular Sciences, 22(16), 8866. https://doi.org/10.3390/ijms22168866

3. Marie C. Mayer, Constanze Breithaupt, Markus Reindl, Kathrin Schanda, Kevin Rostásy, Thomas Berger, Russell C. Dale, Fabienne Brilot, Tomas Olsson, Dieter Jenne, Anne-Katrin Pröbstel, Klaus Dornmair, Hartmut Wekerle, Reinhard Hohlfeld, Brenda Banwell, Amit Bar-Or, Edgar Meinl; Distinction and Temporal Stability of Conformational Epitopes on Myelin Oligodendrocyte Glycoprotein Recognized by Patients with Different Inflammatory Central Nervous System Diseases. J Immunol 1 October 2013; 191 (7): 3594–3604. https://doi.org/10.4049/jimmunol.1301296