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Journal Article

Semisynthesis of functional glycosylphosphatidylinositol-anchored proteins

MPS-Authors
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Roller,  Renée
Daniel Varón Silva, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Malik,  Ankita
Daniel Varón Silva, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Carillo,  Maria Antonietta
Daniel Varón Silva, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Garg,  Monika
Daniel Varón Silva, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Rella,  Antonella
Daniel Varón Silva, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Seeberger,  Peter H.
Peter H. Seeberger, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Varón Silva,  Daniel
Daniel Varón Silva, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

Roller, R., Malik, A., Carillo, M. A., Garg, M., Rella, A., Raulf, M.-K., et al. (2020). Semisynthesis of functional glycosylphosphatidylinositol-anchored proteins. Angewandte Chemie International Edition, 59(29), 12035-12040. doi:10.1002/anie.202002479.


Cite as: https://hdl.handle.net/21.11116/0000-0006-3F29-7
Abstract
Glypiation is a common posttranslational modification of eukaryotic proteins involving the attachment of a glycosylphosphatidylinositol (GPI) glycolipid. GPIs contains a conserved phosphoglycan modified in cell- and tissue-specific manner. GPI complexity suggests roles in biological processes and effects on the attached proteins, but the difficulties to get homogeneous material hinder the studies. Here, we disclose a one-pot intein-mediated ligation (OPL) to obtain GPI-anchored proteins. The strategy allows for glypiation of folded and denatured proteins with a natural linkage to the glycolipid. Using the strategy, glypiated eGFP, Thy1, and the Plasmodium berghei MSP119 were prepared. Glypiation did not alter the structure of eGFP and MSP119 proteins in solution, but it induced a strong pro-inflammatory response in vitro. The strategy provides access to glypiated proteins to elucidate the activity of this modification and for use as vaccine candidates against parasitic infections.