UstiXpress – A novel cellular platform for protein production; applying unconventional secretion

The production of economically relevant and functionally active proteins remains to be a challenge. A convenient way to harvest heterologously expressed proteins of interest is their isolation from the culture medium. Proteins equipped with a signal sequence are typically secreted through the endoplasmic reticulum (ER)–Golgi secretory pathway – the conventional pathway. Unconventional protein secretion however has significant advantages over the conventional pathway, since proteins subject to the uncon¬ventional type of secretion are not processed by ER or Golgi-dependent post-translational modifications.

UstiXpress uses a fungal host (e.g. Ustilago maydis) as novel cellular platform for protein production. This expression system has the potential for high-level protein expression while avoiding post-translational modifications such as N-glycosylation, etc. Fungi, in particular Ustilago maydis, are very well suited eukaryotic microorganisms for genetic manipulation and modified strains can be generated rapidly. Furthermore, biochemical and proteomic approaches are easily applicable.

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