The peptides of the invention drive the optimal secretion of fused polypeptides out of Mycoplasma cells.
They have multiple potential applications, in particular in the area of synthetic biology and next-generation bacterial-based therapies and vaccination.
Technology:
Synthetic biology enables researchers to engineer biological systems for a myriad of applications including producing biofuels and biosensors, delivering commodity chemical and drugs, and decontaminating soil and water. One particularly exciting application is the possibility of creating bacterial factories that can target diseased tissues, and produce and secrete therapeutics in situ.
By systematically studying the secretome of the small bacteria Mycoplasma pneumoniae through in silico and experimental approaches, scientists at CRG designed a battery of sequences that, when fused to heterologous proteins drive their efficient secretion, and do not interfere with their biological activity. This is a step forward towards the engineering of M. pneumoniae as a delivery system to locally express and secrete active proteins with therapeutic applications in humans and animals. In the shorter term, it will help the engineering of M. pneumoniae as a broad-spectrum animal vaccine.
Advantages:
- Widely applicable with regards to polypeptides to be secreted
- Effective over a wide range of protein folds
- Efficient secretion facilitates polypeptide purification from the medium where necessary
- Potentially compatible with continuous culturing
References:
Prof. Serrano is a known expert in the field of protein design, systems biology and the analysis of protein signaling networks. His group has a known track record in the “omics” study of the small bacteria Mycoplasma pneumoniae, and coordinates the MycoSynVac consortium that aims at engineering the bacteria as a universal chassis for animal vaccination using cutting-edge synthetic biology methodologies.
