Enhancing the Production of Complex Proteins in Bacteria
Background Numerous therapeutic proteins contain disulfide bonds. However, the production of proteins containing multiple disulfide linkages in genetically engineered bacteria is very inefficient. Bacteria are often not able to produce complex eukaryotic proteins in an active form and in high amounts because the bacterial machinery that catalyzes the isomerization of disulfide bonds is inefficient. As a result, such proteins have to be produced in mammalian cells at a considerably higher expense.Invention Description The invention provides methods for using the Twin Arginine Translocation (TAT) pathway in bacteria to produce heterologous polypeptides that have multiple disulfide bonds. In addition to the composition of novel secretion mechanisms, methods of screening polypeptide libraries produced by secretion through the TAT pathway are also available. This system allows improved production of recombinant proteins with at least one disulfide bond and opens new opportunities for bacterial expression of complex proteins in a properly folded and functional form.
Benefits
Increase in the production of useful and obtainable therapeutic proteins Broadens the array of proteins produced by bacterial systems
Features
Allows production of recombinant proteins with multiple disulfide bonds Can express libraries of recombinant proteins for screening or testing Exploits TAT pathway
IP Status Two foreign patent application filed
UT Researcher George Georgiou, Ph.D., Chemical Engineering, The University of Texas at Austin Lluis Masip, BS, Chemical Engineering, The University of Texas at Austin Matthew DeLisa, Ph.D., Chemical Engineering, The University of Texas at Austin Laura Segatori, BS, Chemical Engineering, The University of Texas at Austin
OTC Contact Information
512-471-2995
Type of Offer: Licensing
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