Tuesday, August 3, 2010: 8:30 AM
Seacliff AB (Hyatt Regency San Francisco)
Tetrahymena thermophila is a common pond water ciliate that has recently been developed as a manufacturing platform and has shown promise for the production of recombinant proteins of interest to the pharmaceutical and biotechnology industries. A number of biological features make Tetrahymena an attractive host for recombinant protein production including the advantages common to all microbial production platforms such as scalability, high cell density growth and fast generation times in a variety of inexpensive complex and synthetic media formulations. Additionally, Tetrahymena is a complex eukaryote encoding some 24,000 genes that contains all the cellular machinery required for proper folding of complex proteins and the addition of post-translational modifications. Tetrahymena cells also contain hundreds-to-thousands of dense core granules, known as mucocysts, that are docked at the plasma membrane and that can be induced to release their contents in the form of an easily harvestable insoluble proteinaceous matrix. Regulated secretion can be induced by the addition of a number of secretogogues to culture medium and is rapid, occurring on the order of seconds. Mucocysts contain a small family of related gene products called granule lattice (Grl) proteins that are among the most abundant proteins in the cell and that form a crystalline lattice within the mucocysts themselves. We have harnessed the potential of the regulated secretion pathway in Tetrahymena to develop an alternative platform for the production of secreted recombinant proteins and have developed a unique vaccine formulation based on a mucocyst-derived immune stimulating matrix.