The Production of Recombinant Immunoglobulin Superfamily Proteins in the Yeast Saccharomyces Cerevisiae

Although scFvs and scTCRs are structurally homologous, they have very distinct expression and stability behaviors. In fact, in order to develop an efficient scTCR production strategy like that developed for scFvs, it was necessary to alter the characteristics of the protein itself to improve its processing and stability characteristics. These properties were improved using a directed evolution approach and yeast surface display. Evolution resulted in a super-scTCR scaffold with optimized secretion, solubility, and stability properties. This scaffold will, for the first time, enable directed evolution of the binding properties of the scTCR for its peptide/MHC ligand. The results described in this thesis illustrate the power of combining genetic, cellular, and protein engineering tools for improving the secretion and stability characteristics of a target protein.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemical Engineering

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Shusta, Eric Victor

Contributors dc:contributor

• Wittrup, K. Dane

• Biology, Molecular

Language dc:language

eng

Identifier

(MiAaPQ)AAI9953140

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/82475