Faculty Mentor
Dr. Eric T. Boder
Department (e.g. History, Chemistry, Finance, etc.)
Chemical and Biomolecular Engineering
College (e.g. College of Engineering, College of Arts & Sciences, Haslam College of Business, etc.)
College of Engineering
Location
Eureca
Year
2020
Abstract
On the surface of immune cells, class II major histocompatibility complex proteins (MHCII) present antigenic peptides for CD4+ T cell recognition, which initiate a variety of antigen-specific immune responses such as antibody response or cytotoxic T cell activation. In people with with auto-immune diseases including but not limited to type 1 diabetes, multiple sclerosis, and rheumatoid arthritis, detrimental immune responses occur after the presentation of antigenic peptides. A single-chain, minimal MHCII (scm-MHCII) has been designed to retain its function as an antigen-presenting protein with a simplified structure that can be easily produced and manipulated in a laboratory by recombinant microbial expression. By applying directed evolution and selection for protein stability quantified using yeast surface display (YSD), we have engineered a mutant library which may contain highly stable mutants capable of functioning as a highly specific inhibitor of T cell-mediated immune responses with the potential to be applied to treating a variety auto-immune diseases.
Included in
Protein Engineering Potential Inhibitor of Detrimental Immune Responses
Eureca
On the surface of immune cells, class II major histocompatibility complex proteins (MHCII) present antigenic peptides for CD4+ T cell recognition, which initiate a variety of antigen-specific immune responses such as antibody response or cytotoxic T cell activation. In people with with auto-immune diseases including but not limited to type 1 diabetes, multiple sclerosis, and rheumatoid arthritis, detrimental immune responses occur after the presentation of antigenic peptides. A single-chain, minimal MHCII (scm-MHCII) has been designed to retain its function as an antigen-presenting protein with a simplified structure that can be easily produced and manipulated in a laboratory by recombinant microbial expression. By applying directed evolution and selection for protein stability quantified using yeast surface display (YSD), we have engineered a mutant library which may contain highly stable mutants capable of functioning as a highly specific inhibitor of T cell-mediated immune responses with the potential to be applied to treating a variety auto-immune diseases.