For a given protein, the frequency and number of observed hits compared to expected hits is a good indicator of overall immunogenic potential. The ability to compare peptide scores across multiple alleles, a feature unique to the EpiMatrix system, is the key to evaluating the overall immunogenic potential of proteins. The statistical algorithm ClustiMer allows us to screen EpiMatrix results sets and identify putative T cell epitope clusters. We and others have found that potential immunogenicity is not randomly distributed throughout protein sequences but instead tends to “cluster” in immunogenic regions (which are often also immunodominant, see below), facilitating the process of deimmunization. Tools for deimmunization: the EpiMatrix systemĮpiMatrix predicts the binding potential with respect to a panel of nine common Class II super-type alleles, covering the majority of the human population (>90%). The team of scientists at EpiVax are recognized experts in immunogenicity, setting the pace in the deimmunization field with their unique mix of immunoinformatics and immunology. EpiVax has developed and validated a streamlined approach to the deimmunization of therapeutic proteins, coupling advanced computational analysis with high throughput in vitro and in vivo assays. EpiVax’s deimmunization strategy is focused on the identification and elimination of T cell epitopes contained within your candidate sequence.Įstablished leaders, skilled team. DeFT™ is cost effective and highly accurate in establishing and eliminating the immunogenic risks hidden within your protein therapeutic or biologic. The FDA has suggested that protein therapeutic developers assess and manage unwanted immunogenicity. This method of reducing immunogenicity, also known as de-immunization (DeFT), is described in further detail below.ĭeFT: Deimmunization of Functional Therapeutics EpiVax has proprietary technology to identify and introduce Tregitopes (T regulatory epitopes) to reduce immunogenicity and induce tolerance (patented technology/approach). Epitope modifications are easily evaluated in vitro and in vivo prior to release of the protein therapeutic for clinical development. Altered T cell epitopes no longer bind to HLA. This can be accomplished by substituting key amino acids within T cell epitope sequences which abrogate binding to HLA and thereby attenuate epitope potential to trigger a T cell response. Diminishing the immunogenicity of therapeutic proteins without hindering their function will improve clinical outcomes.
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