Relationship between Tregitopes Structure and Binding with Major Histocompatibility Complex Class I
What is it about?
Epitopes of T-cells (tregitopes) are linear sequences of amino acids that present in many animal and human proteins. They demonstrate significant affinity for the antigens of major histocompatibility complex class II (MHC-II). Tregitopes suppress immunological response and could play a significant regulatory role in autoimmune diseases. Tregitopes modulate strongly T-cell response activated by the antigens of the major histocompatibility complex class I (MHC-I). The aim of this study was the attempt to determine the correlation between physicochemical properties and structures of tregitopes and binding strength with MHC-I. 21 amino acid sequences of immunoglobulin G with verified or similar to tregitopes function were selected. The analysis of binding strength with MHC-I was carried out on 41various alleles since MHC-I can be coded by numerous alleles. The first phase of study attempted to find the correlation between the half minimal inhibitory concentration (LogIC50) calculated for MHC-I and physicochemical properties. From all of formulated arithmetic statements, only one allowed to determine significant correlation with LogIC50 with reference to alleles A*02:01 and A*02:06. The correlations for the alleles were linear and sigmoid, respectively (p<0.001). The presence of the repeated amino acids was confirmed in the sequences of the studied compounds. These amino acids are connected with stronger binding or lack of the binding with MHC-I expressed by LogIC50. Presented method can be used in screening of new sequences that have regulatory properties for regulatory T-cells.
Why is it important?
Presented method can be used in screening of new sequences that have regulatory properties for regulatory T-cells. The research article is a valuable addition to the scientific literature due to the presented model that can contribute to search the amino acid sequences potentially responsible for suppression function of proteins that lacks in numerous autoimmune diseases.
The following have contributed to this page: Miss Krystyna Marta Okoniewska