Identification of Peptide Ligands from Solid Phase Combinatorial Peptide Libraries that Bind Staphylococcal Enterotoxin B (SEB)

Abstract

Staphylococcal enterotoxin B (SEB) is a primary toxin that causes food poisoning. It also acts as a superantigen that interacts with the major histocompatibility complex class II molecule (MHCII) and T cell receptor (TCR) to activate large amounts of T cells leading to autoimmune diseases. Highly purified SEB is needed in research and can be used as a standard in current detection methods for SEB. Inexpensive, robust ligands with high affinity would be suitable replacements for antibodies in biosensors for the detection of SEB. Affinity adsorption processes using short peptides as ligands show great promise in purifying and detecting proteins in comparison with other methods due to their high stability and low cost. We have found an affinity peptide ligand, YYWLHH, from a solid phase combinatorial peptide library that can separate SEB from E. coli lysate or BSA. Such a peptide ligand is a good candidate to replace antibodies in purification and to develop new biosensors to detect SEB. In addition, the derived peptide ligand might help in understanding the interaction between SEB and MHCII and TCR.