Sialic acid (SIA) is a primary attachment factor for a range of viruses including influenza and cocksackie viruses. SIA is also used in many cellular binding and recognition processes such as in the case of lectins. The goal of this study is to create a detailed characterization of the binding motifs used in SIA binding in order to design cross-reactive neutralizing antibodies and mimetics as well as define an evolutionary rationale as to why the complementary determining region of SIA binding site antibodies is heavily biased towards certain sequences. These insights will help in the future production of designer antibodies to be broadly neutralizing across multiple strains of SIA binding viruses, as well as provide a procedural base for multi-virus neutralizing antibodies. Additionally, Clayton’s project looks to explore the incorporation of non-canonical amino acids as a tool to further probe and optimize the antibody-antigen binding interaction.
Chemical & Physical Biology
PI: James Crowe, M.D.