Engineering a Better FLUture with Neuraminidase‐Targeted Monoclonal Antibodies

Abstract

Each year epidemiologists and public officials predict which influenza strain will be most prevalent and design a vaccine to target those specific strains; unfortunately, they are not always accurate. Traditional vaccines cause our bodies to produce antibodies that target two subtypes of the influenza A, that both bind to the surface protein Hemagglutinin (HA). However, HA mutates quickly, leaving the body susceptible to new mutant strains of influenza. Fortunately, another surface protein, Neuraminidase (NA), mutates significantly slower than HA, which would makeaa vaccine that targets NA potentially more effective against a broader spectrum of influenza A and B subtypes. According to Stadlbauer et al., one H3N2 infected donor naturally created monoclonal antibodies (mAbs) against NA that are protective against various strains of influenza A and B. Our research explored the mAb 1G01 in relation to H3N2 NA using PDB 6Q23. We found that 1G01 targets the active site of NA resulting from attraction due to a difference in charges, thereby blocking binding to its substrate necessary for NA to support virus binding and replication. Therefore, implementing properties of anti‐NA antibodies into current influenza vaccines could be used to improve their protectiveness against more strains of the virus, increasing the predictive reliability of current vaccines, and as a step towards a universal influenza vaccine. The Mahtomedi MSOE Center for BioMolecular Modeling MAPS Team used 3‐D modeling and printing technology to examine structure‐function relationships of antibodies in relation to influenza. The visual model will be a valuable tool in developing our story.