Expression and purification of conserved, protective streptococcal antigens for monoclonal antibody isolation

Abstract Streptococcus pyogenesis a significant cause of infectious morbidity and mortality globally. Antibiotics remain the essential treatment for S. pyogenesinfection however, as resistance against long-used antibiotics grows amongst bacterial pathogens antibiotic failure becomes increasingly common in pyogenestreatment, necessity alternative methods escalates. Here, we have selected conserved streptococcal antigens to express Escherichia coliin pursuit isolating protective human monoclonal antibodies (mAbs) infection. We successfully expressed serine proteinase ScpC (180 kDa) which impedes recruitment neutrophils infection site. In addition, produced SpyAD (48.9 kDa), protein that is across emm types shown play an role adhesion division. Both proteins are important virulence factors highly emmtypes, making them promising targets future vaccination therapeutic treatments. Following expression purification antigens, used screen peripheral blood mononuclear cells (PBMCs) antigen specific B-cells via flow cytometry. This work confirms use E. colias system employment such mAb isolation. Supported by NIH Post-Baccalaureate Research Education Program