Research Molecular Biologist
Multi-drug resistant Staphylococcus aureus is a notorious pathogen for both animals and humans. Uses lytic enzymes from viruses (bacteriophage) that infect S. aureus to lyse this pathogen. Uses the lytic enzymes instead of antibiotics because a high level of resistance to antibiotics that is already common in S. aureus. To further ensure that resistant strains do not emerge, he has engineered modular enzymes to harbor three unique lytic activities in one protein such that the pathogen must evade three simultaneous antimicrobial activities, a feat that is rare among all bacteria.
Designed triple-acting fusion enzyme antimicrobials to kill Staphylococcus aureus (and multi-drug resistant versions; MRSA). Fusing three, unique, synergistic peptidoglycan hydrolase lytic domains to create an antimicrobial that is highly refractory to resistance development. This battery of antimicrobial enzymes is broadened by the ability to swap cell wall binding domains between enzymes of different genera, and thereby alter the pathogen specificity of his lytic enzymes.