By Andrew Cooper

Faculty Mentor: Dr. Swati Agrawal

Abstract

Bacteriophages, viruses that infect bacteria, have the potential to serve as alternatives to antibiotics due to their unique lytic enzymes, known as endolysins. These enzymes can specifically target and rapidly break down bacterial cell walls, making them effective against pathogenic bacteria while reducing harm to beneficial bacteria in human microbiota or the environment in comparison to broad range antibiotics (Abedon et. al., 2011). Research on endolysins demonstrates their potential to target and kill specific bacterial strains, in particular, those derived from Bacillus thuringiensis phages show promise. For example, the phage endolysins LysB4 and LysPBC5, when expressed in recombinant bacteria, demonstrate potent antibacterial properties on a large host of related species, including those outside their typical host range. This research highlights their potential for therapeutic use (Hong, Seokho et al., Lee, Ko On, et al.). We investigated some of the current research on Bacillus endolysin protein activity via genomic and protein analysis to predict the function and structure of two novel Bacillus thuringiensis endolysins proteins. We did this by utilizing both comparative genomics and proteomics to understand how variations in amino acid sequences might theoretically contribute to different host ranges and lytic activities, based on predicted protein folding and previous research. This could ultimately lead to the development of new antimicrobial agents and contribute to a broader understanding of bacteriophage-host interactions.