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2018 Abstracts

Sequencing and Annotation of 12 Bacteriophage Genomes To Aid In Discovering a Treatment For Methicillin-Resistant Staphylococcus aureus

Spencer Bagley, Brigham Young University

Methicillin-Resistant Staphylococcus aureus (MRSA) is a widespread pathogen, present largely in hospital, community, and livestock agriculture settings. MRSA may also adapt into Vancomycin Resistant Staphylococcus aureus (VRSA) which is immune to all common antibiotics, and is largely untreatable. Due to MRSA’s ability to generate biofilms and adapt to antibiotics, a new form of treatment will soon become necessary, especially if VRSA begins to become prevalent in hospital or community settings. The purpose of this research is to sequence and annotate the genomes of 12 bacteriophage found by my lab through community and livestock based MRSA strains, and to use that information to gain understanding of what characteristics make a lysin or a polysacharidase the most effective at destroying MRSA or MRSA biofilms. To do this, I extracted the DNA from a high titer lysate using the phenol chloroform isoamyl alcohol method, and then purified the DNA by running the whole genome DNA through agarose gel electrophoresis, and then eluting the DNA out of the agarose. The genomes are then subjected to library preparation in order to go through Next generation sequencing on an Illumina HiSeq 2500. This phase of the project is still on-going, but once several phage genomes have been sequenced, I will annotate that data, and use it to find patterns as to what creates the most effective lysin proteins, and polysaccharidase proteins. This data can then be used by biochemists to design a drug modeled after the optimum lysin or polysaccharidase, or it can be used to select the phage itself which will be best suited for fomite decontamination or treatment of MRSA infection. Future studies could include intentionally inducing mutation of a phage to grow in a strain of MRSA outside of it’s natural host range, and observing the change in the coding for the lysin protein in the wild type and mutant strains.