Presentation Title
Mechanism of Mucin Degradation by Stenotrophomonas maltophilia
Abstract
The central research question being investigated for this project is the mechanism by which mucin is degraded by Stenotrophomonas maltophilia. This is being explored by creating a clean deletion of a particular gene that was highly expressed when S. maltophilia was exposed to mucin as a sole carbon and nitrogen source. The gene of particular interest is smlt4395, which encodes a putative serine protease. To explore this, a successful ligation of the two regions flanking smlt 4395 into a plasmid (pGW67) was performed. Then the plasmid containing these regions was transformed into S17lpir cells and mated with wild-type K279aStenotrophomonas maltophilia. However, at this time the mating has only yielded colonies that retained or reverted back to the wild-type gene, rather than colonies that had replaced the wild type gene with the construct that was created to delete it. More work is being done to try to eliminate the possibility of obtaining wild-type reverts and hopefully once there has been successful creation of the clean deletion, it will be possible to look for a defective mucin growth phenotype and complement the phenotype via reintroduction of the gene of interest. This will ultimately lead to important information regarding the genes that are necessary for S. maltophilia to survive in the human cystic fibrosis lung.
Primary Faculty Mentor Name
Matthew Wargo
Graduate Student Mentors
Lauren Hinkel
Faculty/Staff Collaborators
Lauren Hinkel (Graduate Student Mentor)
Status
Undergraduate
Student College
College of Agriculture and Life Sciences
Program/Major
Biological Sciences, Integrated
Primary Research Category
Biological Sciences
Mechanism of Mucin Degradation by Stenotrophomonas maltophilia
The central research question being investigated for this project is the mechanism by which mucin is degraded by Stenotrophomonas maltophilia. This is being explored by creating a clean deletion of a particular gene that was highly expressed when S. maltophilia was exposed to mucin as a sole carbon and nitrogen source. The gene of particular interest is smlt4395, which encodes a putative serine protease. To explore this, a successful ligation of the two regions flanking smlt 4395 into a plasmid (pGW67) was performed. Then the plasmid containing these regions was transformed into S17lpir cells and mated with wild-type K279aStenotrophomonas maltophilia. However, at this time the mating has only yielded colonies that retained or reverted back to the wild-type gene, rather than colonies that had replaced the wild type gene with the construct that was created to delete it. More work is being done to try to eliminate the possibility of obtaining wild-type reverts and hopefully once there has been successful creation of the clean deletion, it will be possible to look for a defective mucin growth phenotype and complement the phenotype via reintroduction of the gene of interest. This will ultimately lead to important information regarding the genes that are necessary for S. maltophilia to survive in the human cystic fibrosis lung.