Presenter's Name(s)

Morgan I. Howlett, UVMFollow

Primary Faculty Mentor Name

Matthew Wargo

Project Collaborators

Lauren Hinkel (Graduate Student Mentor)

Graduate Student Mentors

Lauren Hinkel

Status

Undergraduate

Student College

College of Agriculture and Life Sciences

Program/Major

Biological Sciences, Integrated

Primary Research Category

Biological Sciences

Presentation Title

Mechanism of Mucin Degradation by Stenotrophomonas maltophilia

Time

3:00 PM

Location

Silver Maple Ballroom - Biological Sciences

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.

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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.