Mandy Chu
Pronouns: She/her
Research Mentor(s): Melanie Pearson
Research Mentor School/College/Department: Microbiology and Immunology / Medicine
Program: UROPF
Session: Session 5 (2:40pm – 3:30pm)
Authors:
Abstract
Proteus mirabilis plays a key role in the formation of urinary tract infections, particularly for catheter associated UTIs due to its ability to swarm and form biofilms on catheter surfaces. In particular, P. mirabilis produces mannose-resistant Proteus-like fimbriae (MR/P), the presence of which is needed to cause UTIs. The primary aim of this study is to investigate the unknown MR/P receptor. We predict that the MR/P receptor is hidden without the activity of an unknown enzyme needed to unmask the receptor. One putative sugar cleaving enzyme sialidase is encoded by gene PMI2938. Due to its predicted ability to cleave glycoproteins on Proteus’ cell surface, we hypothesize that the presence of sialidase reveals the MR/P receptor and allows for MR/P fimbrial binding to take place. To test this hypothesis, we mutated the putative sialidase using a targetron approach and utilized biofilm assays. The resulting biofilm assays demonstrated that sialidase has no effect on biofilm formation. There were also no observed changes in swimming or swarming motility. Ultimately, the role of the putative sialidase gene is still unknown. Moving forward, our goal is to pinpoint the function of gene PMI2938 and determine the identity of the MR/P receptor.
