AbWzb: A Regulatory Link between PTP Activity and Microbial Vitality

Faculty Mentor

Mark Dela Cerna

Location

Savannah Ballroom

Type of Research

Proposed

Session Format

Poster Presentation

College

College of Science & Mathematics

Department

BioChem, Chem, Phys

Abstract

Wzb is a low molecular weight protein tyrosine phosphatase (LMW-PTP). It is an essential component in the regulation of extracellular polysaccharide (EPS). EPS contributes to the formation of biofilms, which, in turn, enhance the antimicrobial resistance mechanism for certain Gram-negative bacteria. Among these pathogens, A. baumannii (Ab) is a highly opportunistic bacterium that poses a major threat to the medical field. The production of its biofilm plays a key role in its antibiotic resistance to a growing number of standard antibiotic protocols. This has resulted in a surge of healthcare-associated infections (HAIs) due to its persistence on both biotic and abiotic surfaces. The objective of this study is to purify recombinantly expressed AbWzb characterize its structure, and identify inhibitors which can then be developed as antimicrobial compounds. An understanding of its structure will further facilitate the development of inhibitors through structure-based drug design, supporting current computational and in vitro screening in the lab. Purification and structure determination will also improve our understanding of the molecular mechanism of Wzb as well as related LMW-PTP. The disruption of EPS production through small molecule inhibition of Wzb has the potential to impair the development of EPS which can have broader implications to other bacterial PTPs. This project could lead to the development of a more effective antimicrobial strategy that is less susceptible to the development rapid resistance.

Program Description

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Start Date

4-21-2026 1:30 PM

End Date

4-21-2026 3:30 PM

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Apr 21st, 1:30 PM Apr 21st, 3:30 PM

AbWzb: A Regulatory Link between PTP Activity and Microbial Vitality

Savannah Ballroom

Wzb is a low molecular weight protein tyrosine phosphatase (LMW-PTP). It is an essential component in the regulation of extracellular polysaccharide (EPS). EPS contributes to the formation of biofilms, which, in turn, enhance the antimicrobial resistance mechanism for certain Gram-negative bacteria. Among these pathogens, A. baumannii (Ab) is a highly opportunistic bacterium that poses a major threat to the medical field. The production of its biofilm plays a key role in its antibiotic resistance to a growing number of standard antibiotic protocols. This has resulted in a surge of healthcare-associated infections (HAIs) due to its persistence on both biotic and abiotic surfaces. The objective of this study is to purify recombinantly expressed AbWzb characterize its structure, and identify inhibitors which can then be developed as antimicrobial compounds. An understanding of its structure will further facilitate the development of inhibitors through structure-based drug design, supporting current computational and in vitro screening in the lab. Purification and structure determination will also improve our understanding of the molecular mechanism of Wzb as well as related LMW-PTP. The disruption of EPS production through small molecule inhibition of Wzb has the potential to impair the development of EPS which can have broader implications to other bacterial PTPs. This project could lead to the development of a more effective antimicrobial strategy that is less susceptible to the development rapid resistance.