Cyclic-di-GMP-Regulated Motility in Acinetobacter baumannii

Additional Authors

Garret Reynolds, Gabe Smith ; Department of Health Sciences, College of Public Health, ETSU

Abstract

Hospital acquired infections from multi-drug resistant pathogens is an emerging and dangerous issue that threatens the current state of healthcare environments. Acinetobacter baumannii is known for causing opportunistic infections in susceptible patients partially because it is able to survive for extended periods of time on inanimate objects such as hospital medical equipment. Motility mechanisms in A. baumannii permit this colonization and involve a structure known as a type IV pilus. This structure comprises a complex of proteins that work together to produce bacterial attachment/movement. One regulatory factor is a bacterial secondary messenger known as cyclic-di-GMP, and previous research has identified a role in A. baumannii type IV pilus motility for enzymes that produce (diguanylate cyclases) and degrade (phosphodiesterases) cyclic-di-GMP. Using models from other organisms, our current research has focused on using a Bacterial Two-Hybrid system assay to identify cyclic-di-GMP-related proteins that interact with the pilus machinery. So far, we have discovered that protein 1138 encoded in A. baumannii dimerizes with itself, which supports its case for possibly having enzymatic activity since it contains a phosphodiesterase domain, though its ability to bind cyclic-di-GMP has yet to be proven. It also seems that protein 2255, which contains a PilZ superfamily domain, interacts to a degree with the ATPase PilB that is a part of the protein complex involved in the type IV pilus. This suggests the idea that 2255 could function as an adaptor protein that allows other proteins/molecules to regulate Type IV pilus function due to its biding with PilB. In conclusion, further investigation into this signaling mechanism and how it relates to type IV pilus regulation in A. baumannii could provide vital information which could lead to novel treatments towards this dangerous pathogen.

Start Time

16-4-2025 10:00 AM

End Time

16-4-2025 11:00 AM

Room Number

303

Presentation Type

Oral Presentation

Presentation Subtype

Grad/Comp Orals

Presentation Category

Science, Technology and Engineering

Faculty Mentor

Erik Peterson

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Apr 16th, 10:00 AM Apr 16th, 11:00 AM

Cyclic-di-GMP-Regulated Motility in Acinetobacter baumannii

303

Hospital acquired infections from multi-drug resistant pathogens is an emerging and dangerous issue that threatens the current state of healthcare environments. Acinetobacter baumannii is known for causing opportunistic infections in susceptible patients partially because it is able to survive for extended periods of time on inanimate objects such as hospital medical equipment. Motility mechanisms in A. baumannii permit this colonization and involve a structure known as a type IV pilus. This structure comprises a complex of proteins that work together to produce bacterial attachment/movement. One regulatory factor is a bacterial secondary messenger known as cyclic-di-GMP, and previous research has identified a role in A. baumannii type IV pilus motility for enzymes that produce (diguanylate cyclases) and degrade (phosphodiesterases) cyclic-di-GMP. Using models from other organisms, our current research has focused on using a Bacterial Two-Hybrid system assay to identify cyclic-di-GMP-related proteins that interact with the pilus machinery. So far, we have discovered that protein 1138 encoded in A. baumannii dimerizes with itself, which supports its case for possibly having enzymatic activity since it contains a phosphodiesterase domain, though its ability to bind cyclic-di-GMP has yet to be proven. It also seems that protein 2255, which contains a PilZ superfamily domain, interacts to a degree with the ATPase PilB that is a part of the protein complex involved in the type IV pilus. This suggests the idea that 2255 could function as an adaptor protein that allows other proteins/molecules to regulate Type IV pilus function due to its biding with PilB. In conclusion, further investigation into this signaling mechanism and how it relates to type IV pilus regulation in A. baumannii could provide vital information which could lead to novel treatments towards this dangerous pathogen.