Publications by authors named "Paul J Sieminski"
Article Synopsis
- Mycobacterium tuberculosis (Mtb) is a major health threat, especially with rising drug-resistant strains, making it crucial to find new treatments targeting its iron acquisition mechanisms.
- This study investigates the roles of two periplasmic binding proteins, FecB and FecB2, in Mtb's ability to acquire iron, finding that FecB specifically binds to the Mtb siderophore and has a crucial interaction with the iron acquisition system.
- The researchers determined the 3D structures of FecB and FecB2, revealing different binding features, and identified key interactions that suggest FecB is important for both siderophore and heme uptake in Mtb.
(Mtb), the causative agent of tuberculosis, requires iron for survival. In Mtb, MhuD is the cytosolic protein that degrades imported heme. MhuD is distinct, in both sequence and structure, from canonical heme oxygenases (HOs) but homologous with IsdG-type proteins.
View Article and Find Full Text PDFThe highly contagious disease tuberculosis (TB) is caused by the bacterium Mycobacterium tuberculosis (Mtb), which has been evolving drug resistance at an alarming rate. Like all human pathogens, Mtb requires iron for growth and virulence. Consequently, Mtb iron transport is an emerging drug target.
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