Molybdate-binding periplasmic protein (ModA) (ModA)

ModA is the periplasmic binding protein component of the high-affinity molybdate ABC transporter system (ModABC) in Acinetobacter baumannii. It is responsible for scavenging trace amounts of molybdate from the environment and delivering it to the membrane-bound transport complex, which is essential for the biosynthesis of the molybdenum cofactor (MoCo). This cofactor is required for the function of various molybdoenzymes, such as nitrate reductase and xanthine dehydrogenase, which play critical roles in bacterial metabolism and survival, particularly under the anaerobic or low-oxygen conditions often encountered during host infection. As A. baumannii is a prominent multi-drug resistant (MDR) pathogen associated with severe hospital-acquired infections like pneumonia and sepsis, ModA has emerged as a potential therapeutic target for novel antibacterial strategies. By targeting the nutrient acquisition systems of the bacteria, researchers aim to starve the pathogen of essential trace elements, thereby attenuating its growth and virulence. While no drugs are currently approved specifically for this target, ModA is a subject of interest in structural genomics and anti-virulence drug discovery efforts aimed at overcoming antibiotic resistance.

Other names

Molybdate-binding proteinPeriplasmic molybdate-binding proteinModA subunit of the molybdate ABC transporterMolybdate-binding protein ModA

Inhibition of molybdate uptake, leading to the depletion of essential molybdenum cofactors required for the activity of bacterial molybdoenzymes, thereby impairing metabolic function and reducing virulence.