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PotH is a transmembrane permease protein that constitutes part of the putrescine-specific ATP-binding cassette (ABC) transporter system, commonly referred to as the PotFGHI complex in bacteria such as Escherichia coli [2, 7]. It functions alongside PotI to form the translocation pore, while PotG provides the energy via ATP hydrolysis and PotF serves as the periplasmic substrate-binding protein [2, 15]. Polyamines, including putrescine, are polycationic molecules essential for bacterial survival, playing vital roles in stabilizing nucleic acids, regulating translation, and facilitating biofilm formation [1, 9, 10]. Because polyamines are critical for bacterial virulence and adaptation to host environments, the PotH transporter is a significant target for the development of novel antimicrobial agents [7, 8]. Inhibiting PotH-mediated uptake can lead to intracellular polyamine depletion, which impairs bacterial growth and reduces the ability of pathogens to cause systemic infection [1, 11].
Inhibition of the putrescine-specific ABC transporter system, leading to intracellular polyamine depletion and suppression of bacterial growth and virulence.
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