Iron-regulated surface determinant B protein (IsdB)

Iron-regulated surface determinant B protein (IsdB) is a surface-anchored receptor and virulence factor in Staphylococcus aureus, primarily responsible for capturing iron by binding and internalizing heme from host hemoglobin and related proteins; it also interacts with host extracellular matrix proteins such as vitronectin and von Willebrand factor to mediate bacterial adhesion and invasion[1][2][4][7]. IsdB is expressed under iron-starvation conditions and is vital for bacterial growth and virulence in iron-limited host environments. It contains two NEAT (near-iron transporter) domains which separately bind heme and other host proteins, facilitating both iron acquisition and adherence to host cells[2][1]. Consequently, IsdB is a promising therapeutic target for drugs or compounds designed to inhibit bacterial iron uptake and pathogenesis, and is actively being investigated in research for antimicrobial development[7].

Other names

IsdBiron-regulated surface determinant BStaphylococcal IsdB

Inhibition of IsdB-Hb interaction (blocks iron acquisition, reduces bacterial virulence) Blockade of IsdB-host protein bridging (interferes with adherence/invasion, e.g. via cilengitide interacting with αvβ3 integrins)